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Conserved domains on  [gi|1610576541|ref|NP_001356464|]
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BDNF/NT-3 growth factors receptor isoform i [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
376-663 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 611.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 376 HIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD 455
Cdd:cd05093     1 HIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd05093    81 PLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd05093   161 IGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1610576541 616 LQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLD 663
Cdd:cd05093   241 LQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKASPVYLD 288
IgI_TrkB_d5 cd05855
Fifth domain (immunoglobulin-like) of Trk receptor TrkB; member of the I-set of Ig ...
130-223 3.01e-65

Fifth domain (immunoglobulin-like) of Trk receptor TrkB; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth domain of Trk receptor, TrkB, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors, which mediate the trophic effects of the neurotrophin Nerve Growth Factor (NGF) family. Trks are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkB shares significant sequence homology and domain organization with TrkA and TrkC. The first three domains are leucine-rich domains while the fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrKB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. In some cell systems NT-3 can activate TrkA and TrkB receptors. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. This group belongs to the I-set of IgSF domains


:

Pssm-ID: 409441  Cd Length: 94  Bit Score: 209.71  E-value: 3.01e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 130 APTITFLESPTSDHHWCIPFTVKGNPKPALQWFYNGAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLIAKN 209
Cdd:cd05855     1 PPTITFLELPTRDHHWCIPFTVKGNPKPTLQWFHEGAILNESEYICTKIHVINNTEYHGCLQLDNPTHLNNGIYTLVAKN 80
                          90
                  ....*....|....
gi 1610576541 210 EYGKDEKQISAHFM 223
Cdd:cd05855    81 EYGEDEKNVSAHFM 94
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
49-127 2.31e-14

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member pfam07679:

Pssm-ID: 472250 [Multi-domain]  Cd Length: 90  Bit Score: 68.82  E-value: 2.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  49 NLTVEEGKSITLSCSVAGDPVPNMYWDVGNlvsKHMNETSHTQ-------GSLRITNISSDDSGKqISCVAENLVGEDQD 121
Cdd:pfam07679   9 DVEVQEGESARFTCTVTGTPDPEVSWFKDG---QPLRSSDRFKvtyeggtYTLTISNVQPDDSGK-YTCVATNSAGEAEA 84

                  ....*.
gi 1610576541 122 SVNLTV 127
Cdd:pfam07679  85 SAELTV 90
LRRCT_2 super family cl48324
Leucine rich repeat C-terminal motif; This entry represents the Leucine Rich Repeat C-terminal ...
1-39 8.81e-09

Leucine rich repeat C-terminal motif; This entry represents the Leucine Rich Repeat C-terminal (LRRCT) capping motif from TRK receptors.


The actual alignment was detected with superfamily member pfam16920:

Pssm-ID: 465313  Cd Length: 45  Bit Score: 51.49  E-value: 8.81e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1610576541   1 MWIKTLQEAKSS-PDTQDLYCLNESSKnIPLANLQIPNCG 39
Cdd:pfam16920   7 RWLQLWQEEGLAgLGTQQLYCLNDGSK-IPLQSMNIPNCG 45
 
Name Accession Description Interval E-value
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
376-663 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 611.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 376 HIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD 455
Cdd:cd05093     1 HIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd05093    81 PLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd05093   161 IGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1610576541 616 LQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLD 663
Cdd:cd05093   241 LQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKASPVYLD 288
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
382-651 1.18e-139

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 408.42  E-value: 1.18e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKRELGEGAFGKVFLAEcYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGT-LKGEGENTKIKVAVKTLKEgADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGPdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKR------------KLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPR 620
Cdd:pfam07714 148 LSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPE 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1610576541 621 TCPQEVYELMLGCWQREPHMRKNIKGIHTLL 651
Cdd:pfam07714 228 NCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
382-651 5.06e-136

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 398.85  E-value: 5.06e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  382 IVLKRELGEGAFGKVFLAEcYNLCPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGT-LKGKGDGKEVEVAVKTLKeDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  461 FEYMKHGDLNKFLRAHGPdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:smart00221  80 MEYMPGGDLLDYLRKNRP-----------KELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  541 MSRDVYSTDYYRVGgHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPR 620
Cdd:smart00221 149 LSRDLYDDDYYKVK-GGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPP 227
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1610576541  621 TCPQEVYELMLGCWQREPHMRKNIKGIHTLL 651
Cdd:smart00221 228 NCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
IgI_TrkB_d5 cd05855
Fifth domain (immunoglobulin-like) of Trk receptor TrkB; member of the I-set of Ig ...
130-223 3.01e-65

Fifth domain (immunoglobulin-like) of Trk receptor TrkB; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth domain of Trk receptor, TrkB, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors, which mediate the trophic effects of the neurotrophin Nerve Growth Factor (NGF) family. Trks are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkB shares significant sequence homology and domain organization with TrkA and TrkC. The first three domains are leucine-rich domains while the fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrKB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. In some cell systems NT-3 can activate TrkA and TrkB receptors. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. This group belongs to the I-set of IgSF domains


Pssm-ID: 409441  Cd Length: 94  Bit Score: 209.71  E-value: 3.01e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 130 APTITFLESPTSDHHWCIPFTVKGNPKPALQWFYNGAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLIAKN 209
Cdd:cd05855     1 PPTITFLELPTRDHHWCIPFTVKGNPKPTLQWFHEGAILNESEYICTKIHVINNTEYHGCLQLDNPTHLNNGIYTLVAKN 80
                          90
                  ....*....|....
gi 1610576541 210 EYGKDEKQISAHFM 223
Cdd:cd05855    81 EYGEDEKNVSAHFM 94
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
383-641 1.79e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 163.26  E-value: 1.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKD---ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:COG0515    10 RILRLLGRGGMGVVYLAR-----DLRLGRPVALKVLRPelaADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:COG0515    85 VMEYVEGESLADLLRRRGP-------------LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMSRDVYSTDYYRVgGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVL--- 616
Cdd:COG0515   152 GIARALGGATLTQT-GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPpps 229
                         250       260
                  ....*....|....*....|....*
gi 1610576541 617 QRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:COG0515   230 ELRPDLPPALDAIVLRALAKDPEER 254
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
388-598 1.13e-20

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 96.02  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcpeqDKIL---VAVKTLKD--ASD-NARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:NF033483   15 IGRGGMAEVYLAK--------DTRLdrdVAVKVLRPdlARDpEFVARFRREAQSAASLSHPNIVSVYDVGEDGGIPYIVM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:NF033483   87 EYVDGRTLKDYIREHGP-------------LSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGI 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 542 SRDVYSTdyyrvgghTMLP-------IRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:NF033483  154 ARALSST--------TMTQtnsvlgtVHYLSPEQARGGTVDARSDIYSLGIVLYEMLT-GRPPF 208
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
388-592 9.22e-19

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 87.89  E-value: 9.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLcpeqDKIlVAVKTLK--DASDNARKDFH------------REAELLTNLQHEHIVKFYGVCVE 453
Cdd:PTZ00024   17 LGEGTYGKVEKAYDTLT----GKI-VAIKKVKiiEISNDVTKDRQlvgmcgihfttlRELKIMNEIKHENIMGLVDVYVE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMkHGDLNKFLrahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL 533
Cdd:PTZ00024   92 GDFINLVMDIM-ASDLKKVV-------------DRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGI 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 534 VKIGDFGMSR----DVYSTDYYRVggHTMLPIRWMPPE--SIMYR---------KFTTESDVWSLGVVLWEIFT 592
Cdd:PTZ00024  158 CKIADFGLARrygyPPYSDTLSKD--ETMQRREEMTSKvvTLWYRapellmgaeKYHFAVDMWSVGCIFAELLT 229
I-set pfam07679
Immunoglobulin I-set domain;
49-127 2.31e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.82  E-value: 2.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  49 NLTVEEGKSITLSCSVAGDPVPNMYWDVGNlvsKHMNETSHTQ-------GSLRITNISSDDSGKqISCVAENLVGEDQD 121
Cdd:pfam07679   9 DVEVQEGESARFTCTVTGTPDPEVSWFKDG---QPLRSSDRFKvtyeggtYTLTISNVQPDDSGK-YTCVATNSAGEAEA 84

                  ....*.
gi 1610576541 122 SVNLTV 127
Cdd:pfam07679  85 SAELTV 90
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
48-127 4.58e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.92  E-value: 4.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541   48 PNLTVEEGKSITLSCSVAGDPVPNMYW--DVGNLVSKHMNET---SHTQGSLRITNISSDDSGkQISCVAENLVGEDQDS 122
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWykQGGKLLAESGRFSvsrSGSTSTLTISNVTPEDSG-TYTCAATNSSGSASSG 80

                   ....*
gi 1610576541  123 VNLTV 127
Cdd:smart00410  81 TTLTV 85
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
49-127 1.68e-10

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 57.79  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  49 NLTVEEGKSITLSCSVAGDPVPNMYW--DVGNL-VSKHMNETSHtqgSLRITNISSDDSGKQIsCVAENLVGEDQDSVNL 125
Cdd:cd05725     6 NQVVLVDDSAEFQCEVGGDPVPTVRWrkEDGELpKGRYEILDDH---SLKIRKVTAGDMGSYT-CVAENMVGKIEASATL 81

                  ..
gi 1610576541 126 TV 127
Cdd:cd05725    82 TV 83
LRRCT_2 pfam16920
Leucine rich repeat C-terminal motif; This entry represents the Leucine Rich Repeat C-terminal ...
1-39 8.81e-09

Leucine rich repeat C-terminal motif; This entry represents the Leucine Rich Repeat C-terminal (LRRCT) capping motif from TRK receptors.


Pssm-ID: 465313  Cd Length: 45  Bit Score: 51.49  E-value: 8.81e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1610576541   1 MWIKTLQEAKSS-PDTQDLYCLNESSKnIPLANLQIPNCG 39
Cdd:pfam16920   7 RWLQLWQEEGLAgLGTQQLYCLNDGSK-IPLQSMNIPNCG 45
I-set pfam07679
Immunoglobulin I-set domain;
150-216 8.24e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 47.25  E-value: 8.24e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 150 TVKGNPKPALQWFYNGAILNESKyictKIHVTNhTEYHGCLQLDNPTHMNNGDYTLIAKNEYGKDEK 216
Cdd:pfam07679  23 TVTGTPDPEVSWFKDGQPLRSSD----RFKVTY-EGGTYTLTISNVQPDDSGKYTCVATNSAGEAEA 84
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
147-218 6.60e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 36.33  E-value: 6.60e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541  147 IPFTVKGNPKPALQWFYNGAILNESKyicTKIHVTNHTeYHGCLQLDNPTHMNNGDYTLIAKNEYGKDEKQI 218
Cdd:smart00410  14 LSCEASGSPPPEVTWYKQGGKLLAES---GRFSVSRSG-STSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81
 
Name Accession Description Interval E-value
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
376-663 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 611.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 376 HIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD 455
Cdd:cd05093     1 HIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd05093    81 PLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd05093   161 IGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1610576541 616 LQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLD 663
Cdd:cd05093   241 LQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKASPVYLD 288
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
376-653 0e+00

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 597.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 376 HIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDN-ARKDFHREAELLTNLQHEHIVKFYGVCVEG 454
Cdd:cd05049     1 HIKRDTIVLKRELGEGAFGKVFLGECYNLEPEQDKMLVAVKTLKDASSPdARKDFEREAELLTNLQHENIVKFYGVCTEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKHGDLNKFLRAHGPDAVLMA-EGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL 533
Cdd:cd05049    81 DPLLMVFEYMEHGDLNKFLRSHGPDAAFLAsEDSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 534 VKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQG 613
Cdd:cd05049   161 VKIGDFGMSRDIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEVIECITQG 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1610576541 614 RVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQN 653
Cdd:cd05049   241 RLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQE 280
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
376-652 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 551.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 376 HIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD 455
Cdd:cd05092     1 HIKRRDIVLKWELGEGAFGKVFLAECHNLLPEQDKMLVAVKALKEATESARQDFQREAELLTVLQHQHIVRFYGVCTEGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGN--PPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL 533
Cdd:cd05092    81 PLIMVFEYMRHGDLNRFLRSHGPDAKILDGGEgqAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 534 VKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQG 613
Cdd:cd05092   161 VKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAIECITQG 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1610576541 614 RVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQ 652
Cdd:cd05092   241 RELERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHSRLQ 279
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
376-659 0e+00

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 517.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 376 HIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD 455
Cdd:cd05094     1 HIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNP---PTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 532
Cdd:cd05094    81 PLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPrqaKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQ 612
Cdd:cd05094   161 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQ 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1610576541 613 GRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASP 659
Cdd:cd05094   241 GRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHALGKATP 287
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
382-651 1.18e-139

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 408.42  E-value: 1.18e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKRELGEGAFGKVFLAEcYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGT-LKGEGENTKIKVAVKTLKEgADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGPdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKR------------KLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPR 620
Cdd:pfam07714 148 LSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPE 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1610576541 621 TCPQEVYELMLGCWQREPHMRKNIKGIHTLL 651
Cdd:pfam07714 228 NCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
382-651 5.06e-136

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 398.85  E-value: 5.06e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  382 IVLKRELGEGAFGKVFLAEcYNLCPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGT-LKGKGDGKEVEVAVKTLKeDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  461 FEYMKHGDLNKFLRAHGPdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:smart00221  80 MEYMPGGDLLDYLRKNRP-----------KELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  541 MSRDVYSTDYYRVGgHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPR 620
Cdd:smart00221 149 LSRDLYDDDYYKVK-GGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPP 227
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1610576541  621 TCPQEVYELMLGCWQREPHMRKNIKGIHTLL 651
Cdd:smart00221 228 NCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
382-651 1.92e-135

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 397.29  E-value: 1.92e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  382 IVLKRELGEGAFGKVFLAEcYNLCPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGK-LKGKGGKKKVEVAVKTLKeDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  461 FEYMKHGDLNKFLRAHGPdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:smart00219  80 MEYMEGGDLLSYLRKNRP------------KLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  541 MSRDVYSTDYYRVGgHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPR 620
Cdd:smart00219 148 LSRDLYDDDYYRKR-GGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPP 226
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1610576541  621 TCPQEVYELMLGCWQREPHMRKNIKGIHTLL 651
Cdd:smart00219 227 NCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
386-652 9.01e-135

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 395.75  E-value: 9.01e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNLCPEqdKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd00192     1 KKLGEGAFGEVYKGKLKGGDGK--TVDVAVKTLKeDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHGPdavlMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd00192    79 EGGDLLDFLRKSRP----VFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 VYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQ 624
Cdd:cd00192   155 IYDDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENCPD 234
                         250       260
                  ....*....|....*....|....*...
gi 1610576541 625 EVYELMLGCWQREPHMRKNIKGIHTLLQ 652
Cdd:cd00192   235 ELYELMLSCWQLDPEDRPTFSELVERLE 262
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
376-654 2.90e-127

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 377.49  E-value: 2.90e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 376 HIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEG 454
Cdd:cd05048     1 EIPLSAVRFLEELGEGAFGKVYKGELLGPSSEESAISVAIKTLKEnASPKTQQDFRREAELMSDLQHPNIVCLLGVCTKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTE---LTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGEN 531
Cdd:cd05048    81 QPQCMLFEYMAHGDLHEFLVRHSPHSDVGVSSDDDGTassLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 532 LLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECIT 611
Cdd:cd05048   161 LTVKISDFGLSRDIYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQEVIEMIR 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1610576541 612 QGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05048   241 SRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEIHTRLRTW 283
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
379-652 1.94e-121

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 363.00  E-value: 1.94e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPL 457
Cdd:cd05050     4 RNNIEYVRDIGQGAFGRVFQARAPGLLPYEPFTMVAVKMLKEeASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLNKFLRAHGP---------DAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV 528
Cdd:cd05050    84 CLLFEYMAYGDLNEFLRHRSPraqcslshsTSSARKCGLNPLPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 529 GENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIE 608
Cdd:cd05050   164 GENMVVKIADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGMAHEEVIY 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1610576541 609 CITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQ 652
Cdd:cd05050   244 YVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINRILQ 287
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
379-652 2.21e-117

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 352.80  E-value: 2.21e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECYNLC-----------PEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVK 446
Cdd:cd05051     4 REKLEFVEKLGEGQFGEVHLCEANGLSdltsddfigndNKDEPVLVAVKMLRpDASKNAREDFLKEVKIMSQLKDPNIVR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 447 FYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNC 526
Cdd:cd05051    84 LLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGASATNSKT-LSYGTLLYMATQIASGMKYLESLNFVHRDLATRNC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 527 LVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGK-QPWYQLSNNE 605
Cdd:cd05051   163 LVGPNYTIKIADFGMSRNLYSGDYYRIEGRAVLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCKeQPYEHLTDEQ 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 606 VIECITQG-------RVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQ 652
Cdd:cd05051   243 VIENAGEFfrddgmeVYLSRPPNCPKEIYELMLECWRRDEEDRPTFREIHLFLQ 296
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
377-653 6.60e-109

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 330.07  E-value: 6.60e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD 455
Cdd:cd05032     3 LPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETRVAIKTVNEnASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTGQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTeltQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd05032    83 PTLVVMELMAKGDLKSYLRSRRPEAENNPGLGPPT---LQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd05032   160 IGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVIDGGH 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1610576541 616 LQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQN 653
Cdd:cd05032   240 LDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLKD 277
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
388-653 1.12e-95

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 295.48  E-value: 1.12e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYN-LCPEQDKILVAVKTL-KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd05044     3 LGSGAFGEVFEGTAKDiLGDGSGETKVAVKTLrKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHGPDAVlmaegnPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGEN----LLVKIGDFGM 541
Cdd:cd05044    83 GGDLLSYLRAARPTAF------TPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKdyreRVVKIGDFGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRT 621
Cdd:cd05044   157 ARDIYKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLDQPDN 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1610576541 622 CPQEVYELMLGCWQREPHMRKNIKGIHTLLQN 653
Cdd:cd05044   237 CPDDLYELMLRCWSTDPEERPSFARILEQLQN 268
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
379-652 1.11e-94

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 294.21  E-value: 1.11e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECYNL-----------CPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVK 446
Cdd:cd05095     4 RKLLTFKEKLGEGQFGEVHLCEAEGMekfmdkdfaleVSENQPVLVAVKMLRaDANKNARNDFLKEIKIMSRLKDPNIIR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 447 FYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNC 526
Cdd:cd05095    84 LLAVCITDDPLCMITEYMENGDLNQFLSRQQPEGQLALPSNALT-VSYSDLRFMAAQIASGMKYLSSLNFVHRDLATRNC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 527 LVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGK-QPWYQLSNNE 605
Cdd:cd05095   163 LVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFCReQPYSQLSDEQ 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 606 VIECI-----TQGR--VLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQ 652
Cdd:cd05095   243 VIENTgeffrDQGRqtYLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLLQ 296
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
379-651 4.01e-94

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 292.99  E-value: 4.01e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECYNlcPEQ-------------DKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHI 444
Cdd:cd05096     4 RGHLLFKEKLGEGQFGEVHLCEVVN--PQDlptlqfpfnvrkgRPLLVAVKILRpDANKNARNDFLKEVKILSRLKDPNI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 445 VKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAH------GPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVH 518
Cdd:cd05096    82 IRLLGVCVDEDPLCMITEYMENGDLNQFLSSHhlddkeENGNDAVPPAHCLPAISYSSLLHVALQIASGMKYLSSLNFVH 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 519 RDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGK-QP 597
Cdd:cd05096   162 RDLATRNCLVGENLTIKIADFGMSRNLYAGDYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLCKeQP 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 598 WYQLSNNEVIECI-----TQGR--VLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLL 651
Cdd:cd05096   242 YGELTDEQVIENAgeffrDQGRqvYLFRPPPCPQGLYELMLQCWSRDCRERPSFSDIHAFL 302
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
379-651 2.21e-92

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 288.03  E-value: 2.21e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECYNL-------CPEQDK--ILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFY 448
Cdd:cd05097     4 RQQLRLKEKLGEGQFGEVHLCEAEGLaeflgegAPEFDGqpVLVAVKMLRaDVTKTARNDFLKEIKIMSRLKNPNIIRLL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 449 GVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV 528
Cdd:cd05097    84 GVCVSDDPLCMITEYMENGDLNQFLSQREIESTFTHANNIPS-VSIANLLYMAVQIASGMKYLASLNFVHRDLATRNCLV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 529 GENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGK-QPWYQLSNNEVI 607
Cdd:cd05097   163 GNHYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLCKeQPYSLLSDEQVI 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 608 ECI-----TQGR--VLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLL 651
Cdd:cd05097   243 ENTgeffrNQGRqiYLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKIHHFL 293
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
375-654 2.48e-92

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 287.36  E-value: 2.48e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 375 QHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTL-KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVE 453
Cdd:cd05036     1 KEVPRKNLTLIRALGQGAFGEVYEGTVSGMPGDPSPLQVAVKTLpELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMKHGDLNKFLRAHGPDAvlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV---GE 530
Cdd:cd05036    81 RLPRFILLELMAGGDLKSFLRENRPRP------EQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLtckGP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 531 NLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECI 610
Cdd:cd05036   155 GRVAKIGDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFV 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1610576541 611 TQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKgihTLLQNL 654
Cdd:cd05036   235 TSGGRMDPPKNCPGPVYRIMTQCWQHIPEDRPNFS---TILERL 275
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
387-652 3.70e-90

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 281.90  E-value: 3.70e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAECYnlCPEQDKI-LVAVKTLKDASDNAR-KDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd05090    12 ELGECAFGKIYKGHLY--LPGMDHAqLVAIKTLKDYNNPQQwNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHGPDAVLMA----EGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd05090    90 NQGDLHEFLIMRSPHSDVGCssdeDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPR 620
Cdd:cd05090   170 LSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPCSE 249
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1610576541 621 TCPQEVYELMLGCWQREPHMRKNIKGIHTLLQ 652
Cdd:cd05090   250 DCPPRMYSLMTECWQEIPSRRPRFKDIHARLR 281
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
387-652 8.66e-89

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 278.44  E-value: 8.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNA-RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd05091    13 ELGEDRFGKVYKGHLFGTAPGEQTQAVAIKTLKDKAEGPlREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSYCS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHGPDAVLMAEGNPPT---ELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd05091    93 HGDLHEFLVMRSPHSDVGSTDDDKTvksTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGLF 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 RDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTC 622
Cdd:cd05091   173 REVYAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVIEMIRNRQVLPCPDDC 252
                         250       260       270
                  ....*....|....*....|....*....|
gi 1610576541 623 PQEVYELMLGCWQREPHMRKNIKGIHTLLQ 652
Cdd:cd05091   253 PAWVYTLMLECWNEFPSRRPRFKDIHSRLR 282
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
377-653 1.35e-85

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 270.30  E-value: 1.35e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD 455
Cdd:cd05061     3 VSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNEsASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLRAHGPDAVlMAEGNPPTELtqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd05061    83 PTLVVMELMAHGDLKSYLRSLRPEAE-NNPGRPPPTL--QEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd05061   160 IGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGY 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1610576541 616 LQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQN 653
Cdd:cd05061   240 LDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLKD 277
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
381-654 2.21e-85

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 268.86  E-value: 2.21e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAeCYNLcPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd05033     5 YVTIEKVIGGGEFGEVCSG-SLKL-PGKKEIDVAIKTLKSgYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHgpdavlmaEGnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd05033    83 VTEYMENGSLDKFLREN--------DG----KFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMSRDVYSTD--YYRVGGHtmLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQ 617
Cdd:cd05033   151 GLSRRLEDSEatYTTKGGK--IPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGYRLP 228
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1610576541 618 RPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05033   229 PPMDCPSALYQLMLDCWQKDRNERPTFSQIVSTLDKM 265
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
376-641 2.99e-84

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 266.25  E-value: 2.99e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 376 HIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASD-NARKDFHREAELLTNLQHEHIVKFYGVCVEG 454
Cdd:cd05046     1 AFPRSNLQEITTLGRGEFGEVFLAKAKGIEEEGGETLVLVKALQKTKDeNLQSEFRRELDMFRKLSHKNVVRLLGLCREA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKHGDLNKFLRAHGPDAvlmaEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 534
Cdd:cd05046    81 EPHYMILEYTDLGDLKQFLRATKSKD----EKLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGMSRDVYSTDYYRVgGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGR 614
Cdd:cd05046   157 KVSLLSLSKDVYNSEYYKL-RNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLNRLQAGK 235
                         250       260
                  ....*....|....*....|....*...
gi 1610576541 615 V-LQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05046   236 LeLPVPEGCPSRLYKLMTRCWAVNPKDR 263
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
386-655 1.99e-83

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 263.54  E-value: 1.99e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNlcpeqdKILVAVKTLKDASDNaRKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd05059    10 KELGSGQFGVVHLGKWRG------KIDVAIKMIKEGSMS-EDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDV 545
Cdd:cd05059    83 NGCLLNYLRER------------RGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 546 YSTDYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQE 625
Cdd:cd05059   151 LDDEYTSSVG-TKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGYRLYRPHLAPTE 229
                         250       260       270
                  ....*....|....*....|....*....|
gi 1610576541 626 VYELMLGCWQREPHMRKNIKgihTLLQNLA 655
Cdd:cd05059   230 VYTIMYSCWHEKPEERPTFK---ILLSQLT 256
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
377-647 4.53e-83

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 263.89  E-value: 4.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDK-ILVAVKTLK-DASDNARKDFHREAELLTNL-QHEHIVKFYGVCVE 453
Cdd:cd05053     9 LPRDRLTLGKPLGEGAFGQVVKAEAVGLDNKPNEvVTVAVKMLKdDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMKHGDLNKFLRAH---GPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGE 530
Cdd:cd05053    89 DGPLYVVVEYASKGNLREFLRARrppGEEASPDDPRVPEEQLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 531 NLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECI 610
Cdd:cd05053   169 DNVMKIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLL 248
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1610576541 611 TQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd05053   249 KEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQL 285
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
386-641 1.78e-81

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 257.98  E-value: 1.78e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNLCPeqdkilVAVKTLKDASDNArKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd05034     1 KKLGAGQFGEVWMGVWNGTTK------VAVKTLKPGTMSP-EAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAhgpdavlmAEGNpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRdV 545
Cdd:cd05034    74 KGSLLDYLRT--------GEGR---ALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLAR-L 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 546 YSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQE 625
Cdd:cd05034   142 IEDDEYTAREGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPKPPGCPDE 221
                         250
                  ....*....|....*.
gi 1610576541 626 VYELMLGCWQREPHMR 641
Cdd:cd05034   222 LYDIMLQCWKKEPEER 237
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
377-641 1.47e-80

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 256.18  E-value: 1.47e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNLCPeqdkilVAVKTLKDASDNArKDFHREAELLTNLQHEHIVKFYGVCVEGDP 456
Cdd:cd05068     5 IDRKSLKLLRKLGSGQFGEVWEGLWNNTTP------VAVKTLKPGTMDP-EDFLREAQIMKKLRHPKLIQLYAVCTLEEP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLRAHGpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd05068    78 IYIITELMKHGSLLEYLQGKG------------RSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSRDVYSTDYY--RVGghTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGR 614
Cdd:cd05068   146 ADFGLARVIKVEDEYeaREG--AKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVERGY 223
                         250       260
                  ....*....|....*....|....*..
gi 1610576541 615 VLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05068   224 RMPCPPNCPPQLYDIMLECWKADPMER 250
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
384-653 2.78e-78

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 250.04  E-value: 2.78e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECYNLCPeqdkilVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd05148    10 LERKLGSGYFGEVWEGLWKNRVR------VAIKILKSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAhgpdavlmAEGNpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd05148    84 MEKGSLLAFLRS--------PEGQ---VLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLAR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 ----DVYSTDyyrvggHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRP 619
Cdd:cd05148   153 likeDVYLSS------DKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAGYRMPCP 226
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1610576541 620 RTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQN 653
Cdd:cd05148   227 AKCPQEIYKIMLECWAAEPEDRPSFKALREELDN 260
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
377-641 1.98e-77

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 248.41  E-value: 1.98e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD 455
Cdd:cd05062     3 VAREKITMSRELGQGSFGMVYEGIAKGVVKDEPETRVAIKTVNEaASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLRAHGPDAvlmaEGNPPTEL-TQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 534
Cdd:cd05062    83 PTLVIMELMTRGDLKSYLRSLRPEM----ENNPVQAPpSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGR 614
Cdd:cd05062   159 KIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGG 238
                         250       260
                  ....*....|....*....|....*..
gi 1610576541 615 VLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05062   239 LLDKPDNCPDMLFELMRMCWQYNPKMR 265
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
377-651 7.25e-77

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 246.56  E-value: 7.25e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNlcPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEgD 455
Cdd:cd05056     3 IQREDITLGRCIGEGQFGDVYQGVYMS--PENEKIAVAVKTCKnCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITE-N 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd05056    80 PVWIVMELAPLGELRSYLQVN------------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSRDVYSTDYYRvGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd05056   148 LGDFGLSRYMEDESYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGER 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1610576541 616 LQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLL 651
Cdd:cd05056   227 LPMPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQL 262
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
386-641 7.42e-77

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 246.11  E-value: 7.42e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAecYNLCPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCvEGDPLIMVFEYM 464
Cdd:cd05060     1 KELGHGNFGSVRKG--VYLMKSGKEVEVAVKTLKqEHEKAGKKEFLREASVMAQLDHPCIVRLIGVC-KGEPLMLVMELA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd05060    78 PLGPLLKYLKKRR-------------EIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 V-YSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCP 623
Cdd:cd05060   145 LgAGSDYYRATTAGRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLPRPEECP 224
                         250
                  ....*....|....*...
gi 1610576541 624 QEVYELMLGCWQREPHMR 641
Cdd:cd05060   225 QEIYSIMLSCWKYRPEDR 242
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
386-652 1.09e-75

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 243.12  E-value: 1.09e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECynlcpEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd05041     1 EKIGRGNFGDVYRGVL-----KPDNTEVAVKTCReTLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHGPdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd05041    76 PGGSLLTFLRKKGA------------RLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSRE 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 VYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQ 624
Cdd:cd05041   144 EEDGEYTVSDGLKQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPELCPE 223
                         250       260
                  ....*....|....*....|....*...
gi 1610576541 625 EVYELMLGCWQREPHMRKNIKGIHTLLQ 652
Cdd:cd05041   224 AVYRLMLQCWAYDPENRPSFSEIYNELQ 251
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
387-641 2.34e-75

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 242.25  E-value: 2.34e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAECYNlcPEQDKILVAVKTLKD---ASDNARKDFHREAELLTNLQHEHIVKFYGVcVEGDPLIMVFEY 463
Cdd:cd05040     2 KLGDGSFGVVRRGEWTT--PSGKVIQVAVKCLKSdvlSQPNAMDDFLKEVNAMHSLDHPNLIRLYGV-VLSSPLMMVTEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGPdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd05040    79 APLGSLLDRLRKDQG------------HFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVYST-DYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQ-GRVLQRPRT 621
Cdd:cd05040   147 ALPQNeDHYVMQEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKIDKeGERLERPDD 226
                         250       260
                  ....*....|....*....|
gi 1610576541 622 CPQEVYELMLGCWQREPHMR 641
Cdd:cd05040   227 CPQDIYNVMLQCWAHKPADR 246
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
377-654 1.61e-73

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 237.63  E-value: 1.61e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNlcpeqDKilVAVKTLKDaSDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDP 456
Cdd:cd05039     3 INKKDLKLGELIGKGEFGDVMLGDYRG-----QK--VAVKCLKD-DSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLRAHGPDAVlmaegnpptelTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd05039    75 LYIVTEYMAKGSLVDYLRSRGRAVI-----------TRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKV 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSRDV-YSTDyyrvGGHtmLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd05039   144 SDFGLAKEAsSNQD----GGK--LPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPHVEKGYR 217
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1610576541 616 LQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05039   218 MEAPEGCPPEVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
378-641 2.31e-73

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 238.05  E-value: 2.31e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 378 KRHnIVLKRELGEGAFGKVFLAeCYNlcPEQDKI--LVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVE- 453
Cdd:cd05038     3 ERH-LKFIKQLGEGHFGSVELC-RYD--PLGDNTgeQVAVKSLQpSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESp 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 -GDPLIMVFEYMKHGDLNKFLRAHGPdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 532
Cdd:cd05038    79 gRRSLRLIMEYLPSGSLRDYLQRHRD------------QIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESED 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFGMSRDV-YSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGK-------QPWYQLSNN 604
Cdd:cd05038   147 LVKISDFGLAKVLpEDKEYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDpsqsppaLFLRMIGIA 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1610576541 605 E-------VIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05038   227 QgqmivtrLLELLKSGERLPRPPSCPDEVYDLMKECWEYEPQDR 270
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
379-664 6.42e-73

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 237.94  E-value: 6.42e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECYNLCPE-QDK-ILVAVKTLKD-ASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEG 454
Cdd:cd05099    11 RDRLVLGKPLGEGCFGQVVRAEAYGIDKSrPDQtVTVAVKMLKDnATDKDLADLISEMELMKLIgKHKNIINLLGVCTQE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKHGDLNKFLRAH---GPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGEN 531
Cdd:cd05099    91 GPLYVIVEYAAKGNLREFLRARrppGPDYTFDITKVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTED 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 532 LLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECIT 611
Cdd:cd05099   171 NVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGIPVEELFKLLR 250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 612 QGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKG-IHTLLQNLAKASPVYLDI 664
Cdd:cd05099   251 EGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQlVEALDKVLAAVSEEYLDL 304
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
377-654 1.21e-72

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 235.39  E-value: 1.21e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLA--ECYNLcpeqdkiLVAVKTLKDASdNARKDFHREAELLTNLQHEHIVKFYGVCVEG 454
Cdd:cd05052     3 IERTDITMKHKLGGGQYGEVYEGvwKKYNL-------TVAVKTLKEDT-MEVEEFLKEAAVMKEIKHPNLVQLLGVCTRE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKHGDLNKFLRAhgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 534
Cdd:cd05052    75 PPFYIITEFMPYGNLLDYLRE-----------CNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLV 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGMSRdVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGR 614
Cdd:cd05052   144 KVADFGLSR-LMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKGY 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1610576541 615 VLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05052   223 RMERPEGCPPKVYELMRACWQWNPSDRPSFAEIHQALETM 262
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
352-655 3.98e-71

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 232.76  E-value: 3.98e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 352 IPVIENPQYFGITNSQLkPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKD-FH 430
Cdd:cd05055     8 IESINGNEYVYIDPTQL-PYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAYGLSKSDAVMKVAVKMLKPTAHSSEREaLM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 431 REAELLTNL-QHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAhgpdavlmaegNPPTELTQSQMLHIAQQIAAGMV 509
Cdd:cd05055    87 SELKIMSHLgNHENIVNLLGACTIGGPILVITEYCCYGDLLNFLRR-----------KRESFLTLEDLLSFSYQVAKGMA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 510 YLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWE 589
Cdd:cd05055   156 FLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWE 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 590 IFTYGKQPWYQLS-NNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLA 655
Cdd:cd05055   236 IFSLGSNPYPGMPvDSKFYKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIGKQL 302
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
382-641 5.50e-71

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 230.99  E-value: 5.50e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKRELGEGAFGKVFLAECynlcpeQDKILVAVKTLKDASdNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd05112     6 LTFVQEIGSGQFGLVHLGYW------LNKDKVAIKTIREGA-MSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd05112    79 EFMEHGCLSDYLRTQ------------RGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGM 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SRDVYSTDYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRT 621
Cdd:cd05112   147 TRFVLDDQYTSSTG-TKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAGFRLYKPRL 225
                         250       260
                  ....*....|....*....|
gi 1610576541 622 CPQEVYELMLGCWQREPHMR 641
Cdd:cd05112   226 ASTHVYEIMNHCWKERPEDR 245
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
388-651 1.15e-70

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 229.35  E-value: 1.15e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNlcpeqdkILVAVKTLKDASDNAR--KDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd13999     1 IGSGSFGEVYKGKWRG-------TDVAIKKLKVEDDNDEllKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR-- 543
Cdd:cd13999    74 GGSLYDLLH------------KKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRik 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVYSTDYYRVGGHTmlpiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVI-ECITQGRVLQRPRTC 622
Cdd:cd13999   142 NSTTEKMTGVVGTP----RWMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELSPIQIAaAVVQKGLRPPIPPDC 216
                         250       260
                  ....*....|....*....|....*....
gi 1610576541 623 PQEVYELMLGCWQREPHMRKNIKGIHTLL 651
Cdd:cd13999   217 PPELSKLIKRCWNEDPEKRPSFSEIVKRL 245
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
377-654 2.65e-70

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 229.37  E-value: 2.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVflaeCYNL--CPEQDKILVAVKTLKDA-SDNARKDFHREAELLTNLQHEHIVKFYGVCVE 453
Cdd:cd05066     1 IDASCIKIEKVIGAGEFGEV----CSGRlkLPGKREIPVAIKTLKAGyTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMKHGDLNKFLRAHgpDAvlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL 533
Cdd:cd05066    77 SKPVMIVTEYMENGSLDAFLRKH--DG----------QFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 534 VKIGDFGMSR---DVYSTDYYRVGGHtmLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECI 610
Cdd:cd05066   145 CKVSDFGLSRvleDDPEAAYTTRGGK--IPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAI 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1610576541 611 TQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05066   223 EEGYRLPAPMDCPAALHQLMLDCWQKDRNERPKFEQIVSILDKL 266
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
376-654 2.38e-69

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 226.78  E-value: 2.38e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 376 HIKRHNIVlkrelGEGAFGKVFLAECYnlCPEQDKILVAVKTLKDA-SDNARKDFHREAELLTNLQHEHIVKFYGVCVEG 454
Cdd:cd05063     6 HITKQKVI-----GAGEFGEVFRGILK--MPGRKEVAVAIKTLKPGyTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKHGDLNKFLRAHgpdavlmaEGnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 534
Cdd:cd05063    79 KPAMIITEYMENGALDKYLRDH--------DG----EFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLEC 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGMSR---DVYSTDYYRVGGHtmLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECIT 611
Cdd:cd05063   147 KVSDFGLSRvleDDPEGTYTTSGGK--IPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAIN 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1610576541 612 QGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05063   225 DGFRLPAPMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKL 267
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
387-652 7.32e-69

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 225.20  E-value: 7.32e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAECynlcpEQDKILVAVKTLKDASDNARKD-FHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd05084     3 RIGRGNFGEVFSGRL-----RADNTPVAVKSCRETLPPDLKAkFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHGPdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDV 545
Cdd:cd05084    78 GGDFLTFLRTEGP------------RLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 546 YSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQE 625
Cdd:cd05084   146 EDGVYAATGGMKQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRLPCPENCPDE 225
                         250       260
                  ....*....|....*....|....*..
gi 1610576541 626 VYELMLGCWQREPHMRKNIKGIHTLLQ 652
Cdd:cd05084   226 VYRLMEQCWEYDPRKRPSFSTVHQDLQ 252
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
377-645 1.03e-68

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 224.76  E-value: 1.03e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECynlcpeQDKILVAVKTLKDASdNARKDFHREAELLTNLQHEHIVKFYGVCVEGDP 456
Cdd:cd05113     1 IDPKDLTFLKELGTGQFGVVKYGKW------RGQYDVAIKMIKEGS-MSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLRAHGpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd05113    74 IFIITEYMANGCLLNYLREMR------------KRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKV 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSRDVYSTDYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVL 616
Cdd:cd05113   142 SDFGLSRYVLDDEYTSSVG-SKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEHVSQGLRL 220
                         250       260
                  ....*....|....*....|....*....
gi 1610576541 617 QRPRTCPQEVYELMLGCWQREPHMRKNIK 645
Cdd:cd05113   221 YRPHLASEKVYTIMYSCWHEKADERPTFK 249
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
386-641 4.59e-68

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 223.50  E-value: 4.59e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECynLCPEQDKILVAVKTLKDASDNARKD-FHREAELLTNLQHEHIVKFYGVCV--EGDPLImVFE 462
Cdd:cd05058     1 EVIGKGHFGCVYHGTL--IDSDGQKIHCAVKSLNRITDIEEVEqFLKEGIIMKDFSHPNVLSLLGICLpsEGSPLV-VLP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHgpdavlmaEGNPptelTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd05058    78 YMKHGDLRNFIRSE--------THNP----TVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 RDVYSTDYYRVGGHT--MLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPR 620
Cdd:cd05058   146 RDIYDKEYYSVHNHTgaKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRLLQPE 225
                         250       260
                  ....*....|....*....|.
gi 1610576541 621 TCPQEVYELMLGCWQREPHMR 641
Cdd:cd05058   226 YCPDPLYEVMLSCWHPKPEMR 246
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
377-645 1.65e-66

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 220.65  E-value: 1.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNLCPEQ-DKIL-VAVKTLK-DASDNARKDFHREAELLTNL-QHEHIVKFYGVCV 452
Cdd:cd05098    10 LPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKpNRVTkVAVKMLKsDATEKDLSDLISEMEMMKMIgKHKNIINLLGACT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 453 EGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMA---EGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVG 529
Cdd:cd05098    90 QDGPLYVIVEYASKGNLREYLQARRPPGMEYCynpSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 530 ENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIEC 609
Cdd:cd05098   170 EDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKL 249
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1610576541 610 ITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIK 645
Cdd:cd05098   250 LKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFK 285
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
382-659 2.05e-66

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 219.49  E-value: 2.05e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKRELGEGAFGKVFlaecYNLCPEQDKIL-VAVKTLKDA--SDNARKDFHREAELLTNLQHEHIVKFYGVCV-----E 453
Cdd:cd05075     2 LALGKTLGEGEFGSVM----EGQLNQDDSVLkVAVKTMKIAicTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLqntesE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPL-IMVFEYMKHGDLNKFLrahgpdaVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 532
Cdd:cd05075    78 GYPSpVVILPFMKHGDLHSFL-------LYSRLGDCPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQ 612
Cdd:cd05075   151 NVCVADFGLSKKIYNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQ 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1610576541 613 GRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASP 659
Cdd:cd05075   231 GNRLKQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILKDLP 277
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
381-654 6.41e-66

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 218.68  E-value: 6.41e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd05045     1 NLVLGKTLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKEnASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAH---GPdAVLMAEGNPPTE---------LTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCL 527
Cdd:cd05045    81 IVEYAKYGSLRSFLRESrkvGP-SYLGSDGNRNSSyldnpderaLTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 528 VGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVI 607
Cdd:cd05045   160 VAEGRKMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPERLF 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1610576541 608 ECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05045   240 NLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKM 286
IgI_TrkB_d5 cd05855
Fifth domain (immunoglobulin-like) of Trk receptor TrkB; member of the I-set of Ig ...
130-223 3.01e-65

Fifth domain (immunoglobulin-like) of Trk receptor TrkB; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth domain of Trk receptor, TrkB, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors, which mediate the trophic effects of the neurotrophin Nerve Growth Factor (NGF) family. Trks are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkB shares significant sequence homology and domain organization with TrkA and TrkC. The first three domains are leucine-rich domains while the fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrKB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. In some cell systems NT-3 can activate TrkA and TrkB receptors. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. This group belongs to the I-set of IgSF domains


Pssm-ID: 409441  Cd Length: 94  Bit Score: 209.71  E-value: 3.01e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 130 APTITFLESPTSDHHWCIPFTVKGNPKPALQWFYNGAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLIAKN 209
Cdd:cd05855     1 PPTITFLELPTRDHHWCIPFTVKGNPKPTLQWFHEGAILNESEYICTKIHVINNTEYHGCLQLDNPTHLNNGIYTLVAKN 80
                          90
                  ....*....|....
gi 1610576541 210 EYGKDEKQISAHFM 223
Cdd:cd05855    81 EYGEDEKNVSAHFM 94
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
381-651 3.84e-65

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 215.94  E-value: 3.84e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAeCYNLcPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd05064     6 SIKIERILGTGRFGELCRG-CLKL-PSKRELPVAIHTLRAgCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRGNTMMI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHgpdavlmaEGnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd05064    84 VTEYMSNGALDSFLRKH--------EG----QLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 G-MSRDVYSTDYYRVGGHTmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQR 618
Cdd:cd05064   152 RrLQEDKSEAIYTTMSGKS--PVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVIKAVEDGFRLPA 229
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1610576541 619 PRTCPQEVYELMLGCWQREPHMRKNIKGIHTLL 651
Cdd:cd05064   230 PRNCPNLLHQLMLDCWQKERGERPRFSQIHSIL 262
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
377-645 8.62e-65

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 217.20  E-value: 8.62e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNLcpEQDK----ILVAVKTLKD-ASDNARKDFHREAELLTNL-QHEHIVKFYGV 450
Cdd:cd05100     9 LSRTRLTLGKPLGEGCFGQVVMAEAIGI--DKDKpnkpVTVAVKMLKDdATDKDLSDLVSEMEMMKMIgKHKNIINLLGA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 451 CVEGDPLIMVFEYMKHGDLNKFLRAHGP---DAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCL 527
Cdd:cd05100    87 CTQDGPLYVLVEYASKGNLREYLRARRPpgmDYSFDTCKLPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 528 VGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVI 607
Cdd:cd05100   167 VTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 246
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1610576541 608 ECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIK 645
Cdd:cd05100   247 KLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFK 284
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
382-654 1.06e-64

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 214.71  E-value: 1.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKRELGEGAFGKVFLAecyNLCPEQDKIL-VAVKTLKDASDNAR--KDFHREAELLTNLQHEHIVKFYGVCVEGDPL- 457
Cdd:cd05035     1 LKLGKILGEGEFGSVMEA---QLKQDDGSQLkVAVKTMKVDIHTYSeiEEFLSEAACMKDFDHPNVMRLIGVCFTASDLn 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 -----IMVFEYMKHGDLNKFLRAhgpdavlMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 532
Cdd:cd05035    78 kppspMVILPFMKHGDLHSYLLY-------SRLGGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQ 612
Cdd:cd05035   151 TVCVADFGLSRKIYSGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDYLRN 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 613 GRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05035   231 GNRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENI 272
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
379-645 1.22e-64

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 216.03  E-value: 1.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECYNLCPEQDK--ILVAVKTLKD-ASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEG 454
Cdd:cd05101    23 RDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKeaVTVAVKMLKDdATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKHGDLNKFLRAHGPDAVLMA---EGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGEN 531
Cdd:cd05101   103 GPLYVIVEYASKGNLREYLRARRPPGMEYSydiNRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTEN 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 532 LLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECIT 611
Cdd:cd05101   183 NVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLK 262
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1610576541 612 QGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIK 645
Cdd:cd05101   263 EGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFK 296
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
377-654 2.18e-64

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 214.40  E-value: 2.18e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAEcynLCPEQDKIL-VAVKTLKdASDNARKD---FHREAELLTNLQHEHIVKFYGVCV 452
Cdd:cd05074     6 IQEQQFTLGRMLGKGEFGSVREAQ---LKSEDGSFQkVAVKMLK-ADIFSSSDieeFLREAACMKEFDHPNVIKLIGVSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 453 EGD-----PLIMV-FEYMKHGDLNKFLrahgpdavLMAE-GNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRN 525
Cdd:cd05074    82 RSRakgrlPIPMViLPFMKHGDLHTFL--------LMSRiGEEPFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 526 CLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNE 605
Cdd:cd05074   154 CMLNENMTVCVADFGLSKKIYSGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSE 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1610576541 606 VIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05074   234 IYNYLIKGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELI 282
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
388-654 9.42e-64

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 212.04  E-value: 9.42e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNlcPEQDKILVAVKTLKDA-SDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd05065    12 IGAGEFGEVCRGRLKL--PGKREIFVAIKTLKSGyTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMEN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRahgpdavlMAEGnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR--- 543
Cdd:cd05065    90 GALDSFLR--------QNDG----QFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRfle 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCP 623
Cdd:cd05065   158 DDTSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQDYRLPPPMDCP 237
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1610576541 624 QEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05065   238 TALHQLMLDCWQKDRNLRPKFGQIVNTLDKM 268
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
377-658 7.61e-63

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 209.90  E-value: 7.61e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAeCYNlcpeqDKILVAVKTLKDASDNARKdFHREAELLTNLQHEHIVKFYGVCVEGDP 456
Cdd:cd05072     4 IPRESIKLVKKLGAGQFGEVWMG-YYN-----NSTKVAVKTLKPGTMSVQA-FLEEANLMKTLQHDKLVRLYAVVTKEEP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLRAHGPDAVLMAegnppteltqsQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd05072    77 IYIITEYMAKGSLLDFLKSDEGGKVLLP-----------KLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKI 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSRDVYSTDYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVL 616
Cdd:cd05072   146 ADFGLARVIEDNEYTAREG-AKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSALQRGYRM 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 617 QRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKAS 658
Cdd:cd05072   225 PRMENCPDELYDIMKTCWKEKAEERPTFDYLQSVLDDFYTAT 266
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
386-641 7.99e-63

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 209.33  E-value: 7.99e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECynlcpeQDKILVAVKTLKDASdNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd05114    10 KELGSGLFGVVRLGKW------RAQYKVAIKAIREGA-MSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDV 545
Cdd:cd05114    83 NGCLLNYLRQR------------RGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 546 YSTDYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQE 625
Cdd:cd05114   151 LDDQYTSSSG-AKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRGHRLYRPKLASKS 229
                         250
                  ....*....|....*.
gi 1610576541 626 VYELMLGCWQREPHMR 641
Cdd:cd05114   230 VYEVMYSCWHEKPEGR 245
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
388-664 4.23e-62

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 208.04  E-value: 4.23e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecyNLCPEQD--KILVAVKTLKDASD-NARKDFHREAELLTNLQHEHIVKFYGVCVeGDPLIMVFEYM 464
Cdd:cd05057    15 LGSGAFGTVYKG---VWIPEGEkvKIPVAIKVLREETGpKANEEILDEAYVMASVDHPHLVRLLGICL-SSQVQLITQLM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR- 543
Cdd:cd05057    91 PLGCLLDYVR------------NHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 -DVYSTDYYRVGGhtMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTC 622
Cdd:cd05057   159 lDVDEKEYHAEGG--KVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEIPDLLEKGERLPQPPIC 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 623 PQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDI 664
Cdd:cd05057   237 TIDVYMVLVKCWMIDAESRPTFKELANEFSKMARDPQRYLVI 278
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
384-641 7.77e-61

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 203.92  E-value: 7.77e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  384 LKRELGEGAFGKVFLAECynlcpEQDKILVAVKTL-KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:smart00220   3 ILEKLGEGSFGKVYLARD-----KKTGKLVAIKVIkKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  463 YMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:smart00220  78 YCEGGDLFDLLKKRGR-------------LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLA 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  543 RDVYSTDYYR--VGghTmlpIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSN-NEVIECITQGRVLQRP 619
Cdd:smart00220 145 RQLDPGEKLTtfVG--T---PEYMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDDQlLELFKKIGKPKPPFPP 218
                          250       260
                   ....*....|....*....|....
gi 1610576541  620 R--TCPQEVYELMLGCWQREPHMR 641
Cdd:smart00220 219 PewDISPEAKDLIRKLLVKDPEKR 242
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
379-641 8.04e-61

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 205.42  E-value: 8.04e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNL-QHEHIVKFYGVCVE-GD 455
Cdd:cd05054     6 RDRLKLGKPLGRGAFGKVIQASAFGIDKSATCRTVAVKMLKEgATASEHKALMTELKILIHIgHHLNVVNLLGACTKpGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLRAH------GPDAVL--MAEGNPPTELTQSQ-----MLHIAQQIAAGMVYLASQHFVHRDLA 522
Cdd:cd05054    86 PLMVIVEFCKFGNLSNYLRSKreefvpYRDKGArdVEEEEDDDELYKEPltledLICYSFQVARGMEFLASRKCIHRDLA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 523 TRNCLVGENLLVKIGDFGMSRDVYST-DYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQL 601
Cdd:cd05054   166 ARNILLSENNVVKICDFGLARDIYKDpDYVRKGD-ARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGV 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1610576541 602 S-NNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05054   245 QmDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKER 285
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
388-641 1.12e-60

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 203.31  E-value: 1.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcpeQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd05085     4 LGKGNFGEVYKGTL------KDKTPVAVKTCKeDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD-- 544
Cdd:cd05085    78 GDFLSFLR------------KKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQed 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 --VYSTDyyrvgGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTC 622
Cdd:cd05085   146 dgVYSSS-----GLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKGYRMSAPQRC 220
                         250
                  ....*....|....*....
gi 1610576541 623 PQEVYELMLGCWQREPHMR 641
Cdd:cd05085   221 PEDIYKIMQRCWDYNPENR 239
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
381-652 1.15e-60

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 203.57  E-value: 1.15e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAEcYNLCPeqdkilVAVKTLKdaSDNARKDFHREAELLTNLQHEHIVKFYGVCVEgDPLIMV 460
Cdd:cd05083     7 KLTLGEIIGEGEFGAVLQGE-YMGQK------VAVKNIK--CDVTAQAFLEETAVMTKLQHKNLVRLLGVILH-NGLYIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGPDAVlmaegNPPteltqsQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd05083    77 MELMSKGNLVNFLRSRGRALV-----PVI------QLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDVYSTDyyrvgGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPR 620
Cdd:cd05083   146 LAKVGSMGV-----DNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAVEKGYRMEPPE 220
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1610576541 621 TCPQEVYELMLGCWQREPHMRKNIKGIHTLLQ 652
Cdd:cd05083   221 GCPPDVYSIMTSCWEAEPGKRPSFKKLREKLE 252
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
388-654 2.87e-60

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 202.96  E-value: 2.87e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd05047     3 IGEGNFGQVLKAR---IKKDGLRMDAAIKRMKEyASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAH---GPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd05047    80 HGNLLDFLRKSrvlETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 R--DVYSTDyyrvgghTM--LPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQR 618
Cdd:cd05047   160 RgqEVYVKK-------TMgrLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEK 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1610576541 619 PRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05047   233 PLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 268
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
377-657 3.45e-60

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 202.42  E-value: 3.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAeCYNlcpeqDKILVAVKTLKDASDNARKdFHREAELLTNLQHEHIVKFYGVcVEGDP 456
Cdd:cd05067     4 VPRETLKLVERLGAGQFGEVWMG-YYN-----GHTKVAIKSLKQGSMSPDA-FLAEANLMKQLQHQRLVRLYAV-VTQEP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLRAhgpdavlmAEGnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd05067    76 IYIITEYMENGSLVDFLKT--------PSG---IKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSRDVYSTDYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVL 616
Cdd:cd05067   145 ADFGLARLIEDNEYTAREG-AKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRM 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1610576541 617 QRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKA 657
Cdd:cd05067   224 PRPDNCPEELYQLMRLCWKERPEDRPTFEYLRSVLEDFFTA 264
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
381-664 4.88e-60

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 203.31  E-value: 4.88e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAEcynLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPLI 458
Cdd:cd05089     3 DIKFEDVIGEGNFGQVIKAM---IKKDGLKMNAAIKMLKEfASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLRAH---GPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd05089    80 IAIEYAPYGNLLDFLRKSrvlETDPAFAKEHGTASTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSRdvySTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd05089   160 IADFGLSR---GEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYR 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1610576541 616 LQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDI 664
Cdd:cd05089   237 MEKPRNCDDEVYELMRQCWRDRPYERPPFSQISVQLSRMLEARKAYVNM 285
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
377-652 1.14e-59

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 201.53  E-value: 1.14e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYN-LCPEQDkilVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVE- 453
Cdd:cd05043     3 VSRERVTLSDLLQEGTFGRIFHGILRDeKGKEEE---VLVKTVKDhASEIQVTMLLQESSLLYGLSHQNLLPILHVCIEd 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMKHGDLNKFLRAhgpdaVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL 533
Cdd:cd05043    80 GEKPMVLYPYMNWGNLKLFLQQ-----CRLSEANNPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 534 VKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQG 613
Cdd:cd05043   155 VKITDNALSRDLFPMDYHCLGDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAYLKDG 234
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1610576541 614 RVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQ 652
Cdd:cd05043   235 YRLAQPINCPDELFAVMACCWALDPEERPSFQQLVQCLT 273
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
377-659 1.60e-59

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 201.32  E-value: 1.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNlcPEQDKILVAVKTLK--DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEG 454
Cdd:cd14204     4 IDRNLLSLGKVLGEGEFGSVMEGELQQ--PDGTNHKVAVKTMKldNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCLEV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPL-----IMVFEYMKHGDLNKFLrahgpdaVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVG 529
Cdd:cd14204    82 GSQripkpMVILPFMKYGDLHSFL-------LRSRLGSGPQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 530 ENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIEC 609
Cdd:cd14204   155 DDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYDY 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1610576541 610 ITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASP 659
Cdd:cd14204   235 LLHGHRLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLESLP 284
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
378-634 1.02e-57

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 195.94  E-value: 1.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 378 KRHNIVLKR-ELGEGAFGKVFLAeCYNLcpEQDKILVAVKTLKDASD-NARKDFHREAELLTNLQHEHIVKFYGVCvEGD 455
Cdd:cd05115     1 KRDNLLIDEvELGSGNFGCVKKG-VYKM--RKKQIDVAIKVLKQGNEkAVRDEMMREAQIMHQLDNPYIVRMIGVC-EAE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLrahgpdavlmaeGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd05115    77 ALMLVMEMASGGPLNKFL------------SGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSRDVYSTD-YYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGR 614
Cdd:cd05115   145 ISDFGLSKALGADDsYYKARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGK 224
                         250       260
                  ....*....|....*....|
gi 1610576541 615 VLQRPRTCPQEVYELMLGCW 634
Cdd:cd05115   225 RMDCPAECPPEMYALMSDCW 244
IgI_TrKABC_d5 cd04971
Fifth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB, and TrkC; member of the I-set ...
130-223 1.02e-57

Fifth domain (immunoglobulin-like) of Trk receptors TrkA, TrkB, and TrkC; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth domain of Trk receptors TrkA, TrkB, and TrkC, an immunoglobulin (Ig)-like domain which binds to neurotrophin. The Trk family of receptors are tyrosine kinase receptors. They are activated by dimerization, leading to autophosphorylation of intracellular tyrosine residues, and triggering the signal transduction pathway. TrkA, TrkB, and TrkC share significant sequence homology and domain organization. The first three domains are leucine-rich domains while the fourth and fifth domains are Ig-like domains playing a part in ligand binding. TrkA, TrkB, and TrkC mediate the trophic effects of the neurotrophin Nerve Growth Factor (NGF) family. TrkA is recognized by NGF. TrkB is recognized by brain-derived neurotrophic factor (BDNF) and neurotrophin (NT)-4. TrkC is recognized by NT-3. NT-3 is promiscuous as in some cell systems it activates TrkA and TrkB receptors. TrkA is a receptor found in all major NGF targets, including the sympathetic, trigeminal, and dorsal root ganglia, cholinergic neurons of the basal forebrain, and the striatum. TrKB transcripts are found throughout multiple structures of the central and peripheral nervous systems. The TrkC gene is expressed throughout the mammalian nervous system. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409360  Cd Length: 96  Bit Score: 189.54  E-value: 1.02e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 130 APTITFLESPTSDHHWCIPFTVKGNPKPALQWFYNGAILNESKYICTKIH--VTNHTEYHGCLQLDNPTHMNNGDYTLIA 207
Cdd:cd04971     1 APVIVRLEEPELRHHWCIPFTVRGNPKPTLTWYHNGAVLNESDYIRTEIHyeAATPTEYHGCLKFDNPTHVNNGNYTLVA 80
                          90
                  ....*....|....*.
gi 1610576541 208 KNEYGKDEKQISAHFM 223
Cdd:cd04971    81 SNEYGQDSKSISAHFM 96
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
379-655 3.44e-57

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 198.15  E-value: 3.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLK-DASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDP 456
Cdd:cd05106    37 RDNLQFGKTLGAGAFGKVVEATAFGLGKEDNVLRVAVKMLKaSAHTDEREALMSELKILSHLgQHKNIVNLLGACTHGGP 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLR---------------------------------------------------------AHGPD 479
Cdd:cd05106   117 VLVITEYCCYGDLLNFLRkkaetflnfvmalpeisetssdyknitlekkyirsdsgfssqgsdtyvemrpvssssSQSSD 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 480 AVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTML 559
Cdd:cd05106   197 SKDEEDTEDSWPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIMNDSNYVVKGNARL 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 560 PIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQ-LSNNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREP 638
Cdd:cd05106   277 PVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGiLVNSKFYKMVKRGYQMSRPDFAPPEIYSIMKMCWNLEP 356
                         330
                  ....*....|....*..
gi 1610576541 639 HMRKNIKGIHTLLQNLA 655
Cdd:cd05106   357 TERPTFSQISQLIQRQL 373
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
377-654 4.07e-57

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 194.47  E-value: 4.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAEcYNlcpeqDKILVAVKTLKDASDNARKdFHREAELLTNLQHEHIVKFYGVcVEGDP 456
Cdd:cd05073     8 IPRESLKLEKKLGAGQFGEVWMAT-YN-----KHTKVAVKTMKPGSMSVEA-FLAEANVMKTLQHDKLVKLHAV-VTKEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLRAHgpdavlmaEGNpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd05073    80 IYIITEFMAKGSLLDFLKSD--------EGS---KQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSRDVYSTDYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVL 616
Cdd:cd05073   149 ADFGLARVIEDNEYTAREG-AKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRM 227
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1610576541 617 QRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05073   228 PRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDF 265
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
386-654 5.05e-57

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 194.73  E-value: 5.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAeCYNlcPEQDKI--LVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVE--GDPLIMV 460
Cdd:cd05080    10 RDLGEGHFGKVSLY-CYD--PTNDGTgeMVAVKALKaDCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEqgGKSLQLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLrahgpdavlmaegnPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd05080    87 MEYVPLGSLRDYL--------------PKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDV-YSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTY--GKQP------------WYQLSNNE 605
Cdd:cd05080   153 LAKAVpEGHEYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHcdSSQSpptkflemigiaQGQMTVVR 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1610576541 606 VIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05080   233 LIELLERGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILKTV 281
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
386-653 9.00e-57

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 192.82  E-value: 9.00e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAeCYNlcpeqDKILVAVKTLKDASdNARKDFHREAELLTNLQHEHIVKFYGVCVEgDPLIMVFEYMK 465
Cdd:cd14203     1 VKLGQGCFGEVWMG-TWN-----GTTKVAIKTLKPGT-MSPEAFLEEAQIMKKLRHDKLVQLYAVVSE-EPIYIVTEFMS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAhgpdavlmAEGNpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDV 545
Cdd:cd14203    73 KGSLLDFLKD--------GEGK---YLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 546 YSTDYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQE 625
Cdd:cd14203   142 EDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPES 220
                         250       260
                  ....*....|....*....|....*...
gi 1610576541 626 VYELMLGCWQREPHMRKNIKGIHTLLQN 653
Cdd:cd14203   221 LHELMCQCWRKDPEERPTFEYLQSFLED 248
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
387-653 2.61e-56

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 191.71  E-value: 2.61e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVfLAECYNLCPEQDkiLVAVKTLK-DASDNARKD-FHREAELLTNLQHEHIVKFYGVCvEGDPLIMVFEYM 464
Cdd:cd05116     2 ELGSGNFGTV-KKGYYQMKKVVK--TVAVKILKnEANDPALKDeLLREANVMQQLDNPYIVRMIGIC-EAESWMLVMEMA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd05116    78 ELGPLNKFLQKN-------------RHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 VYSTD-YYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCP 623
Cdd:cd05116   145 LRADEnYYKAQTHGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERMECPAGCP 224
                         250       260       270
                  ....*....|....*....|....*....|
gi 1610576541 624 QEVYELMLGCWQREPHMRKNIKGIHTLLQN 653
Cdd:cd05116   225 PEMYDLMKLCWTYDVDERPGFAAVELRLRN 254
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
388-647 3.62e-55

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 187.09  E-value: 3.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNlcpeqDKILVAVKTL-KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd00180     1 LGKGSFGKVYKARDKE-----TGKKVAVKVIpKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAHGPdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVY 546
Cdd:cd00180    76 GSLKDLLKENKG------------PLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 547 STDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIftygkqpwyqlsnneviecitqgrvlqrprtcpQEV 626
Cdd:cd00180   144 SDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL---------------------------------EEL 190
                         250       260
                  ....*....|....*....|.
gi 1610576541 627 YELMLGCWQREPHMRKNIKGI 647
Cdd:cd00180   191 KDLIRRMLQYDPKKRPSAKEL 211
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
378-645 1.01e-54

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 188.69  E-value: 1.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 378 KRHNIVLKrELGEGAFGKVFLAEcYNlcPEQDKI--LVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEG- 454
Cdd:cd14205     3 ERHLKFLQ-QLGKGNFGSVEMCR-YD--PLQDNTgeVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 -DPLIMVFEYMKHGDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL 533
Cdd:cd14205    79 rRNLRLIMEYLPYGSLRDYLQKH------------KERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 534 VKIGDFGMSRDV-YSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTY---GKQP----WYQLSNNE 605
Cdd:cd14205   147 VKIGDFGLTKVLpQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYiekSKSPpaefMRMIGNDK 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1610576541 606 --------VIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIK 645
Cdd:cd14205   227 qgqmivfhLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFR 274
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
377-654 1.04e-54

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 187.50  E-value: 1.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAEcynlcpeQDKILVAVKTLK-DASDNArkdFHREAELLTNLQHEHIVKFYGVCVEGD 455
Cdd:cd05082     3 LNMKELKLLQTIGKGEFGDVMLGD-------YRGNKVAVKCIKnDATAQA---FLAEASVMTQLRHSNLVQLLGVIVEEK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 -PLIMVFEYMKHGDLNKFLRAHGPdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 534
Cdd:cd05082    73 gGLYIVTEYMAKGSLVDYLRSRGR-----------SVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGMSRDVYSTDyyrvgGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGR 614
Cdd:cd05082   142 KVSDFGLTKEASSTQ-----DTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGY 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1610576541 615 VLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05082   217 KMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQLREQLEHI 256
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
377-641 1.29e-54

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 190.21  E-value: 1.29e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHE-HIVKFYGVCVE- 453
Cdd:cd14207     4 FARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCRVVAVKMLKEgATASEYKALMTELKILIHIGHHlNVVNLLGACTKs 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMKHGDLNKFLRAH------GPDAVLMAE------GNPPTE------------------------------ 491
Cdd:cd14207    84 GGPLMVIVEYCKYGNLSNYLKSKrdffvtNKDTSLQEElikekkEAEPTGgkkkrlesvtssesfassgfqedkslsdve 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 492 -------------LTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTM 558
Cdd:cd14207   164 eeeedsgdfykrpLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKGDAR 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 559 LPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNE-VIECITQGRVLQRPRTCPQEVYELMLGCWQRE 637
Cdd:cd14207   244 LPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGVQIDEdFCSKLKEGIRMRAPEFATSEIYQIMLDCWQGD 323

                  ....
gi 1610576541 638 PHMR 641
Cdd:cd14207   324 PNER 327
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
377-654 1.53e-54

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 191.76  E-value: 1.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKD-FHREAELLTNL-QHEHIVKFYGVCVEG 454
Cdd:cd05107    34 MPRDNLVLGRTLGSGAFGRVVEATAHGLSHSQSTMKVAVKMLKSTARSSEKQaLMSELKIMSHLgPHLNIVNLLGACTKG 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKHGDL------NK--FLRAHG----PDAVLMAEGNPPTE------------------------------- 491
Cdd:cd05107   114 GPIYIITEYCRYGDLvdylhrNKhtFLQYYLdknrDDGSLISGGSTPLSqrkshvslgsesdggymdmskdesadyvpmq 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 492 ------------------------------------------LTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVG 529
Cdd:cd05107   194 dmkgtvkyadiessnyespydqylpsapertrrdtlinespaLSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLIC 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 530 ENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVI-E 608
Cdd:cd05107   274 EGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFTLGGTPYPELPMNEQFyN 353
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1610576541 609 CITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05107   354 AIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDL 399
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
386-651 1.63e-54

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 187.85  E-value: 1.63e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNLC-PEQdkilVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd14206     3 QEIGNGWFGKVILGEIFSDYtPAQ----VVVKELRvSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGPdavlmAEGNPPTELTQ--SQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd14206    79 CQLGDLKRYLRAQRK-----ADGMTPDLPTRdlRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SRDVYSTDYYRVGGHTMLPIRWMPPE-------SIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGR 614
Cdd:cd14206   154 SHNNYKEDYYLTPDRLWIPLRWVAPElldelhgNLIVVDQSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTFVVREQ 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 615 --VLQRPR-TCPQE--VYELMLGCWqREPHMRKNIKGIHTLL 651
Cdd:cd14206   234 qmKLAKPRlKLPYAdyWYEIMQSCW-LPPSQRPSVEELHLQL 274
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
386-651 4.34e-54

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 186.25  E-value: 4.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYN-LCPEQdkilVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd05042     1 QEIGNGWFGKVLLGEIYSgTSVAQ----VVVKELKaSANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGPdavlmAEGNPPTELTQSQMlhiAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd05042    77 CDLGDLKAYLRSERE-----HERGDSDTRTLQRM---ACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAH 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVYSTDYYRVGGHTMLPIRWMPPE-------SIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVL 616
Cdd:cd05042   149 SRYKEDYIETDDKLWFPLRWTAPElvtefhdRLLVVDQTKYSNIWSLGVTLWELFENGAQPYSNLSDLDVLAQVVREQDT 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 617 QRPRtcPQ-------EVYELMLGCWqREPHMRKNIKGIHTLL 651
Cdd:cd05042   229 KLPK--PQlelpysdRWYEVLQFCW-LSPEQRPAAEDVHLLL 267
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
377-661 4.60e-54

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 186.43  E-value: 4.60e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAEcYNLCPEqdkilVAVKTLKDASDNARKdFHREAELLTNLQHEHIVKFYGVCVEgDP 456
Cdd:cd05071     6 IPRESLRLEVKLGQGCFGEVWMGT-WNGTTR-----VAIKTLKPGTMSPEA-FLQEAQVMKKLRHEKLVQLYAVVSE-EP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLRahgpdavlmaeGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd05071    78 IYIVTEYMSKGSLLDFLK-----------GEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSRDVYSTDYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVL 616
Cdd:cd05071   147 ADFGLARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRM 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1610576541 617 QRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQN-LAKASPVY 661
Cdd:cd05071   226 PCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDyFTSTEPQY 271
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
377-654 4.19e-53

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 185.95  E-value: 4.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEG 454
Cdd:cd05102     4 FPRDRLRLGKVLGHGAFGKVVEASAFGIDKSSSCETVAVKMLKEgATASEHKALMSELKILIHIgNHLNVVNLLGACTKP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 D-PLIMVFEYMKHGDLNKFLRA--------------------------------HGP--DAVLMAEG----NPPTE---- 491
Cdd:cd05102    84 NgPLMVIVEFCKYGNLSNFLRAkregfspyrersprtrsqvrsmveavradrrsRQGsdRVASFTEStsstNQPRQevdd 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 492 -----LTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPP 566
Cdd:cd05102   164 lwqspLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGSARLPLKWMAP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 567 ESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLS-NNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIK 645
Cdd:cd05102   244 ESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQiNEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKERPTFS 323

                  ....*....
gi 1610576541 646 GIHTLLQNL 654
Cdd:cd05102   324 DLVEILGDL 332
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
386-651 5.53e-53

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 183.98  E-value: 5.53e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcYNlcPEQDKI--LVAVKTLKDAS-DNARKDFHREAELLTNLQHEHIVKFYGVCVE--GDPLIMV 460
Cdd:cd05079    10 RDLGEGHFGKVELCR-YD--PEGDNTgeQVAVKSLKPESgGNHIADLKKEIEILRNLYHENIVKYKGICTEdgGNGIKLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLrahgPDAVlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd05079    87 MEFLPSGSLKEYL----PRNK--------NKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDVYS-TDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWY--------------QLSNNE 605
Cdd:cd05079   155 LTKAIETdKEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSESSpmtlflkmigpthgQMTVTR 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1610576541 606 VIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKN----IKGIHTLL 651
Cdd:cd05079   235 LVRVLEEGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTfqnlIEGFEAIL 284
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
377-661 1.27e-52

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 182.58  E-value: 1.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAEcYNLCPEqdkilVAVKTLKDASdNARKDFHREAELLTNLQHEHIVKFYGVCVEgDP 456
Cdd:cd05069     9 IPRESLRLDVKLGQGCFGEVWMGT-WNGTTK-----VAIKTLKPGT-MMPEAFLQEAQIMKKLRHDKLVPLYAVVSE-EP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLRahgpdavlmaEGNPpTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd05069    81 IYIVTEFMGKGSLLDFLK----------EGDG-KYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSRDVYSTDYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVL 616
Cdd:cd05069   150 ADFGLARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRM 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1610576541 617 QRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKAS-PVY 661
Cdd:cd05069   229 PCPQGCPESLHELMKLCWKKDPDERPTFEYIQSFLEDYFTATePQY 274
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
381-663 1.53e-52

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 183.28  E-value: 1.53e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAECYNLCPEQDkilVAVKTLKD-ASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPLI 458
Cdd:cd05088     8 DIKFQDVIGEGNFGQVLKARIKKDGLRMD---AAIKRMKEyASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLRAH---GPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd05088    85 LAIEYAPHGNLLDFLRKSrvlETDPAFAIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSRdvySTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd05088   165 IADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYR 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1610576541 616 LQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLD 663
Cdd:cd05088   242 LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERKTYVN 289
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
379-658 3.10e-52

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 183.64  E-value: 3.10e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECYNLcpeqDKI----LVAVKTLKD-ASDNARKDFHREAELLTNLQHE-HIVKFYGVCV 452
Cdd:cd05103     6 RDRLKLGKPLGRGAFGQVIEADAFGI----DKTatcrTVAVKMLKEgATHSEHRALMSELKILIHIGHHlNVVNLLGACT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 453 E-GDPLIMVFEYMKHGDLNKFLRAHGPDAVL------------------------------------------------M 483
Cdd:cd05103    82 KpGGPLMVIVEFCKFGNLSAYLRSKRSEFVPyktkgarfrqgkdyvgdisvdlkrrldsitssqssassgfveekslsdV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 484 AEGNPPTE------LTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHT 557
Cdd:cd05103   162 EEEEAGQEdlykdfLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGDA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 558 MLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIEC-ITQGRVLQRPRTCPQEVYELMLGCWQR 636
Cdd:cd05103   242 RLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEEFCRrLKEGTRMRAPDYTTPEMYQTMLDCWHG 321
                         330       340
                  ....*....|....*....|..
gi 1610576541 637 EPHMRKNIKGIHTLLQNLAKAS 658
Cdd:cd05103   322 EPSQRPTFSELVEHLGNLLQAN 343
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
374-661 6.84e-52

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 180.65  E-value: 6.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 374 VQHIKRHNIVLKRELGEGAFGKVFLAEcYNlcpeqDKILVAVKTLKDASdNARKDFHREAELLTNLQHEHIVKFYGVcVE 453
Cdd:cd05070     3 VWEIPRESLQLIKRLGNGQFGEVWMGT-WN-----GNTKVAIKTLKPGT-MSPESFLEEAQIMKKLKHDKLVQLYAV-VS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMKHGDLNKFLRAhgpdavlmAEGNPpteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL 533
Cdd:cd05070    75 EEPIYIVTEYMSKGSLLDFLKD--------GEGRA---LKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 534 VKIGDFGMSRDVYSTDYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQG 613
Cdd:cd05070   144 CKIADFGLARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERG 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1610576541 614 RVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKAS-PVY 661
Cdd:cd05070   223 YRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATePQY 271
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
388-654 2.58e-51

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 179.32  E-value: 2.58e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVE-GDP-LIMVFEYMK 465
Cdd:cd05081    12 LGKGNFGSVELCR-YDPLGDNTGALVAVKQLQHSGPDQQRDFQREIQILKALHSDFIVKYRGVSYGpGRRsLRLVMEYLP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDV 545
Cdd:cd05081    91 SGCLRDFLQRH------------RARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 546 -YSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQP------WYQLSNNE--------VIECI 610
Cdd:cd05081   159 pLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKScspsaeFLRMMGCErdvpalcrLLELL 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1610576541 611 TQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05081   239 EEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDML 282
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
379-654 1.68e-49

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 177.91  E-value: 1.68e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKD-FHREAELLTNL-QHEHIVKFYGVCVEGDP 456
Cdd:cd05105    36 RDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQaLMSELKIMTHLgPHLNIVNLLGACTKSGP 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDL--------NKFLRAHgPD---------------------AVLMAEGN-------------------- 487
Cdd:cd05105   116 IYIITEYCFYGDLvnylhknrDNFLSRH-PEkpkkdldifginpadestrsyVILSFENKgdymdmkqadttqyvpmlei 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 488 ----------------PPTE-------------------LTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 532
Cdd:cd05105   195 keaskysdiqrsnydrPASYkgsndsevknllsddgsegLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGK 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWY-QLSNNEVIECIT 611
Cdd:cd05105   275 IVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPgMIVDSTFYNKIK 354
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1610576541 612 QGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd05105   355 SGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESL 397
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
386-651 1.95e-48

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 170.94  E-value: 1.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYN-LCPEQdkilVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd05087     3 KEIGHGWFGKVFLGEVNSgLSSTQ----VVVKELKaSASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAhgpdaVLMAEGNPPTELTQSQMlhiAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd05087    79 CPLGDLKGYLRS-----CRAAESMAPDPLTLQRM---ACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSH 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVYSTDYYRVGGHTMLPIRWMPPE-------SIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVL 616
Cdd:cd05087   151 CKYKEDYFVTADQLWVPLRWIAPElvdevhgNLLVVDQTKQSNVWSLGVTIWELFELGNQPYRHYSDRQVLTYTVREQQL 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1610576541 617 QRPR-----TCPQEVYELMLGCWQrEPHMRKNIKGIHTLL 651
Cdd:cd05087   231 KLPKpqlklSLAERWYEVMQFCWL-QPEQRPTAEEVHLLL 269
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
388-664 2.12e-48

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 171.29  E-value: 2.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynLCPEQD--KILVAVKTLKDASdnARKDFHREAE---LLTNLQHEHIVKFYGVCvEGDPLIMVFE 462
Cdd:cd05111    15 LGSGVFGTVHKGI---WIPEGDsiKIPVAIKVIQDRS--GRQSFQAVTDhmlAIGSLDHAYIVRLLGIC-PGASLQLVTQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHgpdavlmaEGNppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd05111    89 LLPLGSLLDHVRQH--------RGS----LGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 RDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTC 622
Cdd:cd05111   157 DLLYPDDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAEVPDLLEKGERLAQPQIC 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 623 PQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDI 664
Cdd:cd05111   237 TIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYLVI 278
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
379-652 3.15e-48

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 173.55  E-value: 3.15e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLK-DASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDP 456
Cdd:cd05104    34 RDRLRFGKTLGAGAFGKVVEATAYGLAKADSAMTVAVKMLKpSAHSTEREALMSELKVLSYLgNHINIVNLLGACTVGGP 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLR------------AHGPDAV---LMAEGNP-------------------PTELTQSQMLHIAQ 502
Cdd:cd05104   114 TLVITEYCCYGDLLNFLRrkrdsficpkfeDLAEAALyrnLLHQREMacdslneymdmkpsvsyvvPTKADKRRGVRSGS 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 503 ----------------------------QIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVG 554
Cdd:cd05104   194 yvdqdvtseileedelaldtedllsfsyQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNYVVK 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 555 GHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLS-NNEVIECITQGRVLQRPRTCPQEVYELMLGC 633
Cdd:cd05104   274 GNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMPvDSKFYKMIKEGYRMDSPEFAPSEMYDIMRSC 353
                         330
                  ....*....|....*....
gi 1610576541 634 WQREPHMRKNIKGIHTLLQ 652
Cdd:cd05104   354 WDADPLKRPTFKQIVQLIE 372
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
384-641 7.10e-48

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 168.92  E-value: 7.10e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECynlcpEQDKILVAVKTLK---DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:cd14014     4 LVRLLGRGGMGEVYRARD-----TLLGRPVAIKVLRpelAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd14014    79 MEYVEGGSLADLLRERGP-------------LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDVYSTDYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVL---Q 617
Cdd:cd14014   146 IARALGDSGLTQTGS-VLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDSPAAVLAKHLQEAPPppsP 223
                         250       260
                  ....*....|....*....|....
gi 1610576541 618 RPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd14014   224 LNPDVPPALDAIILRALAKDPEER 247
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
386-652 1.14e-46

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 165.77  E-value: 1.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcYNLCPEqdkiLVAVKTLKDASDNARKD--FHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd06606     6 ELLGKGSFGSVYLAL-NLDTGE----LMAVKEVELSGDSEEELeaLEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd06606    81 VPGGSLASLLKKFGK-------------LPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVySTDYYRVGGHTML--PiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNN-EVIECITQGRVL-QRP 619
Cdd:cd06606   148 RL-AEIATGEGTKSLRgtP-YWMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWSELGNPvAALFKIGSSGEPpPIP 224
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1610576541 620 RTCPQEVYELMLGCWQREPHMRKNIKgihTLLQ 652
Cdd:cd06606   225 EHLSEEAKDFLRKCLQRDPKKRPTAD---ELLQ 254
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
386-666 1.27e-46

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 167.51  E-value: 1.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAeCYNLCPEQDKILVAVKTLKDA-SDNARKDFHREAELLTNLQHEHIVKFYGVCVEgDPLIMVFEYM 464
Cdd:cd05108    13 KVLGSGAFGTVYKG-LWIPEGEKVKIPVAIKELREAtSPKANKEILDEAYVMASVDNPHVCRLLGICLT-STVQLITQLM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd05108    91 PFGCLLDYVREH------------KDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 VYSTD--YYRVGGHtmLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTC 622
Cdd:cd05108   159 LGAEEkeYHAEGGK--VPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPIC 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1610576541 623 PQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDILG 666
Cdd:cd05108   237 TIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQG 280
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
386-664 1.75e-46

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 165.97  E-value: 1.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAeCYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDpLIMVFEYM 464
Cdd:cd05109    13 KVLGSGAFGTVYKG-IWIPDGENVKIPVAIKVLREnTSPKANKEILDEAYVMAGVGSPYVCRLLGICLTST-VQLVTQLM 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR- 543
Cdd:cd05109    91 PYGCLLDYVREN------------KDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 -DVYSTDYYRVGGHtmLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTC 622
Cdd:cd05109   159 lDIDETEYHADGGK--VPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPIC 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 623 PQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDI 664
Cdd:cd05109   237 TIDVYMIMVKCWMIDSECRPRFRELVDEFSRMARDPSRFVVI 278
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
388-666 1.90e-44

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 161.00  E-value: 1.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynLCPEQD--KILVAVKTLKDASD-NARKDFHREAELLTNLQHEHIVKFYGVCVEgdPLI-MVFEY 463
Cdd:cd05110    15 LGSGAFGTVYKGI---WVPEGEtvKIPVAIKILNETTGpKANVEFMDEALIMASMDHPHLVRLLGVCLS--PTIqLVTQL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHgpdavlmaEGNPPTELtqsqMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd05110    90 MPHGCLLDYVHEH--------KDNIGSQL----LLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLAR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 --DVYSTDYYRVGGHtmLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRT 621
Cdd:cd05110   158 llEGDEKEYNADGGK--MPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPI 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1610576541 622 CPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDILG 666
Cdd:cd05110   236 CTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQRYLVIQG 280
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
386-651 1.27e-43

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 157.72  E-value: 1.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNlcpEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd05086     3 QEIGNGWFGKVLLGEIYT---GTSVARVVVKELKaSANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHGPDAvlmaEGNPPTELTQsqmlHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd05086    80 DLGDLKTYLANQQEKL----RGDSQIMLLQ----RMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIGFS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 VYSTDYYRVGGHTMLPIRWMPPESIMYRK-------FTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQ 617
Cdd:cd05086   152 RYKEDYIETDDKKYAPLRWTAPELVTSFQdgllaaeQTKYSNIWSLGVTLWELFENAAQPYSDLSDREVLNHVIKERQVK 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1610576541 618 RPRtcPQ-------EVYELMLGCWqREPHMRKNIKGIHTLL 651
Cdd:cd05086   232 LFK--PHleqpysdRWYEVLQFCW-LSPEKRPTAEEVHRLL 269
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
388-654 1.41e-43

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 157.17  E-value: 1.41e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcpeQDKILVAVKTLKDASDN----ARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd14061     2 IGVGGFGKVYRGI-------WRGEEVAVKAARQDPDEdisvTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKflrahgpdaVLMAEGNPPTELtqsqmLHIAQQIAAGMVYLASQHFV---HRDLATRNCLVGE--------NL 532
Cdd:cd14061    75 ARGGALNR---------VLAGRKIPPHVL-----VDWAIQIARGMNYLHNEAPVpiiHRDLKSSNILILEaienedleNK 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFGMSRDVYSTDYYRVGGhtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW---------YQLSN 603
Cdd:cd14061   141 TLKITDFGLAREWHKTTRMSAAG----TYAWMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYkgidglavaYGVAV 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 604 NEViecitqgrVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd14061   216 NKL--------TLPIPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLENI 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
383-641 1.79e-43

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 163.26  E-value: 1.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKD---ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:COG0515    10 RILRLLGRGGMGVVYLAR-----DLRLGRPVALKVLRPelaADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:COG0515    85 VMEYVEGESLADLLRRRGP-------------LPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMSRDVYSTDYYRVgGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVL--- 616
Cdd:COG0515   152 GIARALGGATLTQT-GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT-GRPPFDGDSPAELLRAHLREPPPpps 229
                         250       260
                  ....*....|....*....|....*
gi 1610576541 617 QRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:COG0515   230 ELRPDLPPALDAIVLRALAKDPEER 254
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
386-647 1.01e-41

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 152.23  E-value: 1.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECynlcpEQDKILVAVKT--LKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd08215     6 RVIGKGSFGSAYLVRR-----KSDGKLYVLKEidLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGPDAVLMAEgnppteltqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd08215    81 ADGGDLAQKIKKQKKKGQPFPE---------EQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 dVYS-----------TDYYrvgghtmlpirwMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQ 612
Cdd:cd08215   152 -VLEsttdlaktvvgTPYY------------LSPELCENKPYNYKSDIWALGCVLYELCT-LKHPFEANNLPALVYKIVK 217
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1610576541 613 GRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd08215   218 GQYPPIPSQYSSELRDLVNSMLQKDPEKRPSANEI 252
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
388-643 1.93e-39

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 146.06  E-value: 1.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLcpeqdKILVAVKTLK--DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd13978     1 LGSGGFGTVSKARHVSW-----FGMVAIKCLHssPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYME 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRahgpdavlMAEGNPPTELtQSQMLHiaqQIAAGMVYL--ASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd13978    76 NGSLKSLLE--------REIQDVPWSL-RFRIIH---EIALGMNFLhnMDPPLLHHDLKPENILLDNHFHVKISDFGLSK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DV-YSTDYYRVG-----GHTmlpIRWMPPESI--MYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECI-TQGr 614
Cdd:cd13978   144 LGmKSISANRRRgtenlGGT---PIYMAPEAFddFNKKPTSKSDVYSFAIVIWAVLT-RKEPFENAINPLLIMQIvSKG- 218
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1610576541 615 vlQRP------RTC----PQEVYELMLGCWQREPHMRKN 643
Cdd:cd13978   219 --DRPslddigRLKqienVQELISLMIRCWDGNPDARPT 255
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
388-647 5.93e-39

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 144.80  E-value: 5.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNlcpeQDkilVAVKTLKDASDN----ARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd14146     2 IGVGGFGKVYRATWKG----QE---VAVKAARQDPDEdikaTAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLR-AHGPDAVLMAEGNPPTELtqsqmLHIAQQIAAGMVYLASQHFV---HRDLATRNCLVGE--------N 531
Cdd:cd14146    75 ARGGTLNRALAaANAAPGPRRARRIPPHIL-----VNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLLEkiehddicN 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 532 LLVKIGDFGMSRDVYSTDYYRVGGhtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECIT 611
Cdd:cd14146   150 KTLKITDFGLAREWHRTTKMSAAG----TYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDGLAVAYGVA 224
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1610576541 612 QGRV-LQRPRTCPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14146   225 VNKLtLPIPSTCPEPFAKLMKECWEQDPHIRPSFALI 261
Pkinase pfam00069
Protein kinase domain;
383-641 1.40e-37

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 139.30  E-value: 1.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFLaeCYNLcpeQDKILVAVKTLK--DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:pfam00069   2 EVLRKLGSGSFGTVYK--AKHR---DTGKIVAIKKIKkeKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGmvyLASQHFVHRDLATRNclvgenllvkigdfg 540
Cdd:pfam00069  77 LEYVEGGSLFDLLSEKGA-------------FSEREAKFIMKQILEG---LESGSSLTTFVGTPW--------------- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 msrdvystdyyrvgghtmlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVLQR-- 618
Cdd:pfam00069 126 ----------------------YMAPEVLGGNPYGPKVDVWSLGCILYELLT-GKPPFPGINGNEIYELIIDQPYAFPel 182
                         250       260
                  ....*....|....*....|...
gi 1610576541 619 PRTCPQEVYELMLGCWQREPHMR 641
Cdd:pfam00069 183 PSNLSEEAKDLLKKLLKKDPSKR 205
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
388-647 1.59e-37

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 139.94  E-value: 1.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAeCYNlcPEQdkilVAVKTLKDASDNARKDfhreaelLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHG 467
Cdd:cd14059     1 LGSGAQGAVFLG-KFR--GEE----VAVKKVRDEKETDIKH-------LRKLNHPNIIKFKGVCTQAPCYCILMEYCPYG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 468 DLNKFLRAhgpdavlmaeGNpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDV-- 545
Cdd:cd14059    67 QLYEVLRA----------GR---EITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELse 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 546 YSTDYYRVGghtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECI-TQGRVLQRPRTCPQ 624
Cdd:cd14059   134 KSTKMSFAG-----TVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAIIWGVgSNSLQLPVPSTCPD 207
                         250       260
                  ....*....|....*....|...
gi 1610576541 625 EVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14059   208 GFKLLMKQCWNSKPRNRPSFRQI 230
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
381-649 2.88e-37

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 139.57  E-value: 2.88e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAecYNLCPEQdkiLVAVKTL--KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLI 458
Cdd:cd14003     1 NYELGKTLGEGSFGKVKLA--RHKLTGE---KVAIKIIdkSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGD 538
Cdd:cd14003    76 LVMEYASGGELFDYIVNNGR-------------LSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIID 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 539 FGMSRDVY----------STDYyrvgghtmlpirwMPPESIMYRKF-TTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVI 607
Cdd:cd14003   143 FGLSNEFRggsllktfcgTPAY-------------AAPEVLLGRKYdGPKADVWSLGVILYAMLT-GYLPFDDDNDSKLF 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 608 ECITQGRvLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHT 649
Cdd:cd14003   209 RKILKGK-YPIPSHLSPDARDLIRRMLVVDPSKRITIEEILN 249
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
388-597 4.79e-37

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 139.33  E-value: 4.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcpeQDKILVAVKTLKDASDNA-RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd14066     1 IGSGGFGTVYKGVL------ENGTVVAVKRLNEMNCAAsKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAHgpdavlmaEGNPPteLTQSQMLHIAQQIAAGMVYLASQHF---VHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd14066    75 GSLEDRLHCH--------KGSPP--LPWPQRLKIAKGIARGLEYLHEECPppiIHGDIKSSNILLDEDFEPKLTDFGLAR 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 544 D-VYSTDYYRVGGHTMLPIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQP 597
Cdd:cd14066   145 LiPPSESVSKTSAVKGTIG-YLAPEYIRTGRVSTKSDVYSFGVVLLELLT-GKPA 197
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
386-647 4.68e-36

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 136.07  E-value: 4.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECynlcpEQDKILVAVKTLKDA---SDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14007     6 KPLGKGKFGNVYLARE-----KKSGFIVALKVISKSqlqKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHGPDavlmaegnppTELTQSQMLhiaQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd14007    81 YAPNGELYKELKKQKRF----------DEKEAAKYI---YQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 rdVYSTDYYRvggHTML-PIRWMPPESIMYRKFTTESDVWSLGVVLWEiFTYGKQPWYQLSNNEVIECITQGRvLQRPRT 621
Cdd:cd14007   148 --VHAPSNRR---KTFCgTLDYLPPEMVEGKEYDYKVDIWSLGVLCYE-LLVGKPPFESKSHQETYKRIQNVD-IKFPSS 220
                         250       260
                  ....*....|....*....|....*.
gi 1610576541 622 CPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14007   221 VSPEAKDLISKLLQKDPSKRLSLEQV 246
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
388-659 4.99e-36

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 136.03  E-value: 4.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNlcpeqdkILVAVKTLKdaSDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHG 467
Cdd:cd14058     1 VGRGSFGVVCKARWRN-------QIVAVKIIE--SESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 468 DLNKFLraHGPDavlmaegnPPTELTQSQMLHIAQQIAAGMVYLAS---QHFVHRDLATRNCLV---GENLlvKIGDFGM 541
Cdd:cd14058    72 SLYNVL--HGKE--------PKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLtngGTVL--KICDFGT 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SRDVystdyyrvggHTML-----PIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQL--SNNEVIECITQGR 614
Cdd:cd14058   140 ACDI----------STHMtnnkgSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITR-RKPFDHIggPAFRIMWAVHNGE 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1610576541 615 VLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASP 659
Cdd:cd14058   209 RPPLIKNCPKPIESLMTRCWSKDPEKRPSMKEIVKIMSHLMQFFP 253
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
384-601 2.68e-35

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 133.87  E-value: 2.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECynlcpEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd05122     4 ILEKIGKGGFGVVYKARH-----KKTGQIVAIKKINLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd05122    79 CSGGSLKDLLKNTN------------KTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSA 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVYSTdyyrVGGHTML--PIrWMPPESIMYRKFTTESDVWSLGVVLWEIfTYGKQPWYQL 601
Cdd:cd05122   147 QLSDG----KTRNTFVgtPY-WMAPEVIQGKPYGFKADIWSLGITAIEM-AEGKPPYSEL 200
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
388-647 1.05e-34

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 132.60  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLCPEQ-DKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEgDPLIMVFEYMKH 466
Cdd:cd05037     7 LGQGTFTNIYDGILREVGDGRvQEVEVLLKVLDSDHRDISESFFETASLMSQISHKHLVKLYGVCVA-DENIMVQEYVRY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAHGpdavlmaeGNPPTeltqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV------GENLLVKIGDFG 540
Cdd:cd05037    86 GPLDKYLRRMG--------NNVPL----SWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLaregldGYPPFIKLSDPG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDVYSTDyYRVgghtmLPIRWMPPE--SIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQR 618
Cdd:cd05037   154 VPITVLSRE-ERV-----DRIPWIAPEclRNLQANLTIAADKWSFGTTLWEICSGGEEPLSALSSQEKLQFYEDQHQLPA 227
                         250       260
                  ....*....|....*....|....*....
gi 1610576541 619 PRtCPqEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd05037   228 PD-CA-ELAELIMQCWTYEPTKRPSFRAI 254
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
382-647 3.90e-34

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 131.32  E-value: 3.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKRELGEGAFGKVFLAecynLCPEQDkilVAVKTLKDASD----NARKDFHREAELLTNLQHEHIVKFYGVCVEGDPL 457
Cdd:cd14145     8 LVLEEIIGIGGFGKVYRA----IWIGDE---VAVKAARHDPDedisQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLNKflrahgpdaVLMAEGNPPTELtqsqmLHIAQQIAAGMVYLASQHFV---HRDLATRNCLVGE---- 530
Cdd:cd14145    81 CLVMEFARGGPLNR---------VLSGKRIPPDIL-----VNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILEkven 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 531 ----NLLVKIGDFGMSRDVYSTDYYRVGGhtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEV 606
Cdd:cd14145   147 gdlsNKILKITDFGLAREWHRTTKMSAAG----TYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFRGIDGLAV 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 607 IECITQGRV-LQRPRTCPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14145   222 AYGVAMNKLsLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNI 263
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
384-654 3.92e-34

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 131.30  E-value: 3.92e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECYNLcpeqdkiLVAVKTLKDASDN----ARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd14147     7 LEEVIGIGGFGKVYRGSWRGE-------LVAVKAARQDPDEdisvTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKflrahgpdaVLMAEGNPPTELtqsqmLHIAQQIAAGMVYLASQHFV---HRDLATRNCLVG------- 529
Cdd:cd14147    80 VMEYAAGGPLSR---------ALAGRRVPPHVL-----VNWAVQIARGMHYLHCEALVpviHRDLKSNNILLLqpiendd 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 530 -ENLLVKIGDFGMSRDVYSTDYYRVGGhtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIE 608
Cdd:cd14147   146 mEHKTLKITDFGLAREWHKTTQMSAAG----TYAWMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYRGIDCLAVAY 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1610576541 609 CITQGRV-LQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd14147   221 GVAVNKLtLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
388-647 4.04e-34

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 130.88  E-value: 4.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynLCPEQDkilVAVKTLKDASDN----ARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd14148     2 IGVGGFGKVYKG----LWRGEE---VAVKAARQDPDEdiavTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKflrahgpdaVLMAEGNPPTELtqsqmLHIAQQIAAGMVYLASQHFV---HRDLATRNCLVGE--------NL 532
Cdd:cd14148    75 ARGGALNR---------ALAGKKVPPHVL-----VNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILEpienddlsGK 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFGMSRDVYSTDYYRVGGhtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQ 612
Cdd:cd14148   141 TLKITDFGLAREWHKTTKMSAAG----TYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPYREIDALAVAYGVAM 215
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1610576541 613 GRV-LQRPRTCPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14148   216 NKLtLPIPSTCPEPFARLLEECWDPDPHGRPDFGSI 251
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
387-652 5.25e-34

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 130.42  E-value: 5.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAecYNLCPEQdkiLVAVKTLK--DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd06627     7 LIGRGAFGSVYKG--LNLNTGE---FVAIKQISleKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHGPdavlmaegnPPTELTQSQMlhiaQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS-- 542
Cdd:cd06627    82 ENGSLASIIKKFGK---------FPESLVAVYI----YQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVAtk 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 --------RDVYSTDYyrvgghtmlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGR 614
Cdd:cd06627   149 lnevekdeNSVVGTPY------------WMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPYYDLQPMAALFRIVQDD 215
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1610576541 615 VLQRPRTCPQEVYELMLGCWQREPHMRKNIKgihTLLQ 652
Cdd:cd06627   216 HPPLPENISPELRDFLLQCFQKDPTLRPSAK---ELLK 250
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
389-654 9.50e-34

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 129.31  E-value: 9.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 389 GEGAFGKVFLAECYNlcpeQDKiLVAVKTLKDasdnarkdFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGD 468
Cdd:cd14060     2 GGGSFGSVYRAIWVS----QDK-EVAVKKLLK--------IEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 469 LNKFLRAhgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYL---ASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDV 545
Cdd:cd14060    69 LFDYLNS-----------NESEEMDMDQIMTWATDIAKGMHYLhmeAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFH 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 546 YSTDYYRVGGhtMLPirWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECITQ-GRVLQRPRTCPQ 624
Cdd:cd14060   138 SHTTHMSLVG--TFP--WMAPEVIQSLPVSETCDTYSYGVVLWEMLTR-EVPFKGLEGLQVAWLVVEkNERPTIPSSCPR 212
                         250       260       270
                  ....*....|....*....|....*....|
gi 1610576541 625 EVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd14060   213 SFAELMRRCWEADVKERPSFKQIIGILESM 242
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
386-612 1.09e-33

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 130.76  E-value: 1.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECynLCPEQdkiLVAVKTLKdaSDNARKDFH----REAELLTNLQHEHIVKFYGVCVEGDP----- 456
Cdd:cd07840     5 AQIGEGTYGQVYKARN--KKTGE---LVALKKIR--MENEKEGFPitaiREIKLLQKLDHPNVVRLKEIVTSKGSakykg 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 -LIMVFEYMKHgDLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd07840    78 sIYMVFEYMDH-DLTGLLD------------NPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSR---DVYSTDY--------YRvgghtmlpirwmPPESIM-YRKFTTESDVWSLGVVLWEIFTygKQPWYQLSN 603
Cdd:cd07840   145 LADFGLARpytKENNADYtnrvitlwYR------------PPELLLgATRYGPEVDMWSVGCILAELFT--GKPIFQGKT 210
                         250
                  ....*....|
gi 1610576541 604 -NEVIECITQ 612
Cdd:cd07840   211 eLEQLEKIFE 220
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
383-613 1.29e-32

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 126.44  E-value: 1.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFLaeCYNLcpeQDKILVAVKTL--KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:cd05117     3 ELGKVLGRGSFGVVRL--AVHK---KTGEEYAVKIIdkKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV---GENLLVKIG 537
Cdd:cd05117    78 MELCTGGELFDRIVKKGS-------------FSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKII 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 538 DFGMSRDVYSTDYYR--VGghTMLpirWMPPESIMYRKFTTESDVWSLGVVLweiftY----GKQPWYQLSNNEVIECIT 611
Cdd:cd05117   145 DFGLAKIFEEGEKLKtvCG--TPY---YVAPEVLKGKGYGKKCDIWSLGVIL-----YillcGYPPFYGETEQELFEKIL 214

                  ..
gi 1610576541 612 QG 613
Cdd:cd05117   215 KG 216
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
388-641 3.00e-32

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 125.74  E-value: 3.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLaeCYNlcpEQDKILVAVKTLK--------------DASDNARKDFHREAELLTNLQHEHIVKFYGVC-- 451
Cdd:cd14008     1 LGRGSFGKVKL--ALD---TETGQLYAIKIFNksrlrkrregkndrGKIKNALDDVRREIAIMKKLDHPNIVRLYEVIdd 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 452 VEGDPLIMVFEYMKHGDLNKFLRAHGPDAvlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGEN 531
Cdd:cd14008    76 PESDKLYLVLEYCEGGPVMELDSGDRVPP-----------LPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTAD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 532 LLVKIGDFGMSRDV-YSTDYYRVGGHTMLpirWMPPE-----SIMYRKFTteSDVWSLGVVLWeIFTYGKQPWYQLSNNE 605
Cdd:cd14008   145 GTVKISDFGVSEMFeDGNDTLQKTAGTPA---FLAPElcdgdSKTYSGKA--ADIWALGVTLY-CLVFGRLPFNGDNILE 218
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1610576541 606 VIECI-TQGRVLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd14008   219 LYEAIqNQNDEFPIPPELSPELKDLLRRMLEKDPEKR 255
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
388-641 5.66e-32

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 124.82  E-value: 5.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecYNLcpeQDKILVAVKTLKDASDN-----ARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd06632     8 LGSGSFGSVYEG--FNG---DTGDFFAVKEVSLVDDDkksreSVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd06632    83 YVPGGSIHKLLQRYGA-------------FEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 RDVYSTDyyrvgghTMLPIR----WMPPESIMYR--KFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVL 616
Cdd:cd06632   150 KHVEAFS-------FAKSFKgspyWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMAT-GKPPWSQYEGVAAIFKIGNSGEL 221
                         250       260
                  ....*....|....*....|....*.
gi 1610576541 617 QR-PRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd06632   222 PPiPDHLSPDAKDFIRLCLQRDPEDR 247
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
388-641 1.53e-31

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 123.10  E-value: 1.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcpEQDKILVAVK--TLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd14009     1 IGRGSFATVWKGRH-----KQTGEVVAIKeiSRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV---GENLLVKIGDFGMS 542
Cdd:cd14009    76 GGDLSQYIRKRGR-------------LPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 RDVYSTDYyrvgGHTML--PIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPwYQLSNN-EVIECI-TQGRVLQR 618
Cdd:cd14009   143 RSLQPASM----AETLCgsPL-YMAPEILQFQKYDAKADLWSVGAILFEMLV-GKPP-FRGSNHvQLLRNIeRSDAVIPF 215
                         250       260
                  ....*....|....*....|....*
gi 1610576541 619 PRTCP--QEVYELMLGCWQREPHMR 641
Cdd:cd14009   216 PIAAQlsPDCKDLLRRLLRRDPAER 240
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
386-641 4.46e-31

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 122.08  E-value: 4.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLaeCYNLCPEQDkilVAVKTLKDASDN--ARKD---FHREAELLTNLQHEHIVKFYGvCVEGDPLIMV 460
Cdd:cd06625     6 KLLGQGAFGQVYL--CYDADTGRE---LAVKQVEIDPINteASKEvkaLECEIQLLKNLQHERIVQYYG-CLQDEKSLSI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 F-EYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd06625    80 FmEYMPGGSVKDEIKAYGA-------------LTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMS------------RDVYSTDYyrvgghtmlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVI 607
Cdd:cd06625   147 GASkrlqticsstgmKSVTGTPY------------WMSPEVINGEGYGRKADIWSVGCTVVEMLT-TKPPWAEFEPMAAI 213
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1610576541 608 ECI-TQGRVLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd06625   214 FKIaTQPTNPQLPPHVSEDARDFLSLIFVRNKKQR 248
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
386-654 6.31e-31

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 122.61  E-value: 6.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNLcpeqdkiLVAVKTLKDASDNA----RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd14158    21 NKLGEGGFGVVFKGYINDK-------NVAVKKLAAMVDIStedlTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNkflrahgpDAVLMAEGNPPteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd14158    94 TYMPNGSLL--------DRLACLNDTPP--LSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SR----DVYSTDYYRVGGHTMlpirWMPPESimYR-KFTTESDVWSLGVVLWEIFT------YGKQPWYQLSNNE----- 605
Cdd:cd14158   164 ARasekFSQTIMTERIVGTTA----YMAPEA--LRgEITPKSDIFSFGVVLLEIITglppvdENRDPQLLLDIKEeiede 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 606 --VIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd14158   238 ekTIEDYVDKKMGDWDSTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
388-592 6.69e-30

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 119.51  E-value: 6.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcpEQDKILVAVKTLKdaSDNARKDFH----REAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd07829     7 LGEGTYGVVYKAKD-----KKTGEIVALKKIR--LDNEEEGIPstalREISLLKELKHPNIVKLLDVIHTENKLYLVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHgDLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd07829    80 CDQ-DLKKYLD------------KRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLAR 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DV------YSTD----YYRvgghtmlpirwmPPESIM-YRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd07829   147 AFgiplrtYTHEvvtlWYR------------APEILLgSKHYSTAVDIWSVGCIFAELIT 194
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
388-641 7.86e-30

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 118.36  E-value: 7.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKdaSDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHG 467
Cdd:cd14065     1 LGKGFFGEVYKVT-----HRETGKVMVMKELK--RFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 468 DLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGE---NLLVKIGDFGMSRD 544
Cdd:cd14065    74 TLEELLK------------SMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREanrGRNAVVADFGLARE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 VysTDYYRVGGHTMLPIR------WMPPESIMYRKFTTESDVWSLGVVLWEIFT-YGKQPWYqLSNNEVIECITQGRVLQ 617
Cdd:cd14065   142 M--PDEKTKKPDRKKRLTvvgspyWMAPEMLRGESYDEKVDVFSFGIVLCEIIGrVPADPDY-LPRTMDFGLDVRAFRTL 218
                         250       260
                  ....*....|....*....|....
gi 1610576541 618 RPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd14065   219 YVPDCPPSFLPLAIRCCQLDPEKR 242
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
383-641 8.62e-30

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 118.68  E-value: 8.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFLAE-CYNLCPEQDKIL--VAVKTLKDasdNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd08222     3 RVVRKLGSGNFGTVYLVSdLKATADEELKVLkeISVGELQP---DETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLnkflrahgpDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLvKIGDF 539
Cdd:cd08222    80 VTEYCEGGDL---------DDKISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNVI-KVGDF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMSR------DVYS----TDYYrvgghtmlpirwMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIEC 609
Cdd:cd08222   150 GISRilmgtsDLATtftgTPYY------------MSPEVLKHEGYNSKSDIWSLGCILYEMCCL-KHAFDGQNLLSVMYK 216
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1610576541 610 ITQGRVLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd08222   217 IVEGETPSLPDKYSKELNAIYSRMLNKDPALR 248
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
384-653 1.23e-29

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 117.90  E-value: 1.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAEcynlcPEQDKILVAVK--TLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd08529     4 ILNKLGKGSFGVVYKVV-----RKVDGRVYALKqiDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAHgpdavlmaEGNPpteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd08529    79 EYAENGDLHSLIKSQ--------RGRP---LPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SRDVYSTDYYrvgGHTML--PIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVLQRP 619
Cdd:cd08529   148 AKILSDTTNF---AQTIVgtPY-YLSPELCEDKPYNEKSDVWALGCVLYELCT-GKHPFEAQNQGALILKIVRGKYPPIS 222
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1610576541 620 RTCPQEVYELMLGCWQREPHMRKNIKgihTLLQN 653
Cdd:cd08529   223 ASYSQDLSQLIDSCLTKDYRQRPDTT---ELLRN 253
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
388-655 1.61e-29

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 117.99  E-value: 1.61e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcPEQDKILVaVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHG 467
Cdd:cd14154     1 LGKGFFGQAIKVTH----RETGEVMV-MKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 468 DLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDV-- 545
Cdd:cd14154    76 TLKDVLK------------DMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIve 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 546 ---YSTDYYRVGG--HTMLPIR-----------WMPPESIMYRKFTTESDVWSLGVVLWEIFtyGK---QPWYqLSNNEV 606
Cdd:cd14154   144 erlPSGNMSPSETlrHLKSPDRkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEII--GRveaDPDY-LPRTKD 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1610576541 607 IECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLA 655
Cdd:cd14154   221 FGLNVDSFREKFCAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEALY 269
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
381-641 2.91e-29

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 117.31  E-value: 2.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAecynlCPEQDKILVAVKTLKDASD-NARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd06623     2 DLERVKVLGQGSSGVVYKV-----RHKPTGKIYALKKIHVDGDeEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHG--PDAVLMAegnppteltqsqmlhIAQQIAAGMVYLASQ-HFVHRDLATRNCLVGENLLVKI 536
Cdd:cd06623    77 VLEYMDGGSLADLLKKVGkiPEPVLAY---------------IARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSRDVYSTDYYR---VGGHTmlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPwYQLSNN----EVIEC 609
Cdd:cd06623   142 ADFGISKVLENTLDQCntfVGTVT-----YMSPERIQGESYSYAADIWSLGLTLLECAL-GKFP-FLPPGQpsffELMQA 214
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1610576541 610 ITQGRVL-QRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd06623   215 ICDGPPPsLPAEEFSPEFRDFISACLQKDPKKR 247
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
388-590 9.34e-29

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 115.39  E-value: 9.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecYNLcpeQDKILVAVKTLKDASDNARKDFhREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHG 467
Cdd:cd06614     8 IGEGASGEVYKA--TDR---ATGKEVAIKKMRLRKQNKELII-NEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 468 DLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYS 547
Cdd:cd06614    82 SLTDIITQN------------PVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTK 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1610576541 548 TDYYRvggHTML--PIrWMPPESIMYRKFTTESDVWSLGVVLWEI 590
Cdd:cd06614   150 EKSKR---NSVVgtPY-WMAPEVIKRKDYGPKVDIWSLGIMCIEM 190
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
383-647 5.27e-28

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 113.58  E-value: 5.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFLaeCYNLCPEqdkILVAVK--TLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:cd14069     4 DLVQTLGEGAFGEVFL--AVNRNTE---EAVAVKfvDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLnkFLRAHgPDaVLMAEgnppteltqsqmlHIAQ----QIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd14069    79 LEYASGGEL--FDKIE-PD-VGMPE-------------DVAQfyfqQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSrdvystDYYRVGGHTML------PIRWMPPESIMYRKFTTE-SDVWSLGVVLWEIFTyGKQPWYQLSNN--EVI 607
Cdd:cd14069   142 SDFGLA------TVFRYKGKERLlnkmcgTLPYVAPELLAKKKYRAEpVDVWSCGIVLFAMLA-GELPWDQPSDScqEYS 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1610576541 608 ECITQGRVLQRP-RTCPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14069   215 DWKENKKTYLTPwKKIDTAALSLLRKILTENPNKRITIEDI 255
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
409-651 8.61e-28

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 112.87  E-value: 8.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 409 DKILVAVKTLkDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRahgpdavlmaegNP 488
Cdd:cd13992    24 GGRTVAIKHI-TFSRTEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLL------------NR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 489 PTELTQSQMLHIAQQIAAGMVYLASQHF-VHRDLATRNCLVGENLLVKIGDFGMSRdVYSTDYYRVGGHTMLPIR--WMP 565
Cdd:cd13992    91 EIKMDWMFKSSFIKDIVKGMNYLHSSSIgYHGRLKSSNCLVDSRWVVKLTDFGLRN-LLEEQTNHQLDEDAQHKKllWTA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 566 PE----SIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNN-EVIECITQGRVLQRPR------TCPQEVYELMLGCW 634
Cdd:cd13992   170 PEllrgSLLEVRGTQKGDVYSFAIILYEILFR-SDPFALEREVaIVEKVISGGNKPFRPElavlldEFPPRLVLLVKQCW 248
                         250
                  ....*....|....*..
gi 1610576541 635 QREPHMRKNIKGIHTLL 651
Cdd:cd13992   249 AENPEKRPSFKQIKKTL 265
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
386-604 9.60e-28

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 112.78  E-value: 9.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLaeCYNLcpeQDKILVAVKTLK--DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd06626     6 NKIGEGTFGKVYT--AVNL---DTGELMAMKEIRfqDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRaHG---PDAVLMAegnppteltqsqmlhIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd06626    81 CQEGTLEELLR-HGrilDEAVIRV---------------YTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFG 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDVYSTDYYRVGG---HTMLPIRWMPPESIMYRKFTTE---SDVWSLGVVLWEIFTyGKQPWYQLSNN 604
Cdd:cd06626   145 SAVKLKNNTTTMAPGevnSLVGTPAYMAPEVITGNKGEGHgraADIWSLGCVVLEMAT-GKRPWSELDNE 213
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
384-587 2.25e-27

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 111.51  E-value: 2.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECYNlcpEQDKILVAVKTL--KDASDNARKDF-HREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:cd14080     4 LGKTIGEGSYSKVKLAEYTK---SGLKEKVACKIIdkKKAPKDFLEKFlPRELEILRKLRHPNIIQVYSIFERGSKVFIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd14080    81 MEYAEHGDLLEYIQKRGA-------------LSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFG 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 541 MSRDVYSTDyyrvggHTML------PIRWMPPE---SIMYRKFTteSDVWSLGVVL 587
Cdd:cd14080   148 FARLCPDDD------GDVLsktfcgSAAYAAPEilqGIPYDPKK--YDIWSLGVIL 195
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
388-652 4.21e-27

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 110.56  E-value: 4.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLcpeqdkilVAVKTLK--DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEgDPLIMVFEYMK 465
Cdd:cd14062     1 IGSGSFGTVYKGRWHGD--------VAVKKLNvtDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTK-PQLAIVTQWCE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMsrdv 545
Cdd:cd14062    72 GSSLYKHLHVL------------ETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGL---- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 546 ySTDYYRVGGHTMLP-----IRWMPPESIMYRK---FTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIeCITQGRVLQ 617
Cdd:cd14062   136 -ATVKTRWSGSQQFEqptgsILWMAPEVIRMQDenpYSFQSDVYAFGIVLYELLT-GQLPYSHINNRDQI-LFMVGRGYL 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1610576541 618 RP------RTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQ 652
Cdd:cd14062   213 RPdlskvrSDTPKALRRLMEDCIKFQRDERPLFPQILASLE 253
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
376-592 7.11e-27

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 111.64  E-value: 7.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 376 HIKRHNIVLKreLGEGAFGKVFLAECynlcpEQDKILVAVKtlKDASDNARKDFH----REAELLTNLQHEHIVKFYGVC 451
Cdd:cd07866     6 KLRDYEILGK--LGEGTFGEVYKARQ-----IKTGRVVALK--KILMHNEKDGFPitalREIKILKKLKHPNVVPLIDMA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 452 VE------GDPLI--MVFEYMKHgDLNKFLrahgpdavlmaeGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLAT 523
Cdd:cd07866    77 VErpdkskRKRGSvyMVTPYMDH-DLSGLL------------ENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 524 RNCLVGENLLVKIGDFGMSRdVYSTDYYRVGGH---------TMLPIRWM-PPESIM-YRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd07866   144 ANILIDNQGILKIADFGLAR-PYDGPPPNPKGGggggtrkytNLVVTRWYrPPELLLgERRYTTAVDIWGIGCVFAEMFT 222
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
388-641 1.06e-26

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 109.78  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecYNLCPEQdkiLVAVK------TLKDASDNARKD----FHREAELLTNLQHEHIVKFYGvCVEGDPL 457
Cdd:cd06629     9 IGKGTYGRVYLA--MNATTGE---MLAVKqvelpkTSSDRADSRQKTvvdaLKSEIDTLKDLDHPNIVQYLG-FEETEDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVF-EYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd06629    83 FSIFlEYVPGGSIGSCLRKYGK-------------FEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSR---DVYSTDyyrvGGHTML-PIRWMPPESIMYRK--FTTESDVWSLGVVLWEIFTyGKQPWyqlSNNEVIECI 610
Cdd:cd06629   150 SDFGISKksdDIYGNN----GATSMQgSVFWMAPEVIHSQGqgYSAKVDIWSLGCVVLEMLA-GRRPW---SDDEAIAAM 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1610576541 611 TQ-GRVLQRPRTCP-----QEVYELMLGCWQREPHMR 641
Cdd:cd06629   222 FKlGNKRSAPPVPEdvnlsPEALDFLNACFAIDPRDR 258
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
381-648 1.08e-26

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 109.67  E-value: 1.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAECynlcpEQDKILVAVKTLK--DASD-NARKDFHREAELLTNLQHEHIVKFYGVCVEGDPL 457
Cdd:cd08224     1 NYEIEKKIGKGQFSVVYRARC-----LLDGRLVALKKVQifEMMDaKARQDCLKEIDLLQQLNHPNIIKYLASFIENNEL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLNKFLRAHGPDAVLMAEGnppteltqsQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd08224    76 NIVLELADAGDLSRLIKHFKKQKRLIPER---------TIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 538 DFGMSRdVYS-----------TDYYrvgghtmlpirwMPPESIMYRKFTTESDVWSLGVVLWEIFT-----YG-KQPWYQ 600
Cdd:cd08224   147 DLGLGR-FFSskttaahslvgTPYY------------MSPERIREQGYDFKSDIWSLGCLLYEMAAlqspfYGeKMNLYS 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1610576541 601 LSNNeviecITQGRVLQRPRTC-PQEVYELMLGCWQREPHMRKNIKGIH 648
Cdd:cd08224   214 LCKK-----IEKCEYPPLPADLySQELRDLVAACIQPDPEKRPDISYVL 257
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
388-647 1.21e-26

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 109.51  E-value: 1.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLaecynlCPEQDKILVAVKTLKDASDNA--RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd14027     1 LDSGGFGKVSL------CFHRTQGLVVLKTVYTGPNCIehNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYME 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAhgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM-SRD 544
Cdd:cd14027    75 KGNLMHVLKK--------------VSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLaSFK 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 VYS-------------TDYYRVGGHTMLpirWMPPESI--MYRKFTTESDVWSLGVVLWEIFTyGKQPWYQ-LSNNEVIE 608
Cdd:cd14027   141 MWSkltkeehneqrevDGTAKKNAGTLY---YMAPEHLndVNAKPTEKSDVYSFAIVLWAIFA-NKEPYENaINEDQIIM 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 609 CITQGR---VLQRPRTCPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14027   217 CIKSGNrpdVDDITEYCPREIIDLMKLCWEANPEARPTFPGI 258
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
388-641 1.59e-26

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 109.16  E-value: 1.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynlCPEQDKILVAVKTLKDASDNARKD---------FHREAELLTNLQHEHIVKFYGVCVEGDPLI 458
Cdd:cd06628     8 IGSGSFGSVYLG-----MNASSGELMAVKQVELPSVSAENKdrkksmldaLQREIALLRELQHENIVQYLGSSSDANHLN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGD 538
Cdd:cd06628    83 IFLEYVPGGSVATLLNNYG-------------AFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 539 FGMSRDV--YSTDYYRVGGHTML--PIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGR 614
Cdd:cd06628   150 FGISKKLeaNSLSTKNNGARPSLqgSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFPDCTQMQAIFKIGENA 228
                         250       260
                  ....*....|....*....|....*..
gi 1610576541 615 VLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd06628   229 SPTIPSNISSEARDFLEKTFEIDHNKR 255
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
386-641 4.82e-26

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 107.32  E-value: 4.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLaeCYNLCPEQdkiLVAVKTLKDASDNARKDFhREAELLTNL----QHEHIVKFYGVC--VEGDPLIM 459
Cdd:cd05118     5 RKIGEGAFGTVWL--ARDKVTGE---KVAIKKIKNDFRHPKAAL-REIKLLKHLndveGHPNIVKLLDVFehRGGNHLCL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHgDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV-GENLLVKIGD 538
Cdd:cd05118    79 VFELMGM-NLYELIKDY------------PRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILInLELGQLKLAD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 539 FGMSRDVYSTDYYrvggHTMLPIRWMPPESIMYRKFTTES-DVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITqgRVLQ 617
Cdd:cd05118   146 FGLARSFTSPPYT----PYVATRWYRAPEVLLGAKPYGSSiDIWSLGCILAELLT-GRPLFPGDSEVDQLAKIV--RLLG 218
                         250       260
                  ....*....|....*....|....
gi 1610576541 618 rprtcPQEVYELMLGCWQREPHMR 641
Cdd:cd05118   219 -----TPEALDLLSKMLKYDPAKR 237
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
386-647 6.05e-26

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 107.58  E-value: 6.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLA-------ECYNLCPEQdkilvavkTLKDASDnaRKDFHREAELLTNLQHEHIVKFYGVCveGDPLI 458
Cdd:cd14025     2 EKVGSGGFGQVYKVrhkhwktWLAIKCPPS--------LHVDDSE--RMELLEEAKKMEMAKFRHILPVYGIC--SEPVG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLRAHgpdavlmaegNPPTELtQSQMLHiaqQIAAGMVYLASQH--FVHRDLATRNCLVGENLLVKI 536
Cdd:cd14025    70 LVMEYMETGSLEKLLASE----------PLPWEL-RFRIIH---ETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKI 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSR---DVYSTDYYRVGGHTMlpIRWMPPESIMY--RKFTTESDVWSLGVVLWEIFTYgKQPWYQLSN-NEVIECI 610
Cdd:cd14025   136 SDFGLAKwngLSHSHDLSRDGLRGT--IAYLPPERFKEknRCPDTKHDVYSFAIVIWGILTQ-KKPFAGENNiLHIMVKV 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1610576541 611 TQGR-------VLQRPRTCpQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14025   213 VKGHrpslspiPRQRPSEC-QQMICLMKRCWDQDPRKRPTFQDI 255
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
382-641 6.88e-26

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 107.43  E-value: 6.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKRELGEGAFGKVFLAECYNLcpeqdkilVAVKTLKDASDNARKD--FHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd14063     2 LEIKEVIGKGRFGRVHRGRWHGD--------VAIKLLNIDYLNEEQLeaFKEEVAAYKNTRHDNLVLFMGACMDPPHLAI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVgENLLVKIGDF 539
Cdd:cd14063    74 VTSLCKGRTLYSLIHER------------KEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGRVVITDF 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMSRDVYSTDYYRVGGHTMLPIRWMP---PESImyRK------------FTTESDVWSLGVVLWEI----FTYGKQPWyq 600
Cdd:cd14063   141 GLFSLSGLLQPGRREDTLVIPNGWLCylaPEII--RAlspdldfeeslpFTKASDVYAFGTVWYELlagrWPFKEQPA-- 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1610576541 601 lsnnEVIecITQ-GRVLQRPRT---CPQEVYELMLGCWQREPHMR 641
Cdd:cd14063   217 ----ESI--IWQvGCGKKQSLSqldIGREVKDILMQCWAYDPEKR 255
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
377-598 8.50e-26

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 107.91  E-value: 8.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCV-EG 454
Cdd:cd06620     2 LKNQDLETLKDLGAGNGGSVSKVL-----HIPTGTIMAKKVIHiDAKSSVRKQILRELQILHECHSPYIVSFYGAFLnEN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQH-FVHRDLATRNCLVGENLL 533
Cdd:cd06620    77 NNIIICMEYMDCGSLDKILKKKGP-------------FPEEVLGKIAVAVLEGLTYLYNVHrIIHRDIKPSNILVNSKGQ 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 534 VKIGDFGMSRDVYST--DYYrVGGHTmlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd06620   144 IKLCDFGVSGELINSiaDTF-VGTST-----YMSPERIQGGKYSVKSDVWSLGLSIIELAL-GEFPF 203
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
382-647 1.08e-25

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 106.71  E-value: 1.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKReLGEGAFGKVFLAEcynlcPEQDKILVAVK--TLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd08530     3 KVLKK-LGKGSYGSVYKVK-----RLSDNQVYALKevNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHgpdavlMAEGNPpteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd08530    77 VMEYAPFGDLSKLISKR------KKKRRL---FPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMSRDVYSTDYYRVGGHTMlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVLQRP 619
Cdd:cd08530   148 GISKVLKKNLAKTQIGTPL----YAAPEVWKGRPYDYKSDIWSLGCLLYEMAT-FRPPFEARTMQELRYKVCRGKFPPIP 222
                         250       260
                  ....*....|....*....|....*...
gi 1610576541 620 RTCPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd08530   223 PVYSQDLQQIIRSLLQVNPKKRPSCDKL 250
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
388-591 3.89e-25

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 105.45  E-value: 3.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynlCPEQDKILVAVKT--LKDASDNARKDFhREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd13996    14 LGSGGFGSVYKV-----RNKVDGVTYAIKKirLTEKSSASEKVL-REVKALAKLNHPNIVRYYTAWVEEPPLYIQMELCE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRahgpdavlmaEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV-GENLLVKIGDFGMSRD 544
Cdd:cd13996    88 GGTLRDWID----------RRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLdNDDLQVKIGDFGLATS 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 545 VY---------------STDYYRVGGHTMLpirWMPPESIMYRKFTTESDVWSLGVVLWEIF 591
Cdd:cd13996   158 IGnqkrelnnlnnnnngNTSNNSVGIGTPL---YASPEQLDGENYNEKADIYSLGIILFEML 216
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
387-641 4.78e-25

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 105.21  E-value: 4.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd06611    12 ELGDGAFGKVYKAQ-----HKETGLFAAAKIIQIESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLnkflrahgpDAVLMAEGNPpteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVY 546
Cdd:cd06611    87 GAL---------DSIMLELERG---LTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 547 STDYYRvggHTML--PiRWMPPESIMYRKFTTE-----SDVWSLGVVLWEIfTYGKQPWYQLSNNEVIECITQGR--VLQ 617
Cdd:cd06611   155 STLQKR---DTFIgtP-YWMAPEVVACETFKDNpydykADIWSLGITLIEL-AQMEPPHHELNPMRVLLKILKSEppTLD 229
                         250       260
                  ....*....|....*....|....
gi 1610576541 618 RPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd06611   230 QPSKWSSSFNDFLKSCLVKDPDDR 253
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
380-614 6.06e-25

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 104.39  E-value: 6.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 380 HNIVLKRELGEGAFGKVFLAEcynlcpEQDKI-LVAVKTLKDASDNARKD---FHREAELLTNLQHEHIVKFYGVCVEGD 455
Cdd:cd14073     1 HRYELLETLGKGTYGKVKLAI------ERATGrEVAIKSIKKDKIEDEQDmvrIRREIEIMSSLNHPHIIRIYEVFENKD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd14073    75 KIVIVMEYASGGELYDYISERR-------------RLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAK 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSrDVYSTDYYRvggHTML--PIrWMPPESIMYRKFT-TESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECITQ 612
Cdd:cd14073   142 IADFGLS-NLYSKDKLL---QTFCgsPL-YASPEIVNGTPYQgPEVDCWSLGVLLY-TLVYGTMPFDGSDFKRLVKQISS 215

                  ..
gi 1610576541 613 GR 614
Cdd:cd14073   216 GD 217
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
389-641 1.45e-24

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 103.10  E-value: 1.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 389 GEGAFGKVFLAEcynlcPEQDKILVAVK--TLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYmKH 466
Cdd:cd14002    10 GEGSFGKVYKGR-----RKYTGQVVALKfiPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEY-AQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKflrahgpdaVLMAEGNPPTELTQSqmlhIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVY 546
Cdd:cd14002    84 GELFQ---------ILEDDGTLPEEEVRS----IAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 547 StdyyrvggHTML-------PIrWMPPESIMYRKFTTESDVWSLGVVLWEIFtYGKQPWYQLSNNEVIECITQGRVlQRP 619
Cdd:cd14002   151 C--------NTLVltsikgtPL-YMAPELVQEQPYDHTADLWSLGCILYELF-VGQPPFYTNSIYQLVQMIVKDPV-KWP 219
                         250       260
                  ....*....|....*....|..
gi 1610576541 620 RTCPQEVYELMLGCWQREPHMR 641
Cdd:cd14002   220 SNMSPEFKSFLQGLLNKDPSKR 241
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
388-647 1.71e-24

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 103.49  E-value: 1.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLCP--EQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd05078     7 LGQGTFTKIFKGIRREVGDygQLHETEVLLKVLDKAHRNYSESFFEAASMMSQLSHKHLVLNYGVCVCGDENILVQEYVK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHGPDAVLMAEgnppteltqsqmLHIAQQIAAGMVYLASQHFVHRDLATRNCLV--------GENLLVKIG 537
Cdd:cd05078    87 FGSLDTYLKKNKNCINILWK------------LEVAKQLAWAMHFLEEKTLVHGNVCAKNILLireedrktGNPPFIKLS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 538 DFGMSRDVYSTDYYrvgghtMLPIRWMPPESIMY-RKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVL 616
Cdd:cd05078   155 DPGISITVLPKDIL------LERIPWVPPECIENpKNLSLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQL 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1610576541 617 QRPRTCpqEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd05078   229 PAPKWT--ELANLINNCMDYEPDHRPSFRAI 257
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
384-592 1.83e-24

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 104.91  E-value: 1.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAEcYNLCPEQdkilVAVKTLKDASDN---ARKDFhREAELLTNLQHEHIVKFYGVCVEGDP---- 456
Cdd:cd07834     4 LLKPIGSGAYGVVCSAY-DKRTGRK----VAIKKISNVFDDlidAKRIL-REIKILRHLKHENIIGLLDILRPPSPeefn 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 -LIMVFEYMKHgDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd07834    78 dVYIVTELMET-DLHKVIKSPQP-------------LTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLK 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSRDVYS-------TDY-----YRvgghtmlpirwmPPESIM-YRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd07834   144 ICDFGLARGVDPdedkgflTEYvvtrwYR------------APELLLsSKKYTKAIDIWSVGCIFAELLT 201
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
388-641 2.02e-24

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 103.29  E-value: 2.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynLCPEQDkiLVAVKTLK-DASD--NARKDF---HREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd06631     9 LGKGAYGTVYCG----LTSTGQ--LIAVKQVElDTSDkeKAEKEYeklQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd06631    83 EFVPGGSIASILARFGA-------------LEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGC 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SRDVysTDYYRVGGHTML--PIR----WMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGR- 614
Cdd:cd06631   150 AKRL--CINLSSGSQSQLlkSMRgtpyWMAPEVINETGHGRKSDIWSIGCTVFEMAT-GKPPWADMNPMAAIFAIGSGRk 226
                         250       260
                  ....*....|....*....|....*...
gi 1610576541 615 -VLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd06631   227 pVPRLPDKFSPEARDFVHACLTRDQDER 254
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
388-590 3.09e-24

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 103.18  E-value: 3.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecYNLcpEQDKIlVAVK--TLKDASDNARKDFHREAELLTNLQ-HEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd07832     8 IGEGAHGIVFKA--KDR--ETGET-VALKkvALRKLEGGIPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFEYM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHgDLNKFLRAhgpdavlmaEGNPpteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRd 544
Cdd:cd07832    83 LS-SLSEVLRD---------EERP---LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLAR- 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1610576541 545 VYSTDYYRVGGHTMLPIRWMPPEsIMY--RKFTTESDVWSLGVVLWEI 590
Cdd:cd07832   149 LFSEEDPRLYSHQVATRWYRAPE-LLYgsRKYDEGVDLWAVGCIFAEL 195
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
383-592 3.56e-24

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 103.00  E-value: 3.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFLAeCYNLCPEqdkiLVAVKTLKdasdnarKDFH--------REAELLTNLQ-HEHIVKFYGVCVE 453
Cdd:cd07830     2 KVIKQLGDGTFGSVYLA-RNKETGE----LVAIKKMK-------KKFYsweecmnlREVKSLRKLNeHPNIVKLKEVFRE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMKhGDLNKFLRAHgpdavlmaEGNPpteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL 533
Cdd:cd07830    70 NDELYFVFEYME-GNLYQLMKDR--------KGKP---FSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEV 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 534 VKIGDFGMSRDVYS----TDY-----YRVgghtmlpirwmpPEsIMYR--KFTTESDVWSLGVVLWEIFT 592
Cdd:cd07830   138 VKIADFGLAREIRSrppyTDYvstrwYRA------------PE-ILLRstSYSSPVDIWALGCIMAELYT 194
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
387-644 6.27e-24

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 101.69  E-value: 6.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcYnlCPEQdkilVAVKTLKDASDNA--RKDFHREAELLtNLQHEHIVKFYG---VCVEGDPLIMVF 461
Cdd:cd13979    10 PLGSGGFGSVYKAT-Y--KGET----VAVKIVRRRRKNRasRQSFWAELNAA-RLRHENIVRVLAaetGTDFASLGLIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKflrahgpdavLMAEGNPPteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd13979    82 EYCGNGTLQQ----------LIYEGSEP--LPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGC 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SR-----DVYSTDYYRVGGhtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW--------YQLSNNEV-- 606
Cdd:cd13979   150 SVklgegNEVGTPRSHIGG----TYTYRAPELLKGERVTPKADIYSFGITLWQMLT-RELPYaglrqhvlYAVVAKDLrp 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 607 ----IECITQGRVLQRPRTCpqevyelmlgCWQREPHMRKNI 644
Cdd:cd13979   225 dlsgLEDSEFGQRLRSLISR----------CWSAQPAERPNA 256
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
388-652 1.35e-23

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 100.68  E-value: 1.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNlcpeqdKIlVAVKTLKDASDNARKD---FHREAELLTNLQHEHIVKFYGVCVEgDP--LIMVFE 462
Cdd:cd14064     1 IGSGSFGKVYKGRCRN------KI-VAIKRYRANTYCSKSDvdmFCREVSILCRLNHPCVIQFVGACLD-DPsqFAIVTQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLnkFLRAHGPDAVLmaegNPPTELTqsqmlhIAQQIAAGMVYL--ASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd14064    73 YVSGGSL--FSLLHEQKRVI----DLQSKLI------IAVDVAKGMEYLhnLTQPIIHRDLNSHNILLYEDGHAVVADFG 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDVYSTDYYRVgghTMLP--IRWMPPESIMY-RKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVlq 617
Cdd:cd14064   141 ESRFLQSLDEDNM---TKQPgnLRWMAPEVFTQcTRYSIKADVFSYALCLWELLT-GEIPFAHLKPAAAAADMAYHHI-- 214
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1610576541 618 RP---RTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQ 652
Cdd:cd14064   215 RPpigYSIPKPISSLLMRGWNAEPESRPSFVEIVALLE 252
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
386-621 2.61e-23

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 100.38  E-value: 2.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNLcpeqdKILVAVKTLKDAS---DNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14026     3 RYLSRGAFGTVSRARHADW-----RVTVAIKCLKLDSpvgDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLraHGPDAVlmaegnppTELTQSQMLHIAQQIAAGMVYL--ASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd14026    78 YMTNGSLNELL--HEKDIY--------PDVAWPLRLRILYEIALGVNYLhnMSPPLLHHDLKTQNILLDGEFHVKIADFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSR-DVYSTDYYRvgGHTMLP----IRWMPPESI---MYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNN-EVIECIT 611
Cdd:cd14026   148 LSKwRQLSISQSR--SSKSAPeggtIIYMPPEEYepsQKRRASVKHDIYSYAIIMWEVLSR-KIPFEEVTNPlQIMYSVS 224
                         250
                  ....*....|
gi 1610576541 612 QGrvlQRPRT 621
Cdd:cd14026   225 QG---HRPDT 231
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
386-647 2.93e-23

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 99.65  E-value: 2.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNlcpEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd08225     6 KKIGEGSFGKIYLAKAKS---DSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFL-RAHGpdaVLMAEgnppteltqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV-KIGDFGMSR 543
Cdd:cd08225    83 GGDLMKRInRQRG---VLFSE---------DQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIAR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVY-STDYYRVGGHTmlPIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECITQGRVLQRPRTC 622
Cdd:cd08225   151 QLNdSMELAYTCVGT--PY-YLSPEICQNRPYNNKTDIWSLGCVLYELCTL-KHPFEGNNLHQLVLKICQGYFAPISPNF 226
                         250       260
                  ....*....|....*....|....*
gi 1610576541 623 PQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd08225   227 SRDLRSLISQLFKVSPRDRPSITSI 251
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
388-597 4.21e-23

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 100.29  E-value: 4.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNlcpeqdkILVAVKTLKDASD----NARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd14159     1 IGEGGFGCVYQAVMRN-------TEYAVKRLKEDSEldwsVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGpdavlmaeGNPPteLTQSQMLHIAQQIAAGMVYL--ASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd14159    74 LPNGSLEDRLHCQV--------SCPC--LSWSQRLHVLLGTARAIQYLhsDSPSLIHGDVKSSNILLDAALNPKLGDFGL 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 542 ---SRDVYSTDYYRVGGHTML---PIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQP 597
Cdd:cd14159   144 arfSRRPKQPGMSSTLARTQTvrgTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLT-GRRA 204
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
388-598 7.20e-23

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 98.53  E-value: 7.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflaECYNLCPEQDKILVAVKTL-KDASDNARKDFH----REAELLTNLQHEHIVKFYGVCV-EGDPLIMVF 461
Cdd:cd13994     1 IGKGATSVV---RIVTKKNPRSGVLYAVKEYrRRDDESKRKDYVkrltSEYIISSKLHHPNIVKVLDLCQdLHGKWCLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKflrahgpdavLMAEGNPPTELTQSQMLhiaQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG- 540
Cdd:cd13994    78 EYCPGGDLFT----------LIEKADSLSLEEKDCFF---KQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGt 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 541 -------------MSRDVYSTDYYrvgghtmlpirwMPPESIMYRKFTTES-DVWSLGVVLWEIFTyGKQPW 598
Cdd:cd13994   145 aevfgmpaekespMSAGLCGSEPY------------MAPEVFTSGSYDGRAvDVWSCGIVLFALFT-GRFPW 203
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
388-598 1.02e-22

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 98.23  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLaeCYNLCPEQDKILVAVKTLKDASDNARK--DFHREAELLTNLQHEHIVKFYGvCVE--GDPLIMVF-E 462
Cdd:cd06651    15 LGQGAFGRVYL--CYDVDTGRELAAKQVQFDPESPETSKEvsALECEIQLLKNLQHERIVQYYG-CLRdrAEKTLTIFmE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd06651    92 YMPGGSVKDQLKAYGA-------------LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAS 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 543 RDVYSTDYYRVGGHTMLPI-RWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPW 598
Cdd:cd06651   159 KRLQTICMSGTGIRSVTGTpYWMSPEVISGEGYGRKADVWSLGCTVVEMLTE-KPPW 214
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
381-601 1.08e-22

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 98.19  E-value: 1.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLaeCYNLCPEQDKILVAVKTLKDASDNARK--DFHREAELLTNLQHEHIVKFYGvCVEGDP-- 456
Cdd:cd06652     3 NWRLGKLLGQGAFGRVYL--CYDADTGRELAVKQVQFDPESPETSKEvnALECEIQLLKNLLHERIVQYYG-CLRDPQer 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 -LIMVFEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd06652    80 tLSIFMEYMPGGSIKDQLKSYGA-------------LTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVK 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSRDVYSTdyyRVGGHTMLPIR----WMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQL 601
Cdd:cd06652   147 LGDFGASKRLQTI---CLSGTGMKSVTgtpyWMSPEVISGEGYGRKADIWSVGCTVVEMLTE-KPPWAEF 212
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
387-590 1.89e-22

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 97.79  E-value: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd06643    12 ELGDGAFGKVYKAQ-----NKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLnkflrahgpDAVLMAEGNPpteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS---- 542
Cdd:cd06643    87 GAV---------DAVMLELERP---LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSaknt 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 543 -----RDVYSTDYYrvgghtmlpirWMPPESIMY-----RKFTTESDVWSLGVVLWEI 590
Cdd:cd06643   155 rtlqrRDSFIGTPY-----------WMAPEVVMCetskdRPYDYKADVWSLGVTLIEM 201
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
379-613 1.95e-22

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 97.33  E-value: 1.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAEcynlcpEQDKILVAVKTL-KDASDNARKDFH--REAELLTNLQHEHIVKFYGVCVEGD 455
Cdd:cd14161     2 KHRYEFLETLGKGTYGRVKKAR------DSSGRLVAIKSIrKDRIKDEQDLLHirREIEIMSSLNHPHIISVYEVFENSS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd14161    76 KIVIVMEYASRGDLYDYISERQR-------------LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIK 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610576541 536 IGDFGMSrDVYSTDYYrVGGHTMLPIrWMPPESIMYRKFT-TESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECITQG 613
Cdd:cd14161   143 IADFGLS-NLYNQDKF-LQTYCGSPL-YASPEIVNGRPYIgPEVDSWSLGVLLY-ILVHGTMPFDGHDYKILVKQISSG 217
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
388-601 2.00e-22

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 96.95  E-value: 2.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcpEQDKILVAVKTLKDASDNarKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHG 467
Cdd:cd06612    11 LGEGSYGSVYKAIH-----KETGQVVAIKVVPVEEDL--QEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCGAG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 468 DLNKFLRAHGpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYS 547
Cdd:cd06612    84 SVSDIMKITN------------KTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTD 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 548 TDYYRvggHTML--PIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQL 601
Cdd:cd06612   152 TMAKR---NTVIgtPF-WMAPEVIQEIGYNNKADIWSLGITAIEMAE-GKPPYSDI 202
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
388-590 2.32e-22

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 97.33  E-value: 2.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYnlcpEQDKILVaVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHG 467
Cdd:cd14221     1 LGKGCFGQAIKVTHR----ETGEVMV-MKELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 468 DLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYS 547
Cdd:cd14221    76 TLRGIIK------------SMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVD 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 548 TDYYRVGGHTML-PIR-----------WMPPESIMYRKFTTESDVWSLGVVLWEI 590
Cdd:cd14221   144 EKTQPEGLRSLKkPDRkkrytvvgnpyWMAPEMINGRSYDEKVDVFSFGIVLCEI 198
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
381-588 4.62e-22

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 96.18  E-value: 4.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAEcYNLCPEQdkilVAVKTLK----DASDNARKdFHREAELLTNLQHEHIVKFYGVCVEGDP 456
Cdd:cd14079     3 NYILGKTLGVGSFGKVKLAE-HELTGHK----VAVKILNrqkiKSLDMEEK-IRREIQILKLFRHPHIIRLYEVIETPTD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd14079    77 IFMVMEYVSGGELFDYIVQKG-------------RLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKI 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 537 GDFGMSRDVYSTDYYRVGGHTmlPiRWMPPESIMYRKFT-TESDVWSLGVVLW 588
Cdd:cd14079   144 ADFGLSNIMRDGEFLKTSCGS--P-NYAAPEVISGKLYAgPEVDVWSCGVILY 193
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
388-641 5.02e-22

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 95.90  E-value: 5.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcPEQDKILVAVKTLKDASDNARKDF-HREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd14120     1 IGHGAFAVVFKGRH----RKKPDLPVAIKCITKKNLSKSQNLlGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV---------GENLLVKIG 537
Cdd:cd14120    77 GDLADYLQAKG-------------TLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLshnsgrkpsPNDIRLKIA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 538 DFGMSRDVYSTDY-YRVGGHTMlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVL 616
Cdd:cd14120   144 DFGFARFLQDGMMaATLCGSPM----YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQELKAFYEKNANL 218
                         250       260
                  ....*....|....*....|....*..
gi 1610576541 617 QR--PRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd14120   219 RPniPSGTSPALKDLLLGLLKRNPKDR 245
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
387-665 6.09e-22

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 96.29  E-value: 6.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAECYNlcpEQDKILVAVKTLKDASDNArKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd06641    11 KIGKGSFGEVFKGIDNR---TQKVVAIKIIDLEEAEDEI-EDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRahgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVY 546
Cdd:cd06641    87 GSALDLLE--------------PGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 547 STDYYRvGGHTMLPIrWMPPESIMYRKFTTESDVWSLGVVLWEIfTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEV 626
Cdd:cd06641   153 DTQIKR-N*FVGTPF-WMAPEVIKQSAYDSKADIWSLGITAIEL-ARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPL 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1610576541 627 YELMLGCWQREPHMRKNIKGI--HTLLQNLAKASPVYLDIL 665
Cdd:cd06641   230 KEFVEACLNKEPSFRPTAKELlkHKFILRNAKKTSYLTELI 270
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
391-641 6.48e-22

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 96.63  E-value: 6.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 391 GAFGKVFLAECynlcpeqDKILVAVKTL----KDASDNARKDFHreaelLTNLQHEHIVKFYGVCVEGDPLI----MVFE 462
Cdd:cd14053     6 GRFGAVWKAQY-------LNRLVAVKIFplqeKQSWLTEREIYS-----LPGMKHENILQFIGAEKHGESLEaeywLITE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYL-------ASQH---FVHRDLATRNCLVGENL 532
Cdd:cd14053    74 FHERGSLCDYLKGN--------------VISWNELCKIAESMARGLAYLhedipatNGGHkpsIAHRDFKSKNVLLKSDL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFGMSRdVYSTD------YYRVGGHtmlpiRWMPPE----SImyrKFTTES----DVWSLGVVLWEI-----FTY 593
Cdd:cd14053   140 TACIADFGLAL-KFEPGkscgdtHGQVGTR-----RYMAPEvlegAI---NFTRDAflriDMYAMGLVLWELlsrcsVHD 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 594 GKQPWYQL----------SNNEVIECITQGRvlQRPRTCPQ--------EVYELMLGCWQREPHMR 641
Cdd:cd14053   211 GPVDEYQLpfeeevgqhpTLEDMQECVVHKK--LRPQIRDEwrkhpglaQLCETIEECWDHDAEAR 274
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
377-657 8.47e-22

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 95.90  E-value: 8.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNLcpeqdkilVAVKTLKDASDNARK--DFHREAELLTNLQHEHIVKFYGVCVEG 454
Cdd:cd14151     5 IPDGQITVGQRIGSGSFGTVYKGKWHGD--------VAVKMLNVTAPTPQQlqAFKNEVGVLRKTRHVNILLFMGYSTKP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DpLIMVFEYMKHGDLNKFLRAhgpdavlmaegnPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 534
Cdd:cd14151    77 Q-LAIVTQWCEGSSLYHHLHI------------IETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTV 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGM----SRDVYSTDYYRVGGhtmlPIRWMPPESIMYRK---FTTESDVWSLGVVLWEIFTyGKQPWYQLSN-NEV 606
Cdd:cd14151   144 KIGDFGLatvkSRWSGSHQFEQLSG----SILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMT-GQLPYSNINNrDQI 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 607 IECITQGRV---LQRPRT-CPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKA 657
Cdd:cd14151   219 IFMVGRGYLspdLSKVRSnCPKAMKRLMAECLKKKRDERPLFPQILASIELLARS 273
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
381-641 8.50e-22

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 95.49  E-value: 8.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAEcyNLcpeQDKILVAVKTL-------KDASDNARKDFHREAELLTNL-QHEHIVKFYGVCV 452
Cdd:cd13993     1 RYQLISPIGEGAYGVVYLAV--DL---RTGRKYAIKCLyksgpnsKDGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 453 EGDPLIMVFEYMKHGDL--NKFLRAHGPDAVLMaegnppteltqsqMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGE 530
Cdd:cd13993    76 TEVAIYIVLEYCPNGDLfeAITENRIYVGKTEL-------------IKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQ 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 531 N-LLVKIGDFGMS-RDVYSTDyYRVGGHtmlpiRWMPPESI----MYRKF--TTESDVWSLGVVLWEIfTYGKQPWYQLS 602
Cdd:cd13993   143 DeGTVKLCDFGLAtTEKISMD-FGVGSE-----FYMAPECFdevgRSLKGypCAAGDIWSLGIILLNL-TFGRNPWKIAS 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 603 NNEVIECITQGR---VLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd13993   216 ESDPIFYDYYLNspnLFDVILPMSDDFYNLLRQIFTVNPNNR 257
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
384-631 8.59e-22

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 95.44  E-value: 8.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECYNLcpeqdKILVAVKTL--KDASDNARKDF-HREAELLTNLQHEHIVKFYGvCVEGDP---L 457
Cdd:cd14162     4 VGKTLGHGSYAVVKKAYSTKH-----KCKVAIKIVskKKAPEDYLQKFlPREIEVIKGLKHPNLICFYE-AIETTSrvyI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMvfEYMKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd14162    78 IM--ELAENGDLLDYIRKNG-------------ALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKIT 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 538 DFGMSRDVYSTDYYRV-------GGHTmlpirWMPPE---SIMYRKFTteSDVWSLGVVLWEIFtYGKQPwYQLSNNEVI 607
Cdd:cd14162   143 DFGFARGVMKTKDGKPklsetycGSYA-----YASPEilrGIPYDPFL--SDIWSMGVVLYTMV-YGRLP-FDDSNLKVL 213
                         250       260
                  ....*....|....*....|....*
gi 1610576541 608 -ECITQGRVLQRPRTCPQEVYELML 631
Cdd:cd14162   214 lKQVQRRVVFPKNPTVSEECKDLIL 238
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
381-598 9.07e-22

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 95.48  E-value: 9.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLaeCYNLCPEQDKILVAVKTLKDASDNARK--DFHREAELLTNLQHEHIVKFYGvCVEgDP-- 456
Cdd:cd06653     3 NWRLGKLLGRGAFGEVYL--CYDADTGRELAVKQVPFDPDSQETSKEvnALECEIQLLKNLRHDRIVQYYG-CLR-DPee 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 --LIMVFEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 534
Cdd:cd06653    79 kkLSIFVEYMPGGSVKDQLKAYGA-------------LTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNV 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 535 KIGDFGMSRDVYSTdyYRVG----GHTMLPIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPW 598
Cdd:cd06653   146 KLGDFGASKRIQTI--CMSGtgikSVTGTPY-WMSPEVISGEGYGRKADVWSVACTVVEMLTE-KPPW 209
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
381-590 1.25e-21

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 95.57  E-value: 1.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVflAECYNlcpEQDKILVAVKT-LKDASDNARKDFHREAELLTNLQHEHIVKFYGVCV-EGDPLI 458
Cdd:cd06621     2 KIVELSSLGEGAGGSV--TKCRL---RNTKTIFALKTiTTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLdEQDSSI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 -MVFEYMKHGDLNKFLRAhgpdavLMAEGNPPTELTqsqMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd06621    77 gIAMEYCEGGSLDSIYKK------VKKKGGRIGEKV---LGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLC 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 538 DFGMSRDVYS--------TDYYrvgghtmlpirwMPPESIMYRKFTTESDVWSLGVVLWEI 590
Cdd:cd06621   148 DFGVSGELVNslagtftgTSYY------------MAPERIQGGPYSITSDVWSLGLTLLEV 196
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
386-647 1.27e-21

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 95.02  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcynlcPEQDKILVAVKTL-KDASDNA--RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14116    11 RPLGKGKFGNVYLAR-----EKQSKFILALKVLfKAQLEKAgvEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHGpdavlmaegnppTELTQSQMLHIaQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd14116    86 YAPLGTVYRELQKLS------------KFDEQRTATYI-TELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 RDVYSTDYYRVGGhtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEiFTYGKQPWYQLSNNEVIECITqgRV-LQRPRT 621
Cdd:cd14116   153 VHAPSSRRTTLCG----TLDYLPPEMIEGRMHDEKVDLWSLGVLCYE-FLVGKPPFEANTYQETYKRIS--RVeFTFPDF 225
                         250       260
                  ....*....|....*....|....*.
gi 1610576541 622 CPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14116   226 VTEGARDLISRLLKHNPSQRPMLREV 251
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
388-589 1.28e-21

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 95.72  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynlcpeQDKI---LVAVKTLK-----DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd07841     8 LGEGTYAVVYKA--------RDKEtgrIVAIKKIKlgerkEAKDGINFTALREIKLLQELKHPNIIGLLDVFGHKSNINL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMkHGDLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd07841    80 VFEFM-ETDLEKVIK------------DKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADF 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 540 GMSRDVYSTDyyRVGGHTMLPIRWMPPESIM-YRKFTTESDVWSLGVVLWE 589
Cdd:cd07841   147 GLARSFGSPN--RKMTHQVVTRWYRAPELLFgARHYGVGVDMWSVGCIFAE 195
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
385-641 1.30e-21

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 95.08  E-value: 1.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 385 KRELGEGAFGKVFLAECynlcPEQDKILVAVKTL-KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd14202     7 KDLIGHGAFAVVFKGRH----KEKHDLEVAVKCInKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVG---------ENLLV 534
Cdd:cd14202    83 CNGGDLADYLHTMR-------------TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGMSRDVYS-TDYYRVGGHTMlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQG 613
Cdd:cd14202   150 KIADFGFARYLQNnMMAATLCGSPM----YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPFQASSPQDLRLFYEKN 224
                         250       260       270
                  ....*....|....*....|....*....|
gi 1610576541 614 RVLQR--PRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd14202   225 KSLSPniPRETSSHLRQLLLGLLQRNQKDR 254
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
381-645 1.40e-21

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 94.82  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKDFH---------------REAELLTNLQHEHIV 445
Cdd:cd14077     2 NWEFVKTIGAGSMGKVKLAK-----HIRTGEKCAIKIIPRASNAGLKKERekrlekeisrdirtiREAALSSLLNHPHIC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 446 KFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRN 525
Cdd:cd14077    77 RLRDFLRTPNHYYMLFEYVDGGQLLDYIISHGK-------------LKEKQARKFARQIASALDYLHRNSIVHRDLKIEN 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 526 CLVGENLLVKIGDFGMSrDVYStdyYRVGGHTML-PIRWMPPESIMYRKFT-TESDVWSLGVVLWEIFTyGKQPWYQLSN 603
Cdd:cd14077   144 ILISKSGNIKIIDFGLS-NLYD---PRRLLRTFCgSLYFAAPELLQAQPYTgPEVDVWSFGVVLYVLVC-GKVPFDDENM 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 604 NEVIECITQGRVlQRPRTCPQEVYELMLGCWQREPHMRKNIK 645
Cdd:cd14077   219 PALHAKIKKGKV-EYPSYLSSECKSLISRMLVVDPKKRATLE 259
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
388-647 2.20e-21

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 93.92  E-value: 2.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKvflaeCYNLCPEQDKILVAVKTL---KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd14188     9 LGKGGFAK-----CYEMTDLTTNKVYAAKIIphsRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd14188    84 SRRSMAHILKAR-------------KVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAAR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 VYSTDYYRvggHTMLPI-RWMPPESIMYRKFTTESDVWSLGVVLWEIFtYGKQPWYQLSNNEVIECITQGRvLQRPRTCP 623
Cdd:cd14188   151 LEPLEHRR---RTICGTpNYLSPEVLNKQGHGCESDIWALGCVMYTML-LGRPPFETTNLKETYRCIREAR-YSLPSSLL 225
                         250       260
                  ....*....|....*....|....
gi 1610576541 624 QEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14188   226 APAKHLIASMLSKNPEDRPSLDEI 249
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
369-659 2.30e-21

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 94.71  E-value: 2.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 369 KPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLcpeqdkilVAVKTLK--DASDNARKDFHREAELLTNLQHEHIVK 446
Cdd:cd14149     1 RDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGD--------VAVKILKvvDPTPEQFQAFRNEVAVLRKTRHVNILL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 447 FYGVCVEGDpLIMVFEYMKHGDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNC 526
Cdd:cd14149    73 FMGYMTKDN-LAIVTQWCEGSSLYKHLHVQ------------ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 527 LVGENLLVKIGDFGMsrdvySTDYYRVGGHTML-----PIRWMPPESIMYRK---FTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd14149   140 FLHEGLTVKIGDFGL-----ATVKSRWSGSQQVeqptgSILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYELMT-GELPY 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 599 YQLSN-NEVIECITQGRVL----QRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASP 659
Cdd:cd14149   214 SHINNrDQIIFMVGRGYASpdlsKLYKNCPKAMKRLVADCIKKVKEERPLFPQILSSIELLQHSLP 279
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
386-613 2.39e-21

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 94.33  E-value: 2.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAecynlcpeQDK---ILVAVKTLKDASDNA-RKDFHREAELLTNLQHEHIVKFYGVC-VEGDpLIMV 460
Cdd:cd06605     7 GELGEGNGGVVSKV--------RHRpsgQIMAVKVIRLEIDEAlQKQILRELDVLHKCNSPYIVGFYGAFySEGD-ISIC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQH-FVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd06605    78 MEYMDGGSLDKILKEVGR-------------IPERILGKIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQVKLCDF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMS----RDVYSTDyyrVGGHTmlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNN------EVIEC 609
Cdd:cd06605   145 GVSgqlvDSLAKTF---VGTRS-----YMAPERISGGKYTVKSDIWSLGLSLVELAT-GRFPYPPPNAKpsmmifELLSY 215

                  ....
gi 1610576541 610 ITQG 613
Cdd:cd06605   216 IVDE 219
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
383-647 2.89e-21

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 93.66  E-value: 2.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFLAEcynlcPEQDKILVAVK--TLKDASDNARKDFHREAELLTNLQHEHIVKfYGVCVEGDP--LI 458
Cdd:cd08223     3 QFLRVIGKGSYGEVWLVR-----HKRDRKQYVIKklNLKNASKRERKAAEQEAKLLSKLKHPNIVS-YKESFEGEDgfLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLRahgpdavlMAEGNPpteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGD 538
Cdd:cd08223    77 IVMGFCEGGDLYTRLK--------EQKGVL---LEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 539 FGMSRDVYS----------TDYYrvgghtmlpirwMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIE 608
Cdd:cd08223   146 LGIARVLESssdmattligTPYY------------MSPELFSNKPYNHKSDVWALGCCVYEMATL-KHAFNAKDMNSLVY 212
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1610576541 609 CITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd08223   213 KILEGKLPPMPKQYSPELGELIKAMLHQDPEKRPSVKRI 251
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
388-641 3.64e-21

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 93.35  E-value: 3.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynlcpeQDK---ILVAVKTLKDASDNARKDFHR---EAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd05123     1 LGKGSFGKVLLV--------RKKdtgKLYAMKVLRKKEIIKRKEVEHtlnERNILERVNHPFIVKLHYAFQTEEKLYLVL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd05123    73 DYVPGGELFSHLSKEGR-------------FPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SRDVYSTD---YYRVGghTmlpIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGrVLQR 618
Cdd:cd05123   140 AKELSSDGdrtYTFCG--T---PEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLT-GKPPFYAENRKEIYEKILKS-PLKF 212
                         250       260
                  ....*....|....*....|...
gi 1610576541 619 PRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05123   213 PEYVSPEAKSLISGLLQKDPTKR 235
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
393-655 3.80e-21

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 93.86  E-value: 3.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 393 FGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKF 472
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 473 LRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVY------ 546
Cdd:cd14222    81 LRADDP-------------FPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeekkkp 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 547 ----STDYYRVGGHTMLPIR--------WMPPESIMYRKFTTESDVWSLGVVLWEIFTygkqpwyQLSNNEviECITqgR 614
Cdd:cd14222   148 ppdkPTTKKRTLRKNDRKKRytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVLCEIIG-------QVYADP--DCLP--R 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 615 VLQ------------RPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLA 655
Cdd:cd14222   217 TLDfglnvrlfwekfVPKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFEALS 269
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
385-652 4.65e-21

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 93.53  E-value: 4.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 385 KREL-GEGAFGKVFLAECYnlcpEQDKILVAVKTL-KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14201    10 RKDLvGHGAFAVVFKGRHR----KKTDWEVAIKSInKKNLSKSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVME 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVG---------ENLL 533
Cdd:cd14201    86 YCNGGDLADYLQAKG-------------TLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 534 VKIGDFGMSRDVYSTDY-YRVGGHTMlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQ 612
Cdd:cd14201   153 IKIADFGFARYLQSNMMaATLCGSPM----YMAPEVIMSQHYDAKADLWSIGTVIYQCLV-GKPPFQANSPQDLRMFYEK 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1610576541 613 GRVLQR--PRTCPQEVYELMLGCWQREPHMRKNIKGI--HTLLQ 652
Cdd:cd14201   228 NKNLQPsiPRETSPYLADLLLGLLQRNQKDRMDFEAFfsHPFLE 271
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
383-597 5.27e-21

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 93.46  E-value: 5.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFLAecynlcpeQDKIL---VAVKT--LKDASDNArKDFHREAELLTNLQHEHIVKFYGVCVEGDPL 457
Cdd:cd06609     4 TLLERIGKGSFGEVYKG--------IDKRTnqvVAIKVidLEEAEDEI-EDIQQEIQFLSQCDSPYITKYYGSFLKGSKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLNKFLRAHGPDAVLMAEgnppteltqsqmlhIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd06609    75 WIIMEYCGGGSVLDLLKPGPLDETYIAF--------------ILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLA 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 538 DFGMSRDVYSTDYYRvggHTML--PIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQP 597
Cdd:cd06609   141 DFGVSGQLTSTMSKR---NTFVgtPF-WMAPEVIKQSGYDEKADIWSLGITAIELAK-GEPP 197
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
384-648 5.36e-21

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 93.09  E-value: 5.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTL---KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:cd14081     5 LGKTLGKGQTGLVKLAK-----HCVTGQKVAIKIVnkeKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd14081    80 LEYVSGGELFDYLVKKGR-------------LTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRdvystdyYRVGGHtML------PiRWMPPESIMYRKFT-TESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQG 613
Cdd:cd14081   147 MAS-------LQPEGS-LLetscgsP-HYACPEVIKGEKYDgRKADIWSCGVILYALLV-GALPFDDDNLRQLLEKVKRG 216
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1610576541 614 rVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIH 648
Cdd:cd14081   217 -VFHIPHFISPDAQDLLRRMLEVNPEKRITIEEIK 250
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
382-637 6.56e-21

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 92.77  E-value: 6.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKReLGEGAFGKVFLAECYNLcpeqdkilVAVKTLKDASDNARK--DFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd14150     3 SMLKR-IGTGSFGTVFRGKWHGD--------VAVKILKVTEPTPEQlqAFKNEMQVLRKTRHVNILLFMGFMTRPNFAII 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VfEYMKHGDLNKFLraHGPDavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd14150    74 T-QWCEGSSLYRHL--HVTE----------TRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDF 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMsrdvySTDYYRVGGHTML-----PIRWMPPESIMYRK---FTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIeCIT 611
Cdd:cd14150   141 GL-----ATVKTRWSGSQQVeqpsgSILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMS-GTLPYSNINNRDQI-IFM 213
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1610576541 612 QGRVLQRP------RTCPQEVYELMLGC--WQRE 637
Cdd:cd14150   214 VGRGYLSPdlsklsSNCPKAMKRLLIDClkFKRE 247
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
389-641 6.90e-21

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 93.27  E-value: 6.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 389 GEGAFGKVFLAECYNLcpeqdkiLVAVKTLkdaSDNARKDFHREAELLT--NLQHEHIVKFYG----VCVEGDPLIMVFE 462
Cdd:cd13998     4 GKGRFGEVWKASLKNE-------PVAVKIF---SSRDKQSWFREKEIYRtpMLKHENILQFIAaderDTALRTELWLVTA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHF---------VHRDLATRNCLVGENLL 533
Cdd:cd13998    74 FHPNGSL*DYLSLH--------------TIDWVSLCRLALSVARGLAHLHSEIPgctqgkpaiAHRDLKSKNILVKNDGT 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 534 VKIGDFGMS-RDVYSTDYYRVGGHTML-PIRWMPPE----SIMYRKFTT--ESDVWSLGVVLWEIF-----TYGKQPWYQ 600
Cdd:cd13998   140 CCIADFGLAvRLSPSTGEEDNANNGQVgTKRYMAPEvlegAINLRDFESfkRVDIYAMGLVLWEMAsrctdLFGIVEEYK 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 601 LSNNEVI---ECITQGRVL-----QRPR------TCP--QEVYELMLGCWQREPHMR 641
Cdd:cd13998   220 PPFYSEVpnhPSFEDMQEVvvrdkQRPNipnrwlSHPglQSLAETIEECWDHDAEAR 276
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
382-644 7.72e-21

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 92.66  E-value: 7.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKReLGEGAFGKVFLAecynLCPeqDKILVAVK--TLKDASDNARKDFHREAELLTNLQHE-HIVKFYG--VCVEGDP 456
Cdd:cd14131     4 EILKQ-LGKGGSSKVYKV----LNP--KKKIYALKrvDLEGADEQTLQSYKNEIELLKKLKGSdRIIQLYDyeVTDEDDY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYmKHGDLNKFLRAHGPDAVLMAEgnppTELTQSQMLHIAQQIaagmvylasqH---FVHRDLATRNCLVGENLL 533
Cdd:cd14131    77 LYMVMEC-GEIDLATILKKKRPKPIDPNF----IRYYWKQMLEAVHTI----------HeegIVHSDLKPANFLLVKGRL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 534 vKIGDFGMSRDV--YSTDYYR---VGghtmlPIRWMPPESIMYRKFTTE----------SDVWSLGVVLWEiFTYGKQPW 598
Cdd:cd14131   142 -KLIDFGIAKAIqnDTTSIVRdsqVG-----TLNYMSPEAIKDTSASGEgkpkskigrpSDVWSLGCILYQ-MVYGKTPF 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1610576541 599 YQLSN-NEVIECITQ-GRVLQRPRTCPQEVYELMLGCWQREPHMRKNI 644
Cdd:cd14131   215 QHITNpIAKLQAIIDpNHEIEFPDIPNPDLIDVMKRCLQRDPKKRPSI 262
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
388-598 1.13e-20

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 96.02  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcpeqDKIL---VAVKTLKD--ASD-NARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:NF033483   15 IGRGGMAEVYLAK--------DTRLdrdVAVKVLRPdlARDpEFVARFRREAQSAASLSHPNIVSVYDVGEDGGIPYIVM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:NF033483   87 EYVDGRTLKDYIREHGP-------------LSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGI 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 542 SRDVYSTdyyrvgghTMLP-------IRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:NF033483  154 ARALSST--------TMTQtnsvlgtVHYLSPEQARGGTVDARSDIYSLGIVLYEMLT-GRPPF 208
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
384-588 1.14e-20

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 92.07  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTL-KDASDNAR-KDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd14071     4 IERTIGKGNFAVVKLAR-----HRITKTEVAIKIIdKSQLDEENlKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd14071    79 EYASNGEIFDYLAQHG-------------RMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGF 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 542 SrdvystDYYRVGGHTML-----PirWMPPESIMYRKFT-TESDVWSLGVVLW 588
Cdd:cd14071   146 S------NFFKPGELLKTwcgspP--YAAPEVFEGKEYEgPQLDIWSLGVVLY 190
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
394-590 1.15e-20

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 91.77  E-value: 1.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 394 GKVFLAECYNLCPEQDKILVAVKTLKDASDnaRKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFL 473
Cdd:cd14155     2 GSGFFSEVYKVRHRTSGQVMALKMNTLSSN--RANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 474 RAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV--GENLLVKI-GDFGMSRDVYSTDY 550
Cdd:cd14155    80 DSNEP-------------LSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrDENGYTAVvGDFGLAEKIPDYSD 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1610576541 551 yrvgGHTMLPI----RWMPPESIMYRKFTTESDVWSLGVVLWEI 590
Cdd:cd14155   147 ----GKEKLAVvgspYWMAPEVLRGEPYNEKADVFSYGIILCEI 186
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
381-654 1.26e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 92.01  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAECynLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:cd08228     3 NFQIEKKIGRGQFSEVYRATC--LLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGPDAVLMAEgnppteltqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd08228    81 LELADAGDLSQMIKYFKKQKRLIPE---------RTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRdVYSTDyyRVGGHTMLPI-RWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECitqgrvlQRP 619
Cdd:cd08228   152 LGR-FFSSK--TTAAHSLVGTpYYMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYGDKMNLFSLC-------QKI 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1610576541 620 RTC-----PQEVY-----ELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd08228   221 EQCdypplPTEHYseklrELVSMCIYPDPDQRPDIGYVHQIAKQM 265
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
384-641 1.42e-20

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 92.04  E-value: 1.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECYnlcPEQDKilVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd06610     5 LIEVIGSGATAVVYAAYCL---PKKEK--VAIKRIDlEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLnkflrahgpdAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd06610    80 LLSGGSL----------LDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 RDVYS-TDYYRVGGHTML--PIrWMPPEsIM--YRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVLQ 617
Cdd:cd06610   150 ASLATgGDRTRKVRKTFVgtPC-WMAPE-VMeqVRGYDFKADIWSFGITAIELAT-GAAPYSKYPPMKVLMLTLQNDPPS 226
                         250       260
                  ....*....|....*....|....*....
gi 1610576541 618 RPRTCPQEVY-----ELMLGCWQREPHMR 641
Cdd:cd06610   227 LETGADYKKYsksfrKMISLCLQKDPSKR 255
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
384-619 1.79e-20

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 91.77  E-value: 1.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECYNLCPEQD-KILVAVKTLkdASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14098     4 IIDRLGSGTFAEVKKAVEVETGKMRAiKQIVKRKVA--GNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHGpdAVLMAEGNPpteltqsqmlhIAQQIAAGMVYLASQHFVHRDLATRNCLVGEN--LLVKIGDFG 540
Cdd:cd14098    82 YVEGGDLMDFIMAWG--AIPEQHARE-----------LTKQILEAMAYTHSMGITHRDLKPENILITQDdpVIVKISDFG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRdvystdyyRVGGHTML-----PIRWMPPESIMYRK------FTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIEC 609
Cdd:cd14098   149 LAK--------VIHTGTFLvtfcgTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVMLT-GALPFDGSSQLPVEKR 219
                         250
                  ....*....|
gi 1610576541 610 ITQGRVLQRP 619
Cdd:cd14098   220 IRKGRYTQPP 229
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
394-641 1.85e-20

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 91.43  E-value: 1.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 394 GKVFLAECYNLCPEQDKILVAVKTLKDASDnaRKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKfl 473
Cdd:cd14156     2 GSGFFSKVYKVTHGATGKVMVVKIYKNDVD--QHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEE-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 474 rahgpdavLMAEGNPPteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK---IGDFGMSRDVY---S 547
Cdd:cd14156    78 --------LLAREELP--LSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVGempA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 548 TDYYR----VGGHTmlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFtyGKQPwyqlSNNEVIecitqgrvlqrPRT-- 621
Cdd:cd14156   148 NDPERklslVGSAF-----WMAPEMLRGEPYDRKVDVFSFGIVLCEIL--ARIP----ADPEVL-----------PRTgd 205
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1610576541 622 --------------CPQEVYELMLGCWQREPHMR 641
Cdd:cd14156   206 fgldvqafkemvpgCPEPFLDLAASCCRMDAFKR 239
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
388-592 2.08e-20

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 92.42  E-value: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcpeqDKILVAVKTLKDASdnaRKDFHREAEL--LTNLQHEHIVKFYGVC----VEGDP-LIMV 460
Cdd:cd14054     3 IGQGRYGTVWKGSL-------DERPVAVKVFPARH---RQNFQNEKDIyeLPLMEHSNILRFIGADerptADGRMeYLLV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLAS------QH---FVHRDLATRNCLVGEN 531
Cdd:cd14054    73 LEYAPKGSLCSYLREN--------------TLDWMSSCRMALSLTRGLAYLHTdlrrgdQYkpaIAHRDLNSRNVLVKAD 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610576541 532 LLVKIGDFGMSRDVYSTDYYRVGGHTMLP--------IRWMPPESI----------MYRKfttESDVWSLGVVLWEIFT 592
Cdd:cd14054   139 GSCVICDFGLAMVLRGSSLVRGRPGAAENasisevgtLRYMAPEVLegavnlrdceSALK---QVDVYALGLVLWEIAM 214
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
387-592 2.12e-20

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 92.00  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFlaECYNLCPEQdkiLVAVKTLKDASDN--ARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd07833     8 VVGEGAYGVVL--KCRNKATGE---IVAIKKFKESEDDedVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHG---DLNKFLRAHGPDAVlmaegnppteltQSQMLHIAQQIAagmvYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd07833    83 ERTlleLLEASPGGLPPDAV------------RSYIWQLLQAIA----YCHSHNIIHRDIKPENILVSESGVLKLCDFGF 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 542 SR------DVYSTDYyrvgghtmLPIRWM-PPE----SIMYRKfttESDVWSLGVVLWEIFT 592
Cdd:cd07833   147 ARaltarpASPLTDY--------VATRWYrAPEllvgDTNYGK---PVDVWAIGCIMAELLD 197
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
388-641 2.15e-20

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 91.52  E-value: 2.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEC---------YNLCPEQDKILVAVKTLKDA-----SDNARKDFHREAELLTNLQHEHIVKFYGVCVE 453
Cdd:cd14000     2 LGDGGFGSVYRASYkgepvavkiFNKHTSSNFANVPADTMLRHlratdAMKNFRLLRQELTVLSHLHHPSIVYLLGIGIH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 gdPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEgnpptELTQSqmlhIAQQIAAGMVYLASQHFVHRDLATRNCLV----- 528
Cdd:cd14000    82 --PLMLVLELAPLGSLDHLLQQDSRSFASLGR-----TLQQR----IALQVADGLRYLHSAMIIYRDLKSHNVLVwtlyp 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 529 GENLLVKIGDFGMSRDVYSTDYYRVGGHTmlpiRWMPPESIMYR-KFTTESDVWSLGVVLWEIFTyGKQPW---YQLSNN 604
Cdd:cd14000   151 NSAIIIKIADYGISRQCCRMGAKGSEGTP----GFRAPEIARGNvIYNEKVDVFSFGMLLYEILS-GGAPMvghLKFPNE 225
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1610576541 605 EVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd14000   226 FDIHGGLRPPLKQYECAPWPEVEVLMKKCWKENPQQR 262
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
388-597 2.19e-20

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 91.40  E-value: 2.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcpeQDKILVAVKTLKDASDNARK-DFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd14664     1 IGRGGAGTVYKGVM------PNGTLVAVKRLKGEGTQGGDhGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAHGPDAVlmaegnpptELTQSQMLHIAQQIAAGMVYL---ASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd14664    75 GSLGELLHSRPESQP---------PLDWETRQRIALGSARGLAYLhhdCSPLIIHRDVKSNNILLDEEFEAHVADFGLAK 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 544 DVYSTDyyrvgGHTMLPIR----WMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQP 597
Cdd:cd14664   146 LMDDKD-----SHVMSSVAgsygYIAPEYAYTGKVSEKSDVYSYGVVLLELIT-GKRP 197
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
387-591 2.35e-20

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 91.95  E-value: 2.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLK-DASDNARKDFH-REAELLTNLQ---HEHIVKFYGVCV-----EGDP 456
Cdd:cd07838     6 EIGEGAYGTVYKAR-----DLQDGRFVALKKVRvPLSEEGIPLSTiREIALLKQLEsfeHPNVVRLLDVCHgprtdRELK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMkHGDLNKFLRAHgpdavlmaegnPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd07838    81 LTLVFEHV-DQDLATYLDKC-----------PKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKL 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 537 GDFGMSRdVYS----------TDYYRvgghtmlpirwmPPESIMYRKFTTESDVWSLGVVLWEIF 591
Cdd:cd07838   149 ADFGLAR-IYSfemaltsvvvTLWYR------------APEVLLQSSYATPVDMWSVGCIFAELF 200
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
386-647 2.58e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 90.95  E-value: 2.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLaeCYNLcpeQDKILVAVKT--LKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd08220     6 RVVGRGAYGTVYL--CRRK---DDNKLVIIKQipVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGpdAVLMAEgnppteltqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGEN-LLVKIGDFGMS 542
Cdd:cd08220    81 APGGTLFEYIQQRK--GSLLSE---------EEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKrTVVKIGDFGIS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 RDVYS-TDYYRVGGHTMlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECITQGRVLQRPRT 621
Cdd:cd08220   150 KILSSkSKAYTVVGTPC----YISPELCEGKPYNQKSDIWALGCVLYELASL-KRAFEAANLPALVLKIMRGTFAPISDR 224
                         250       260
                  ....*....|....*....|....*.
gi 1610576541 622 CPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd08220   225 YSEELRHLILSMLHLDPNKRPTLSEI 250
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
384-641 2.87e-20

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 90.78  E-value: 2.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTL-------KDASDNARkdfhREAELLTNLQHEHIVKFYGVCVEGDP 456
Cdd:cd05578     4 ILRVIGKGSFGKVCIVQ-----KKDTKKMFAMKYMnkqkcieKDSVRNVL----NELEILQELEHPFLVNLWYSFQDEED 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLnkflRAHGPDAVLMAEgnppteltqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd05578    75 MYMVVDLLLGGDL----RYHLQQKVKFSE---------ETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSRDVySTDYYRVGGHTMLPirWMPPESIMYRKFTTESDVWSLGVVLWEiFTYGKQPwYQLSNNEVIECITQGRVL 616
Cdd:cd05578   142 TDFNIATKL-TDGTLATSTSGTKP--YMAPEVFMRAGYSFAVDWWSLGVTAYE-MLRGKRP-YEIHSRTSIEEIRAKFET 216
                         250       260
                  ....*....|....*....|....*...
gi 1610576541 617 QR---PRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05578   217 ASvlyPAGWSEEAIDLINKLLERDPQKR 244
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
388-641 3.45e-20

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 90.43  E-value: 3.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecYNlcPEQDKILVAVKTL--KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd14121     3 LGSGTYATVYKA--YR--KSGAREVVAVKCVskSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV--GENLLVKIGDFGMSR 543
Cdd:cd14121    79 GGDLSRFIRSRR-------------TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLssRYNPVLKLADFGFAQ 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVYSTDYyrvgGHTML--PIrWMPPESIMYRKFTTESDVWSLGVVLWEIFtYGKQPWYQLSNNEVIECITQGRVLQRPRT 621
Cdd:cd14121   146 HLKPNDE----AHSLRgsPL-YMAPEMILKKKYDARVDLWSVGVILYECL-FGRAPFASRSFEELEEKIRSSKPIEIPTR 219
                         250       260
                  ....*....|....*....|..
gi 1610576541 622 CP--QEVYELMLGCWQREPHMR 641
Cdd:cd14121   220 PElsADCRDLLLRLLQRDPDRR 241
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
388-605 3.53e-20

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 90.93  E-value: 3.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcyNLcpeQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHG 467
Cdd:cd06624    16 LGKGTFGVVYAAR--DL---STQVRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 468 DLNKFLRAH-GPdavlmAEGNPPTeltqsqMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGE-NLLVKIGDFGMSRdv 545
Cdd:cd06624    91 SLSALLRSKwGP-----LKDNENT------IGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSK-- 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 546 ystdyyRVGGHTML------PIRWMPPESIMY--RKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNE 605
Cdd:cd06624   158 ------RLAGINPCtetftgTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMAT-GKPPFIELGEPQ 218
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
388-598 3.79e-20

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 90.46  E-value: 3.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASdNARKDFHREAELLTNLQ-HEHIVKFYGVCVEG-DPLIMVFEYMK 465
Cdd:cd13987     1 LGEGTYGKVLLAV-----HKGSGTKMALKFVPKPS-TKLKDFLREYNISLELSvHPHIIKTYDVAFETeDYYVFAQEYAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLnkfLRAHGPDAVLmaegnpPTELTQSqmlhIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL--VKIGDFGMSR 543
Cdd:cd13987    75 YGDL---FSIIPPQVGL------PEERVKR----CAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCrrVKLCDFGLTR 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVYSTDYYRvggHTMLPirWMPPE---SIMYRKFTTE--SDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd13987   142 RVGSTVKRV---SGTIP--YTAPEvceAKKNEGFVVDpsIDVWAFGVLLFCCLT-GNFPW 195
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
388-647 4.13e-20

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit, common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 90.35  E-value: 4.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLCP-EQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDpLIMVFEYMKH 466
Cdd:cd14208     7 LGKGSFTKIYRGLRTDEEDdERCETEVLLKVMDPTHGNCQESFLEAASIMSQISHKHLVLLHGVCVGKD-SIMVQEFVCH 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAHGpdavlmAEGNPPTeltqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV------GENLLVKIGDFG 540
Cdd:cd14208    86 GALDLYLKKQQ------QKGPVAI----SWKLQVVKQLAYALNYLEDKQLVHGNVSAKKVLLsregdkGSPPFIKLSDPG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDVYSTDyyrvgghtMLP--IRWMPPESIM-YRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQ 617
Cdd:cd14208   156 VSIKVLDEE--------LLAerIPWVAPECLSdPQNLALEADKWGFGATLWEIFSGGHMPLSALDPSKKLQFYNDRKQLP 227
                         250       260       270
                  ....*....|....*....|....*....|
gi 1610576541 618 RPRTCpqEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14208   228 APHWI--ELASLIQQCMSYNPLLRPSFRAI 255
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
388-598 5.33e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 90.18  E-value: 5.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFgkvflAECYNLCPEQDKILVAVKTLKDASDNARK------DFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd06630     8 LGTGAF-----SSCYQARDVKTGTLMAVKQVSFCRNSSSEqeevveAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV---GENLlvKIGD 538
Cdd:cd06630    83 EWMAGGSVASLLSKYGA-------------FSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVdstGQRL--RIAD 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 539 FGMSRDVySTDYYRVG---GHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd06630   148 FGAAARL-ASKGTGAGefqGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMAT-AKPPW 208
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
386-647 5.72e-20

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 90.31  E-value: 5.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDA---SDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14117    12 RPLGKGKFGNVYLAR-----EKQSKFIVALKVLFKSqieKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd14117    87 YAPRGELYKELQKHG-------------RFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 rdVYSTDYYRvggHTML-PIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRvLQRPRT 621
Cdd:cd14117   154 --VHAPSLRR---RTMCgTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLV-GMPPFESASHTETYRRIVKVD-LKFPPF 226
                         250       260
                  ....*....|....*....|....*.
gi 1610576541 622 CPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14117   227 LSDGSRDLISKLLRYHPSERLPLKGV 252
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
385-597 6.33e-20

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 89.92  E-value: 6.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 385 KRELGEGAFGKVFLAEcynlcpEQD-KILVAVKTLKDAS---DNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:cd14099     6 GKFLGKGGFAKCYEVT------DMStGKVYAGKVVPKSSltkPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd14099    80 LELCSNGSLMELLKRRKA-------------LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFG 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 541 MSRDVYSTDYYRVgghTM--LPiRWMPPEsIMYRK--FTTESDVWSLGVVLWEIFTyGKQP 597
Cdd:cd14099   147 LAARLEYDGERKK---TLcgTP-NYIAPE-VLEKKkgHSFEVDIWSLGVILYTLLV-GKPP 201
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
380-613 6.80e-20

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 90.35  E-value: 6.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 380 HNIVLKRELGEGAFGKVFLAecynlcpeQDKI---LVAVKTLKDA---SDNARKDFHREAELLTNLQHEHIVKFYGVCVE 453
Cdd:cd05581     1 NDFKFGKPLGEGSYSTVVLA--------KEKEtgkEYAIKVLDKRhiiKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMKHGDLNKFLRAHGpdavlmaegnppteltqSQMLHIAQQIAAGMV----YLASQHFVHRDLATRNCLVG 529
Cdd:cd05581    73 ESKLYFVLEYAPNGDLLEYIRKYG-----------------SLDEKCTRFYTAEIVlaleYLHSKGIIHRDLKPENILLD 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 530 ENLLVKIGDFGmSRDVYSTDY--------YRVGGHTMLPIR--------WMPPESIMYRKFTTESDVWSLGVVLWEIFTy 593
Cdd:cd05581   136 EDMHIKITDFG-TAKVLGPDSspestkgdADSQIAYNQARAasfvgtaeYVSPELLNEKPAGKSSDLWALGCIIYQMLT- 213
                         250       260
                  ....*....|....*....|
gi 1610576541 594 GKQPWYQLSNNEVIECITQG 613
Cdd:cd05581   214 GKPPFRGSNEYLTFQKIVKL 233
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
388-647 7.33e-20

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 89.62  E-value: 7.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLA-ECYNLCpeqdkiLVAVKTLKDAS----DNARKDFHREAELLTNLQHEHIVKFYGVCV--EGDPLIMV 460
Cdd:cd14119     1 LGEGSYGKVKEVlDTETLC------RRAVKILKKRKlrriPNGEANVKREIQILRRLNHRNVIKLVDVLYneEKQKLYMV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMkHGDLnkflrahgpdaVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd14119    75 MEYC-VGGL-----------QEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSR--DVYSTDY--YRVGGHtmlPiRWMPPE----SIMYRKFttESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQ 612
Cdd:cd14119   143 VAEalDLFAEDDtcTTSQGS---P-AFQPPEiangQDSFSGF--KVDIWSAGVTLYNMTT-GKYPFEGDNIYKLFENIGK 215
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1610576541 613 GrVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14119   216 G-EYTIPDDVDPDLQDLLRGMLEKDPEKRFTIEQI 249
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
390-610 9.69e-20

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 89.98  E-value: 9.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 390 EGAFGKVFLAecynLCPEQDKIlVAVKTLKdaSDNARKDFH----REAELLTNLQHEHIVKFYGVCVeGDPL---IMVFE 462
Cdd:cd07843    15 EGTYGVVYRA----RDKKTGEI-VALKKLK--MEKEKEGFPitslREINILLKLQHPNIVTVKEVVV-GSNLdkiYMVME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHgDLNKflrahgpdavLMAEGNPPteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd07843    87 YVEH-DLKS----------LMETMKQP--FLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 RDVYS----------TDYYRvgghtmlpirwmPPESIM-YRKFTTESDVWSLGVVLWEIFTygKQPWYQLSNN-EVIECI 610
Cdd:cd07843   154 REYGSplkpytqlvvTLWYR------------APELLLgAKEYSTAIDMWSVGCIFAELLT--KKPLFPGKSEiDQLNKI 219
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
386-647 1.23e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 89.10  E-value: 1.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNlcpEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd08218     6 KKIGEGSFGKALLVKSKE---DGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLnkFLRAHGPDAVLMAEgnppteltqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDV 545
Cdd:cd08218    83 GGDL--YKRINAQRGVLFPE---------DQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 546 YS----------TDYYrvgghtmlpirwMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECITQGRV 615
Cdd:cd08218   152 NStvelartcigTPYY------------LSPEICENKPYNNKSDIWALGCVLYEMCTL-KHAFEAGNMKNLVLKIIRGSY 218
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1610576541 616 LQRPRTCPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd08218   219 PPVPSRYSYDLRSLVSQLFKRNPRDRPSINSI 250
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
387-641 1.36e-19

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 89.71  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd06644    19 ELGDGAFGKVYKAK-----NKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLnkflrahgpDAVLMAEGNpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS---- 542
Cdd:cd06644    94 GAV---------DAIMLELDR---GLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSaknv 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 -----RDVY-STDYyrvgghtmlpirWMPPESIMYRK-----FTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECIT 611
Cdd:cd06644   162 ktlqrRDSFiGTPY------------WMAPEVVMCETmkdtpYDYKADIWSLGITLIEMAQI-EPPHHELNPMRVLLKIA 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1610576541 612 QGR--VLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd06644   229 KSEppTLSQPSKWSMEFRDFLKTALDKHPETR 260
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
388-645 2.41e-19

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 88.57  E-value: 2.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynlCPEQDKILVAVKT--LKDASDNArKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd06640    12 IGKGSFGEVFKG-----IDNRTQQVVAIKIidLEEAEDEI-EDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAhGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDV 545
Cdd:cd06640    86 GGSALDLLRA-GP-------------FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 546 YSTDYYR---VGghtmLPIrWMPPESIMYRKFTTESDVWSLGVVLWEIfTYGKQPWYQLSNNEVIECITQGRVLQRPRTC 622
Cdd:cd06640   152 TDTQIKRntfVG----TPF-WMAPEVIQQSAYDSKADIWSLGITAIEL-AKGEPPNSDMHPMRVLFLIPKNNPPTLVGDF 225
                         250       260
                  ....*....|....*....|...
gi 1610576541 623 PQEVYELMLGCWQREPHMRKNIK 645
Cdd:cd06640   226 SKPFKEFIDACLNKDPSFRPTAK 248
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
386-647 2.77e-19

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 88.06  E-value: 2.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFgkvflAECYNLCPEQDKILVAVKTL---KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14189     7 RLLGKGGF-----ARCYEMTDLATNKTYAVKVIphsRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd14189    82 LCSRKSLAHIWKAR-------------HTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 RDVYSTDYYR--VGGHTmlpiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVLQrPR 620
Cdd:cd14189   149 ARLEPPEQRKktICGTP----NYLAPEVLLRQGHGPESDVWSLGCVMYTLLC-GNPPFETLDLKETYRCIKQVKYTL-PA 222
                         250       260
                  ....*....|....*....|....*..
gi 1610576541 621 TCPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14189   223 SLSLPARHLLAGILKRNPGDRLTLDQI 249
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
386-641 3.04e-19

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 87.72  E-value: 3.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLaecynLCPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGvCVEGDP-LIMVFEY 463
Cdd:cd08219     6 RVVGEGSFGRALL-----VQHVNSDQKYAMKEIRlPKSSSAVEDSRKEAVLLAKMKHPNIVAFKE-SFEADGhLYIVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRahgpdavlMAEGNPPTELTqsqMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd08219    80 CDGGDLMQKIK--------LQRGKLFPEDT---ILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVYSTDYYRVgGHTMLPIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECITQGRVLQRPRTCP 623
Cdd:cd08219   149 LLTSPGAYAC-TYVGTPY-YVPPEIWENMPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLILKVCQGSYKPLPSHYS 225
                         250
                  ....*....|....*...
gi 1610576541 624 QEVYELMLGCWQREPHMR 641
Cdd:cd08219   226 YELRSLIKQMFKRNPRSR 243
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
412-656 4.08e-19

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 88.04  E-value: 4.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 412 LVAVKTL----KDASDNARKdfhrEAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHgpDAVLmaegn 487
Cdd:cd14042    32 LVAIKKVnkkrIDLTREVLK----ELKHMRDLQHDNLTRFIGACVDPPNICILTEYCPKGSLQDILENE--DIKL----- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 488 ppTELTQSQMLHiaqQIAAGMVYLASQHFV-HRDLATRNCLVGENLLVKIGDFGMsRDVYSTDYYRVGGHT----MLpir 562
Cdd:cd14042   101 --DWMFRYSLIH---DIVKGMHYLHDSEIKsHGNLKSSNCVVDSRFVLKITDFGL-HSFRSGQEPPDDSHAyyakLL--- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 563 WMPPE--SIMYRKF--TTESDVWSLGVVLWEIFTYgKQPWYQ----LSNNEVIECItqGRVLQRP--R------TCPQEV 626
Cdd:cd14042   172 WTAPEllRDPNPPPpgTQKGDVYSFGIILQEIATR-QGPFYEegpdLSPKEIIKKK--VRNGEKPpfRpsldelECPDEV 248
                         250       260       270
                  ....*....|....*....|....*....|
gi 1610576541 627 YELMLGCWQREPHMRKNIKGIHTLLQNLAK 656
Cdd:cd14042   249 LSLMQRCWAEDPEERPDFSTLRNKLKKLNK 278
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
386-661 4.27e-19

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 87.60  E-value: 4.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNlcpEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd14097     7 RKLGQGSFGVVIEATHKE---TQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV-------GENLLVKIGD 538
Cdd:cd14097    84 DGELKELLLRKG-------------FFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidnNDKLNIKVTD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 539 FGMSRDVYStdyyrvGGHTML------PIrWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECITQ 612
Cdd:cd14097   151 FGLSVQKYG------LGEDMLqetcgtPI-YMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVAKSEEKLFEEIRK 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1610576541 613 GRVlqrprTCPQEVyelmlgcWQREPHMRKNIkgihtlLQNLAKASPVY 661
Cdd:cd14097   223 GDL-----TFTQSV-------WQSVSDAAKNV------LQQLLKVDPAH 253
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
387-605 4.49e-19

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 87.92  E-value: 4.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd07836     7 KLGEGTYATVYKGR-----NRTTGEIVALKEIHlDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 hGDLNKFLRAHGPDAVLmaegnpPTELTQSQMlhiaQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR-- 543
Cdd:cd07836    82 -KDLKKYMDTHGVRGAL------DPNTVKSFT----YQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARaf 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 544 ----DVYSTD----YYRvgghtmlpirwmPPESIM-YRKFTTESDVWSLGVVLWEIFTyGKqPWYQLSNNE 605
Cdd:cd07836   151 gipvNTFSNEvvtlWYR------------APDVLLgSRTYSTSIDIWSVGCIMAEMIT-GR-PLFPGTNNE 207
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
387-641 4.64e-19

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 88.10  E-value: 4.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcYnlcpEQDKilVAVKTLKDASDNArkdFHREAELLTN--LQHEHIVKFY-------GVCVEgdpL 457
Cdd:cd14056     2 TIGKGRYGEVWLGK-Y----RGEK--VAVKIFSSRDEDS---WFRETEIYQTvmLRHENILGFIaadikstGSWTQ---L 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHF--------VHRDLATRNCLVG 529
Cdd:cd14056    69 WLITEYHEHGSLYDYLQRN--------------TLDTEEALRLAYSAASGLAHLHTEIVgtqgkpaiAHRDLKSKNILVK 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 530 ENLLVKIGDFGM----SRDVYSTDY---YRVGghtmlPIRWMPPE----SIMYRKFTT--ESDVWSLGVVLWEIFTYG-- 594
Cdd:cd14056   135 RDGTCCIADLGLavryDSDTNTIDIppnPRVG-----TKRYMAPEvlddSINPKSFESfkMADIYSFGLVLWEIARRCei 209
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 595 -------KQPWYQLSNN-------EVIECITQGRVLQRPR----TCPQEVYELMLGCWQREPHMR 641
Cdd:cd14056   210 ggiaeeyQLPYFGMVPSdpsfeemRKVVCVEKLRPPIPNRwksdPVLRSMVKLMQECWSENPHAR 274
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
387-597 5.10e-19

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 87.42  E-value: 5.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAecYNlcpEQD------KILVAVKTLKDASDNARKD-----------------FHREAELLTNLQHEH 443
Cdd:cd14118     1 EIGKGSYGIVKLA--YN---EEDntlyamKILSKKKLLKQAGFFRRPPprrkpgalgkpldpldrVYREIAILKKLDHPN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 444 IVKFygVCVEGDP----LIMVFEYMKHGdlnkflrahgpdAVLMAEGNPPteLTQSQMLHIAQQIAAGMVYLASQHFVHR 519
Cdd:cd14118    76 VVKL--VEVLDDPnednLYMVFELVDKG------------AVMEVPTDNP--LSEETARSYFRDIVLGIEYLHYQKIIHR 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 520 DLATRNCLVGENLLVKIGDFGMSRDVYSTDYY---RVGGHTmlpirWMPPESIM--YRKFTTES-DVWSLGVVLWeIFTY 593
Cdd:cd14118   140 DIKPSNLLLGDDGHVKIADFGVSNEFEGDDALlssTAGTPA-----FMAPEALSesRKKFSGKAlDIWAMGVTLY-CFVF 213

                  ....
gi 1610576541 594 GKQP 597
Cdd:cd14118   214 GRCP 217
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
388-645 5.81e-19

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 87.42  E-value: 5.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflaecYNLCPEQDKILVAVKT--LKDASDNArKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd06642    12 IGKGSFGEV-----YKGIDNRTKEVVAIKIidLEEAEDEI-EDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRahgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDV 545
Cdd:cd06642    86 GGSALDLLK--------------PGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 546 YSTDYYRvGGHTMLPIrWMPPESIMYRKFTTESDVWSLGVVLWEIfTYGKQPWYQLSNNEVIECITQGR--VLQRPRTCP 623
Cdd:cd06642   152 TDTQIKR-NTFVGTPF-WMAPEVIKQSAYDFKADIWSLGITAIEL-AKGEPPNSDLHPMRVLFLIPKNSppTLEGQHSKP 228
                         250       260
                  ....*....|....*....|..
gi 1610576541 624 QEvyELMLGCWQREPHMRKNIK 645
Cdd:cd06642   229 FK--EFVEACLNKDPRFRPTAK 248
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
407-647 7.61e-19

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 86.91  E-value: 7.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 407 EQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGpdavlmaeg 486
Cdd:cd05077    33 YEKEIKVILKVLDPSHRDISLAFFETASMMRQVSHKHIVLLYGVCVRDVENIMVEEFVEFGPLDLFMHRKS--------- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 487 nppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL-------VKIGDFGMSRDVYSTDyyrvggHTML 559
Cdd:cd05077   104 ---DVLTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNILLAREGIdgecgpfIKLSDPGIPITVLSRQ------ECVE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 560 PIRWMPPESIM-YRKFTTESDVWSLGVVLWEIFTYGKQPwyqLSNNEVIEC--ITQGRVLQRPRTCpQEVYELMLGCWQR 636
Cdd:cd05077   175 RIPWIAPECVEdSKNLSIAADKWSFGTTLWEICYNGEIP---LKDKTLAEKerFYEGQCMLVTPSC-KELADLMTHCMNY 250
                         250
                  ....*....|.
gi 1610576541 637 EPHMRKNIKGI 647
Cdd:cd05077   251 DPNQRPFFRAI 261
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
386-647 7.66e-19

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 86.67  E-value: 7.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKD--ASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd13997     6 EQIGSGSFSEVFKVR-----SKVDGCLYAVKKSKKpfRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHGPDavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd13997    81 LCENGSLQDALEELSPI----------SKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 RDVYSTDYYRVGGHtmlpiRWMPPESIM-YRKFTTESDVWSLGVVLWEI-----FTYGKQPWYQLSnneviecitQGRVL 616
Cdd:cd13997   151 TRLETSGDVEEGDS-----RYLAPELLNeNYTHLPKADIFSLGVTVYEAatgepLPRNGQQWQQLR---------QGKLP 216
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1610576541 617 QRPRTC-PQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd13997   217 LPPGLVlSQELTRLLKVMLDPDPTRRPTADQL 248
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
387-653 8.75e-19

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 86.83  E-value: 8.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLK--DASDNARKDFHREAELLTNLQHEHIVKFYGVCVegDP------LI 458
Cdd:cd08217     7 TIGKGSFGTVRKVR-----RKSDGKILVWKEIDygKMSEKEKQQLVSEVNILRELKHPNIVRYYDRIV--DRanttlyIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MvfEYMKHGDLNKFLRAHGPDAVLMAEgnppteltqSQMLHIAQQIAAGMVY-----LASQHFVHRDLATRNCLVGENLL 533
Cdd:cd08217    80 M--EYCEGGDLAQLIKKCKKENQYIPE---------EFIWKIFTQLLLALYEchnrsVGGGKILHRDLKPANIFLDSDNN 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 534 VKIGDFGMSRDVYS----------TDYYrvgghtmlpirwMPPESIMYRKFTTESDVWSLGVVLWEIFTygKQPWYQLSN 603
Cdd:cd08217   149 VKLGDFGLARVLSHdssfaktyvgTPYY------------MSPELLNEQSYDEKSDIWSLGCLIYELCA--LHPPFQAAN 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 604 N-EVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKgihTLLQN 653
Cdd:cd08217   215 QlELAKKIKEGKFPRIPSRYSSELNEVIKSMLNVDPDKRPSVE---ELLQL 262
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
386-614 8.93e-19

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 87.06  E-value: 8.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAecYNlcpEQDKILVAVKTLKD--------ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPL 457
Cdd:cd14084    12 RTLGSGACGEVKLA--YD---KSTCKKVAIKIINKrkftigsrREINKPRNIETEIEILKKLSHPCIIKIEDFFDAEDDY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLnkFLRAHGPdavlMAEGNPPTELTQSQMLHiaqqiaaGMVYLASQHFVHRDLATRNCLVG---ENLLV 534
Cdd:cd14084    87 YIVLELMEGGEL--FDRVVSN----KRLKEAICKLYFYQMLL-------AVKYLHSNGIIHRDLKPENVLLSsqeEECLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGMSRDVYSTDYYRVGGHTMLpirWMPPE---SIMYRKFTTESDVWSLGVVLWEIFTyGKQPW-YQLSNNEVIECI 610
Cdd:cd14084   154 KITDFGLSKILGETSLMKTLCGTPT---YLAPEvlrSFGTEGYTRAVDCWSLGVILFICLS-GYPPFsEEYTQMSLKEQI 229

                  ....
gi 1610576541 611 TQGR 614
Cdd:cd14084   230 LSGK 233
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
388-592 9.22e-19

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 87.89  E-value: 9.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLcpeqDKIlVAVKTLK--DASDNARKDFH------------REAELLTNLQHEHIVKFYGVCVE 453
Cdd:PTZ00024   17 LGEGTYGKVEKAYDTLT----GKI-VAIKKVKiiEISNDVTKDRQlvgmcgihfttlRELKIMNEIKHENIMGLVDVYVE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMkHGDLNKFLrahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL 533
Cdd:PTZ00024   92 GDFINLVMDIM-ASDLKKVV-------------DRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGI 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 534 VKIGDFGMSR----DVYSTDYYRVggHTMLPIRWMPPE--SIMYR---------KFTTESDVWSLGVVLWEIFT 592
Cdd:PTZ00024  158 CKIADFGLARrygyPPYSDTLSKD--ETMQRREEMTSKvvTLWYRapellmgaeKYHFAVDMWSVGCIFAELLT 229
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
384-589 1.15e-18

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 86.21  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAEcyNLcpeQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd06613     4 LIQRIGSGTYGDVYKAR--NI---ATGELAAVKVIKLEPGDDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd06613    79 CGGGSLQDIYQVTGP-------------LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSA 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 544 DVYSTDYYR---VGghTMLpirWMPPESIMYRK---FTTESDVWSLGVVLWE 589
Cdd:cd06613   146 QLTATIAKRksfIG--TPY---WMAPEVAAVERkggYDGKCDIWALGITAIE 192
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
388-540 1.17e-18

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 82.88  E-value: 1.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLCPEqdkilVAVKTLKDASDNARKDFHREAE-LLTNLQHE-HIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIG-----VAVKIGDDVNNEEGEDLESEMDiLRRLKGLElNIPKVLVTEDVDGPNILLMELVK 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 466 HGDLNKFLRAhgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd13968    76 GGTLIAYTQE--------------EELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
388-623 1.24e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 87.17  E-value: 1.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynlcpeQDKI---LVAVKTLKdaSDNARKDFH----REAELLTNLQHEHIVKFYGVCV-------- 452
Cdd:cd07864    15 IGEGTYGQVYKA--------KDKDtgeLVALKKVR--LDNEKEGFPitaiREIKILRQLNHRSVVNLKEIVTdkqdaldf 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 453 --EGDPLIMVFEYMKHgDLNKFLRAHGPDavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGE 530
Cdd:cd07864    85 kkDKGAFYLVFEYMDH-DLMGLLESGLVH------------FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 531 NLLVKIGDFGMSRdVYSTDYYRVGGHTMLPIRWMPPESIM-YRKFTTESDVWSLGVVLWEIFTygKQPWYQlSNNEV--I 607
Cdd:cd07864   152 KGQIKLADFGLAR-LYNSEESRPYTNKVITLWYRPPELLLgEERYGPAIDVWSCGCILGELFT--KKPIFQ-ANQELaqL 227
                         250
                  ....*....|....*.
gi 1610576541 608 ECITqgRVLQRPrtCP 623
Cdd:cd07864   228 ELIS--RLCGSP--CP 239
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
423-641 3.30e-18

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 86.80  E-value: 3.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 423 DNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLnkflrahgpdavlmaEGnppTELTQSQML-HIA 501
Cdd:PLN00034  113 DTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSL---------------EG---THIADEQFLaDVA 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 502 QQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSrdvystdyyRVGGHTMLP-------IRWMPPESI----- 569
Cdd:PLN00034  175 RQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVS---------RILAQTMDPcnssvgtIAYMSPERIntdln 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 570 --MYRKFTteSDVWSLGVVLWEI------FTYGKQ-PWYQLSnnevieC-ITQGRVLQRPRTCPQEVYELMLGCWQREPH 639
Cdd:PLN00034  246 hgAYDGYA--GDIWSLGVSILEFylgrfpFGVGRQgDWASLM------CaICMSQPPEAPATASREFRHFISCCLQREPA 317

                  ..
gi 1610576541 640 MR 641
Cdd:PLN00034  318 KR 319
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
386-641 3.63e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 84.79  E-value: 3.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcynlcPEQDKILVAVK--TLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd08221     6 RVLGRGAFGEAVLYR-----KTEDNSLVVWKevNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNkflrahgpDAVLMAEGnpptELTQSQM-LHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd08221    81 CNGGNLH--------DKIAQQKN----QLFPEEVvLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGIS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 RdVYSTDYYRVGGHTMLPIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQpwYQLSN--NEVIEcITQGRVLQRPR 620
Cdd:cd08221   149 K-VLDSESSMAESIVGTPY-YMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRT--FDATNplRLAVK-IVQGEYEDIDE 223
                         250       260
                  ....*....|....*....|.
gi 1610576541 621 TCPQEVYELMLGCWQREPHMR 641
Cdd:cd08221   224 QYSEEIIQLVHDCLHQDPEDR 244
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
381-654 4.37e-18

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 85.08  E-value: 4.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAECYnlcpeQDKILVAVKTLK--DASD-NARKDFHREAELLTNLQHEHIVKFYGVCVEGDPL 457
Cdd:cd08229    25 NFRIEKKIGRGQFSEVYRATCL-----LDGVPVALKKVQifDLMDaKARADCIKEIDLLKQLNHPNVIKYYASFIEDNEL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLNKFLRAHGPDAVLMAEgnppteltqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd08229   100 NIVLELADAGDLSRMIKHFKKQKRLIPE---------KTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 538 DFGMSRDVYSTDyyrVGGHTMLPI-RWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIEC--ITQGR 614
Cdd:cd08229   171 DLGLGRFFSSKT---TAAHSLVGTpYYMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYGDKMNLYSLCkkIEQCD 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1610576541 615 VLQRPRT-CPQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd08229   247 YPPLPSDhYSEELRQLVNMCINPDPEKRPDITYVYDVAKRM 287
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
388-597 5.22e-18

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 84.20  E-value: 5.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLaecynLCPEQDKILVAVKTLKDAS---DNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd05572     1 LGVGGFGRVEL-----VQLKSKGRTFALKCVKKRHivqTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHGpdavLMAEgnpptelTQSQMLhIAQQIAAgMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd05572    76 LGGELWTILRDRG----LFDE-------YTARFY-TACVVLA-FEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKK 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 545 VYS---------TDYYrvgghtmlpirwMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQP 597
Cdd:cd05572   143 LGSgrktwtfcgTPEY------------VAPEIILNKGYDFSVDYWSLGILLYELLT-GRPP 191
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
388-592 6.62e-18

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 85.11  E-value: 6.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcpEQDKILVAVKTLKdaSDNARKDFH----REAELLTNLQHEHIVKFYGVCV--EGDPLIMVF 461
Cdd:cd07845    15 IGEGTYGIVYRARD-----TTSGEIVALKKVR--MDNERDGIPisslREITLLLNLRHPNIVELKEVVVgkHLDSIFLVM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHgDLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd07845    88 EYCEQ-DLASLLD------------NMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 542 SRdVYSTDYyrvggHTMLP----IRWMPPESIM-YRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd07845   155 AR-TYGLPA-----KPMTPkvvtLWYRAPELLLgCTTYTTAIDMWAVGCILAELLA 204
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
391-615 6.79e-18

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 84.19  E-value: 6.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 391 GAFGKVFLAEcynlcPEQDKILVAVKTLKdASDNARKD-FHR---EAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd05579     4 GAYGRVYLAK-----KKSTGDLYAIKVIK-KRDMIRKNqVDSvlaERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAHGPDAVLMAEgnppteltqsqmlHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD-- 544
Cdd:cd05579    78 GDLYSLLENVGALDEDVAR-------------IYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVgl 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 VYSTDYYRVGGHTMLPIR-----------WMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQG 613
Cdd:cd05579   145 VRRQIKLSIQKKSNGAPEkedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLV-GIPPFHAETPEEIFQNILNG 223

                  ..
gi 1610576541 614 RV 615
Cdd:cd05579   224 KI 225
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
388-641 9.68e-18

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 84.06  E-value: 9.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynLCPEQDKIlVAVKTLK-DASDNARKDFHREAELLTNLQH---EHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd06917     9 VGRGSYGAVYRG----YHVKTGRV-VALKVLNlDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAhGPdavlMAEgnppteltqsqmLHIAQQIAAGMVYLASQH---FVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd06917    84 CEGGSIRTLMRA-GP----IAE------------RYIAVIMREVLVALKFIHkdgIIHRDIKAANILVTNTGNVKLCDFG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDVYSTDYYRVgghTML--PIrWMPPESIMY-RKFTTESDVWSLGVVLWEIfTYGKQPWYQLSNNEVIECITQgrvlQ 617
Cdd:cd06917   147 VAASLNQNSSKRS---TFVgtPY-WMAPEVITEgKYYDTKADIWSLGITTYEM-ATGNPPYSDVDALRAVMLIPK----S 217
                         250       260
                  ....*....|....*....|....*....
gi 1610576541 618 RPRTCPQEVY-----ELMLGCWQREPHMR 641
Cdd:cd06917   218 KPPRLEGNGYspllkEFVAACLDEEPKDR 246
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
387-592 1.10e-17

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 83.71  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKT--LKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd07860     7 KIGEGTYGVVYKAR-----NKLTGEVVALKKirLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 kHGDLNKFLrahgpdavlmaEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd07860    82 -HQDLKKFM-----------DASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARA 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1610576541 545 VYSTdyYRVGGHTMLPIRWMPPESIMYRKF-TTESDVWSLGVVLWEIFT 592
Cdd:cd07860   150 FGVP--VRTYTHEVVTLWYRAPEILLGCKYySTAVDIWSLGCIFAEMVT 196
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
379-633 1.17e-17

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 83.04  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLkrelGEGAFGKVFLAecYNlcpEQDKILVA--VKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDP 456
Cdd:cd13983     4 KFNEVL----GRGSFKTVYRA--FD---TEEGIEVAwnEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVF--EYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQH--FVHRDLATRNCLV-GEN 531
Cdd:cd13983    75 KEVIFitELMTSGTLKQYLKRFKR-------------LKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFInGNT 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 532 LLVKIGDFGMSRDVYSTDYYRVGGhtmLPiRWMPPEsiMYRKFTTES-DVWSLGVVLWEIFTyGKQPWYQLSNN-EVIEC 609
Cdd:cd13983   142 GEVKIGDLGLATLLRQSFAKSVIG---TP-EFMAPE--MYEEHYDEKvDIYAFGMCLLEMAT-GEYPYSECTNAaQIYKK 214
                         250       260
                  ....*....|....*....|....*...
gi 1610576541 610 ITQGrvlQRP----RTCPQEVYELMLGC 633
Cdd:cd13983   215 VTSG---IKPeslsKVKDPELKDFIEKC 239
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
381-646 1.50e-17

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 84.20  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAECynlcpEQDKILVAVKTLKD----ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDP 456
Cdd:cd05619     6 DFVLHKMLGKGSFGKVFLAEL-----KGTNQFFAIKALKKdvvlMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTKEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLRA-HGPDAvlmaegnppteltqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd05619    81 LFFVMEYLNGGDLMFHIQScHKFDL--------------PRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSRDVYSTDyYRVGGHTMLPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd05619   147 IADFGMCKENMLGD-AKTSTFCGTP-DYIAPEILLGQKYNTSVDWWSFGVLLYEMLI-GQSPFHGQDEEELFQSIRMDNP 223
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1610576541 616 LQrPRTCPQEVYELMLGCWQREPHMRKNIKG 646
Cdd:cd05619   224 FY-PRWLEKEAKDILVKLFVREPERRLGVRG 253
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
387-595 1.67e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 83.25  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVK--TLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd07839     7 KIGEGTYGTVFKAK-----NRETHEIVALKrvRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHgDLNKFLRAhgpdavlmAEGNPPTELTQSQMLhiaqQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd07839    82 DQ-DLKKYFDS--------CNGDIDPEIVKSFMF----QLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARA 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 545 V------YS----TDYYRvgghtmlpirwmPPESIMYRK-FTTESDVWSLGVVLWEIFTYGK 595
Cdd:cd07839   149 FgipvrcYSaevvTLWYR------------PPDVLFGAKlYSTSIDMWSAGCIFAELANAGR 198
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
384-585 2.46e-17

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 82.74  E-value: 2.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECYNlcpeqDKILVAVKTLKDASDNaRKDFHREAELLTNL-QHEHIVKFYGV------CVEGDP 456
Cdd:cd06608    10 LVEVIGEGTYGKVYKARHKK-----TGQLAAIKIMDIIEDE-EEEIKLEINILRKFsNHPNIATFYGAfikkdpPGGDDQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHG---DLNKFLRAHGpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL 533
Cdd:cd06608    84 LWLVMEYCGGGsvtDLVKGLRKKG------------KRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAE 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1610576541 534 VKIGDFGMSRDVYSTDYYRvggHTML--PIrWMPPESIMYRK-----FTTESDVWSLGV 585
Cdd:cd06608   152 VKLVDFGVSAQLDSTLGRR---NTFIgtPY-WMAPEVIACDQqpdasYDARCDVWSLGI 206
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
383-648 2.65e-17

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 82.14  E-value: 2.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFLAECYNLcpeqdKILVAVKTL--KDASDNARKDF-HREAELLTNLQHEHIVKFYGVCVEGDPLI- 458
Cdd:cd14165     4 ILGINLGEGSYAKVKSAYSERL-----KCNVAIKIIdkKKAPDDFVEKFlPRELEILARLNHKSIIKTYEIFETSDGKVy 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLRAHGPdavlmaegnpPTELTQSQMLHiaqQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGD 538
Cdd:cd14165    79 IVMELGVQGDLLEFIKLRGA----------LPEDVARKMFH---QLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 539 FGMSRDVYSTDyyrvGGHTML------PIRWMPPESIMYRKFTTE-SDVWSLGVVLWeIFTYGKQPwYQLSNNEVIECIT 611
Cdd:cd14165   146 FGFSKRCLRDE----NGRIVLsktfcgSAAYAAPEVLQGIPYDPRiYDIWSLGVILY-IMVCGSMP-YDDSNVKKMLKIQ 219
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1610576541 612 QGRVLQRPRTCPQ--EVYELMLGCWQREPHMRKNIKGIH 648
Cdd:cd14165   220 KEHRVRFPRSKNLtsECKDLIYRLLQPDVSQRLCIDEVL 258
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
388-602 3.90e-17

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 82.03  E-value: 3.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynlcpeQDKI---LVAVK--TLKDASDNARKdFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14046    14 LGKGAFGQVVKV--------RNKLdgrYYAIKkiKLRSESKNNSR-ILREVMLLSRLNHQHVVRYYQAWIERANLYIQME 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKhgdlNKFLRAhgpdavLMAEGNpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd14046    85 YCE----KSTLRD------LIDSGL---FQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLA 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 543 RDV--------------YSTDYYRVGGHTML--PIRWMPPE--SIMYRKFTTESDVWSLGVVLWEIftygkqpWYQLS 602
Cdd:cd14046   152 TSNklnvelatqdinksTSAALGSSGDLTGNvgTALYVAPEvqSGTKSTYNEKVDMYSLGIIFFEM-------CYPFS 222
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
387-620 4.74e-17

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 81.33  E-value: 4.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAECYNlcpeqDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd06648    14 KIGEGSTGIVCIATDKS-----TGRQVAVKKMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAhgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVy 546
Cdd:cd06648    89 GALTDIVTH--------------TRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQV- 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 547 STDYYRVGGHTMLPIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYqlsNNEVIECITQGRVLQRPR 620
Cdd:cd06648   154 SKEVPRRKSLVGTPY-WMAPEVISRLPYGTEVDIWSLGIMVIEMVD-GEPPYF---NEPPLQAMKRIRDNEPPK 222
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
388-607 6.43e-17

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 81.60  E-value: 6.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecYNLcpeQDKILVAVKT---LKDASDNARKDFH----REAELLTNLQHEHIVKFYGVC-VEGDPLIM 459
Cdd:cd13990     8 LGKGGFSEVYKA--FDL---VEQRYVACKIhqlNKDWSEEKKQNYIkhalREYEIHKSLDHPRIVKLYDVFeIDTDSFCT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHgpdavlmaeGNPPTELTQSqmlhIAQQIAAGMVYLA--SQHFVHRDLATRNCLVGEN---LLV 534
Cdd:cd13990    83 VLEYCDGNDLDFYLKQH---------KSIPEREARS----IIMQVVSALKYLNeiKPPIIHYDLKPGNILLHSGnvsGEI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGMSR-------DVYSTDYYRVGGHTMlpirW-MPPESIM----YRKFTTESDVWSLGVVLWEIFtYGKQPWYQLS 602
Cdd:cd13990   150 KITDFGLSKimddesyNSDGMELTSQGAGTY----WyLPPECFVvgktPPKISSKVDVWSVGVIFYQML-YGRKPFGHNQ 224

                  ....*
gi 1610576541 603 NNEVI 607
Cdd:cd13990   225 SQEAI 229
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
409-651 7.93e-17

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 81.09  E-value: 7.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 409 DKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVcVEGDPLIM-VFEYMKHGDLNKFL--RAHGPDAVLMae 485
Cdd:cd14044    30 DKKVVILKDLKNNEGNFTEKQKIELNKLLQIDYYNLTKFYGT-VKLDTMIFgVIEYCERGSLRDVLndKISYPDGTFM-- 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 486 gnpPTELTQSQMLHIAQqiaaGMVYL-ASQHFVHRDLATRNCLVGENLLVKIGDFgmsrdvystdyyrvGGHTMLPIR-- 562
Cdd:cd14044   107 ---DWEFKISVMYDIAK----GMSYLhSSKTEVHGRLKSTNCVVDSRMVVKITDF--------------GCNSILPPSkd 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 563 -WMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECITqgRVLQRPRTCP--------------QEVY 627
Cdd:cd14044   166 lWTAPEHLRQAGTSQKGDVYSYGIIAQEIILR-KETFYTAACSDRKEKIY--RVQNPKGMKPfrpdlnlesagereREVY 242
                         250       260
                  ....*....|....*....|....
gi 1610576541 628 ELMLGCWQREPHMRKNIKGIHTLL 651
Cdd:cd14044   243 GLVKNCWEEDPEKRPDFKKIENTL 266
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
384-588 8.16e-17

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 80.64  E-value: 8.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAEcynLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd14072     4 LLKTIGKGNFAKVKLAR---HVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGPdavlMAEGNPPTELtqsqmlhiaQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd14072    81 ASGGEVFDYLVAHGR----MKEKEARAKF---------RQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSN 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 544 DvystdyYRVGGH--TML---PirWMPPESIMYRKFT-TESDVWSLGVVLW 588
Cdd:cd14072   148 E------FTPGNKldTFCgspP--YAAPELFQGKKYDgPEVDVWSLGVILY 190
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
388-586 8.24e-17

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 80.35  E-value: 8.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLaecynlCPE-QDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd14103     1 LGRGKFGTVYR------CVEkATGKELAAKFIKCRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLnkFLRAHGPDavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRN--CLVGENLLVKIGDFGMSRD 544
Cdd:cd14103    75 GEL--FERVVDDD----------FELTERDCILFMRQICEGVQYMHKQGILHLDLKPENilCVSRTGNQIKIIDFGLARK 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 545 VYSTDYYRVGGHTmlPiRWMPPESIMYRKFTTESDVWSLGVV 586
Cdd:cd14103   143 YDPDKKLKVLFGT--P-EFVAPEVVNYEPISYATDMWSVGVI 181
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
387-591 9.52e-17

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 80.61  E-value: 9.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARkdfhREAELLTNLQHEHIVKFYGvCVEG-----------D 455
Cdd:cd14047    13 LIGSGGFGQVFKAK-----HRIDGKTYAIKRVKLNNEKAE----REVKALAKLDHPNIVRYNG-CWDGfdydpetsssnS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 P------LIMVFEYMKHGDLNKFL--RAHGPDAVLMAegnppteltqsqmLHIAQQIAAGMVYLASQHFVHRDLATRNCL 527
Cdd:cd14047    83 SrsktkcLFIQMEFCEKGTLESWIekRNGEKLDKVLA-------------LEIFEQITKGVEYIHSKKLIHRDLKPSNIF 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 528 VGENLLVKIGDFGMSRDVySTDYYRVGGHTMLpiRWMPPESIMYRKFTTESDVWSLGVVLWEIF 591
Cdd:cd14047   150 LVDTGKVKIGDFGLVTSL-KNDGKRTKSKGTL--SYMSPEQISSQDYGKEVDIYALGLILFELL 210
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
379-647 1.04e-16

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 80.72  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLI 458
Cdd:cd05076    12 RTNIYEGRLLVEGSGEPEEDKELVPGRDRGQELRVVLKVLDPSHHDIALAFFETASLMSQVSHTHLVFVHGVCVRGSENI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLRAHgpdavlmaEGNPPTELTqsqmLHIAQQIAAGMVYLASQHFVHRDLATRNCLV-------GEN 531
Cdd:cd05076    92 MVEEFVEHGPLDVWLRKE--------KGHVPMAWK----FVVARQLASALSYLENKNLVHGNVCAKNILLarlgleeGTS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 532 LLVKIGDFGMSRDVYSTDyyrvggHTMLPIRWMPPESI-MYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECI 610
Cdd:cd05076   160 PFIKLSDPGVGLGVLSRE------ERVERIPWIAPECVpGGNSLSTAADKWGFGATLLEICFNGEAPLQSRTPSEKERFY 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1610576541 611 TQGRVLQRPrTCPqEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd05076   234 QRQHRLPEP-SCP-ELATLISQCLTYEPTQRPSFRTI 268
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
388-613 1.04e-16

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 80.05  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcpEQDKILVAVKTLKD--ASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd14050     9 LGEGSFGEVFKVRS-----REDGKLYAVKRSRSrfRGEKDRKRKLEEVERHEKLgEHPNCVRFIKAWEEKGILYIQTELC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KhGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd14050    84 D-TSLQQYCEETH-------------SLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVE 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 545 VYSTDyyrVGGHTMLPIRWMPPEsIMYRKFTTESDVWSLGVVLWEIFTY-----GKQPWYQLSNNEVIECITQG 613
Cdd:cd14050   150 LDKED---IHDAQEGDPRYMAPE-LLQGSFTKAADIFSLGITILELACNlelpsGGDGWHQLRQGYLPEEFTAG 219
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
387-626 1.21e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 80.85  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcyNLcpEQDKILVAVKTLKDASDNARKDFH--REAELLTNLQ---HEHIVKFYGVCV-----EGDP 456
Cdd:cd07862     8 EIGEGAYGKVFKAR--DL--KNGGRFVALKRVRVQTGEEGMPLStiREVAVLRHLEtfeHPNVVRLFDVCTvsrtdRETK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHgDLNKFLRAhgpdavlMAEGNPPTELTQSQMLHIAQqiaaGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd07862    84 LTLVFEHVDQ-DLTTYLDK-------VPEPGVPTETIKDMMFQLLR----GLDFLHSHRVVHRDLKPQNILVTSSGQIKL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSRdVYStdyYRVGGHTMLPIRWM-PPESIMYRKFTTESDVWSLGVVLWEIFTygKQPWYQlSNNEVIECitqGRV 615
Cdd:cd07862   152 ADFGLAR-IYS---FQMALTSVVVTLWYrAPEVLLQSSYATPVDLWSVGCIFAEMFR--RKPLFR-GSSDVDQL---GKI 221
                         250
                  ....*....|....*.
gi 1610576541 616 -----LQRPRTCPQEV 626
Cdd:cd07862   222 ldvigLPGEEDWPRDV 237
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
382-592 2.02e-16

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 80.24  E-value: 2.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKRELGEGAFGKVFLAECYNlcpeqDKILVAVK-TLKDasdnarKDF-HREAELLTNLQHEHIVKFYGVCVEGDP--- 456
Cdd:cd14137     6 YTIEKVIGSGSFGVVYQAKLLE-----TGEVVAIKkVLQD------KRYkNRELQIMRRLKHPNIVKLKYFFYSSGEkkd 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 ---LIMVFEYMKhGDLNKFLRAHgpdavLMAEGNPPteltqsqMLHI---AQQIAAGMVYLASQHFVHRDLATRNCLV-G 529
Cdd:cd14137    75 evyLNLVMEYMP-ETLYRVIRHY-----SKNKQTIP-------IIYVklySYQLFRGLAYLHSLGICHRDIKPQNLLVdP 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 530 ENLLVKIGDFG----MSRDVYSTDY-----YRvgghtmlpirwmPPESIM-YRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd14137   142 ETGVLKLCDFGsakrLVPGEPNVSYicsryYR------------APELIFgATDYTTAIDIWSAGCVLAELLL 202
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
384-592 2.03e-16

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 79.62  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFlaECYNLcpeQDKILVAVKTLKDasdnaRKDFHR----EAELLTNLQ------HEHIVKFYGVCVE 453
Cdd:cd14133     3 VLEVLGKGTFGQVV--KCYDL---LTGEEVALKIIKN-----NKDYLDqsldEIRLLELLNkkdkadKYHIVRLKDVFYF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMKHG--DLNKFLRAHGpdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGEN 531
Cdd:cd14133    73 KNHLCIVFELLSQNlyEFLKQNKFQY--------------LSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASY 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 532 --LLVKIGDFGMSrdVYSTD---------YYRVgghtmlpirwmpPESIMYRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd14133   139 srCQIKIIDFGSS--CFLTQrlysyiqsrYYRA------------PEVILGLPYDEKIDMWSLGCILAELYT 196
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
388-641 2.44e-16

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 80.52  E-value: 2.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcyNLCPEQDKILVAVKTLKDASDNARKDFHREAE--LLTNLQHEHIVKF-YGVCVEGDpLIMVFEYM 464
Cdd:cd05582     3 LGQGSFGKVFLVR--KITGPDAGTLYAMKVLKKATLKVRDRVRTKMErdILADVNHPFIVKLhYAFQTEGK-LYLILDFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLnkFLRAhgPDAVLMAEgnppteltQSQMLHIAQqIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR- 543
Cdd:cd05582    80 RGGDL--FTRL--SKEVMFTE--------EDVKFYLAE-LALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKe 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 --DVYSTDYYRVGghtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRvLQRPRT 621
Cdd:cd05582   147 siDHEKKAYSFCG-----TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQGKDRKETMTMILKAK-LGMPQF 219
                         250       260
                  ....*....|....*....|
gi 1610576541 622 CPQEVYELMLGCWQREPHMR 641
Cdd:cd05582   220 LSPEAQSLLRALFKRNPANR 239
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
388-597 3.33e-16

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 79.26  E-value: 3.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynlCPEQDKILVAVKT--LKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd07835     7 IGEGTYGVVYKA-----RDKLTGEIVALKKirLETEDEGVPSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEFLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HgDLNKFLRAHGPDavlmaeGNPPtELTQSQMLhiaqQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR-- 543
Cdd:cd07835    82 L-DLKKYMDSSPLT------GLDP-PLIKSYLY----QLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARaf 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 544 ----DVYS----TDYYRVgghtmlpirwmpPESIM-YRKFTTESDVWSLGVVLWEIFTygKQP 597
Cdd:cd07835   150 gvpvRTYThevvTLWYRA------------PEILLgSKHYSTPVDIWSVGCIFAEMVT--RRP 198
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
388-596 3.40e-16

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 79.53  E-value: 3.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDAS-DNARKDFHREAELLTNLQHEHIVKFYGVCVEGDP---------- 456
Cdd:cd14048    14 LGRGGFGVVFEAK-----NKVDDCNYAVKRIRLPNnELAREKVLREVRALAKLDHPGIVRYFNAWLERPPegwqekmdev 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 -LIMVFEYMKHGDLNKFLRAHgpdavLMAEGNPpteltQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd14048    89 yLYIQMQLCRKENLKDWMNRR-----CTMESRE-----LFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVK 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 536 IGDFGMSR---------------DVYSTDYYRVGghTMLpirWMPPESIMYRKFTTESDVWSLGVVLWE-IFTYGKQ 596
Cdd:cd14048   159 VGDFGLVTamdqgepeqtvltpmPAYAKHTGQVG--TRL---YMSPEQIHGNQYSEKVDIFALGLILFElIYSFSTQ 230
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
388-598 3.52e-16

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 78.75  E-value: 3.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARkdFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHG 467
Cdd:cd14186     9 LGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQR--VRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 468 DLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYS 547
Cdd:cd14186    87 EMSRYLK------------NRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKM 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 548 TD--YYRVGGHTmlpiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd14186   155 PHekHFTMCGTP----NYISPEIATRSAHGLESDVWSLGCMFYTLLV-GRPPF 202
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
386-615 4.24e-16

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 79.16  E-value: 4.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDAsDNARKD----FHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd05580     7 KTLGTGSFGRVRLVK-----HKDSGKYYALKILKKA-KIIKLKqvehVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAhgpdavlmaEGNPPTELTQsqmlHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd05580    81 EYVPGGELFSLLRR---------SGRFPNDVAK----FYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGF 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 542 SRDVYSTDYYRVGGHtmlpiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd05580   148 AKRVKDRTYTLCGTP-----EYLAPEIILSKGHGKAVDWWALGILIYEMLA-GYPPFFDENPMKIYEKILEGKI 215
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
384-588 4.68e-16

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 78.58  E-value: 4.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAeCYNLCPEQdkilVAVKTLKDAS---DNARkdFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:cd14078     7 LHETIGSGGFAKVKLA-THILTGEK----VAIKIMDKKAlgdDLPR--VKTEIEALKNLSHQHICRLYHVIETDNKIFMV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd14078    80 LEYCPGGELFDYIVAK-------------DRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFG 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1610576541 541 MSRDVYSTDYYRVGGHTMLPIrWMPPESIMYRKFT-TESDVWSLGVVLW 588
Cdd:cd14078   147 LCAKPKGGMDHHLETCCGSPA-YAAPELIQGKPYIgSEADVWSMGVLLY 194
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
384-598 4.85e-16

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 79.24  E-value: 4.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAecYNlcpEQDKILVAVKTLKDASDNARKDFHR--------------------------EAELLT 437
Cdd:cd14199     6 LKDEIGKGSYGVVKLA--YN---EDDNTYYAMKVLSKKKLMRQAGFPRrppprgaraapegctqprgpiervyqEIAILK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 438 NLQHEHIVKFygVCVEGDP----LIMVFEYMKHGdlnkflrahgpdAVLMAEGNPPteLTQSQMLHIAQQIAAGMVYLAS 513
Cdd:cd14199    81 KLDHPNVVKL--VEVLDDPsedhLYMVFELVKQG------------PVMEVPTLKP--LSEDQARFYFQDLIKGIEYLHY 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 514 QHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVggHTMLPIRWMPPESIM-YRK-FTTES-DVWSLGVVLWeI 590
Cdd:cd14199   145 QKIIHRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLT--NTVGTPAFMAPETLSeTRKiFSGKAlDVWAMGVTLY-C 221

                  ....*...
gi 1610576541 591 FTYGKQPW 598
Cdd:cd14199   222 FVFGQCPF 229
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
388-615 5.89e-16

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 78.08  E-value: 5.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLaecynlCPEQ-DKILVAVKTLKDASDNaRKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd14006     1 LGRGRFGVVKR------CIEKaTGREFAAKFIPKRDKK-KEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL--LVKIGDFGMSRD 544
Cdd:cd14006    74 GELLDRLAERG-------------SLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLARK 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 545 VYSTDYYRvggHTMLPIRWMPPESIMYRKFTTESDVWSLGVVlweifTY----GKQPWYQLSNNEVIECITQGRV 615
Cdd:cd14006   141 LNPGEELK---EIFGTPEFVAPEIVNGEPVSLATDMWSIGVL-----TYvllsGLSPFLGEDDQETLANISACRV 207
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
375-595 7.63e-16

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 79.14  E-value: 7.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 375 QHI-KRHNIVLKreLGEGAFGKVFLAECynlcpEQDKILVAVKTLKDASDN---ARKDFhREAELLTNL-QHEHIVKFYG 449
Cdd:cd07852     3 KHIlRRYEILKK--LGKGAYGIVWKAID-----KKTGEVVALKKIFDAFRNatdAQRTF-REIMFLQELnDHPNIIKLLN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 450 VC-VEGDPLI-MVFEYMKhGDLNKFLRAHgpdaVLmaegnppteltqsQMLH---IAQQIAAGMVYLASQHFVHRDLATR 524
Cdd:cd07852    75 VIrAENDKDIyLVFEYME-TDLHAVIRAN----IL-------------EDIHkqyIMYQLLKALKYLHSGGVIHRDLKPS 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 525 NCLVGENLLVKIGDFGMSRDVYS----------TDYyrvgghtmLPIRWM-PPESIM-YRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd07852   137 NILLNSDCRVKLADFGLARSLSQleeddenpvlTDY--------VATRWYrAPEILLgSTRYTKGVDMWSVGCILGEMLL 208

                  ...
gi 1610576541 593 yGK 595
Cdd:cd07852   209 -GK 210
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
388-617 9.19e-16

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 79.25  E-value: 9.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKD---FHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd05573     9 IGRGAFGEVWLVR-----DKDTGQVYAMKILRKSDMLKREQiahVRAERDILADADSPWIVRLHYAFQDEDHLYLVMEYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHGpdaVLmaegnppTEltqsqmlHIAQQIAAGMV----YLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd05573    84 PGGDLMNLLIKYD---VF-------PE-------ETARFYIAELVlaldSLHKLGFIHRDIKPDNILLDADGHIKLADFG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDVYSTD---YYRVGGHTML------PIRW------------------MPPESIMYRKFTTESDVWSLGVVLWEIFtY 593
Cdd:cd05573   147 LCTKMNKSGdreSYLNDSVNTLfqdnvlARRRphkqrrvraysavgtpdyIAPEVLRGTGYGPECDWWSLGVILYEML-Y 225
                         250       260
                  ....*....|....*....|....
gi 1610576541 594 GKQPWYQLSNNEvieciTQGRVLQ 617
Cdd:cd05573   226 GFPPFYSDSLVE-----TYSKIMN 244
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
386-591 1.10e-15

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 78.08  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVflaecYNLCPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd07870     6 EKLGEGSYATV-----YKGISRINGQLVALKVISmKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 kHGDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR- 543
Cdd:cd07870    81 -HTDLAQYMIQH------------PGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARa 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 544 -----DVYSTDyyrvgghtMLPIRWMPPESIM-YRKFTTESDVWSLGVVLWEIF 591
Cdd:cd07870   148 ksipsQTYSSE--------VVTLWYRPPDVLLgATDYSSALDIWGAGCIFIEML 193
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
381-590 1.16e-15

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 77.76  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAECYNLcpeqdKILVAVKTLKDASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDP--- 456
Cdd:cd13985     1 RYQVTKQLGEGGFSYVYLAHDVNT-----GRRYALKRMYFNDEEQLRVAIKEIEIMKRLcGHPNIVQYYDSAILSSEgrk 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 -LIMVFEYMKhGDLNKFLrahgpdavlmaEGNPPTELTQSQMLHIAQQIAAGMVYLASQH--FVHRDLATRNCLVGENLL 533
Cdd:cd13985    76 eVLLLMEYCP-GSLVDIL-----------EKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGR 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 534 VKIGDFG-MSRDVYStdYYR----------VGGHTMLPIRwmPPESI-MYRKF--TTESDVWSLGVVLWEI 590
Cdd:cd13985   144 FKLCDFGsATTEHYP--LERaeevniieeeIQKNTTPMYR--APEMIdLYSKKpiGEKADIWALGCLLYKL 210
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
387-599 1.45e-15

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 77.72  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd06659    28 KIGEGSTGVVCIAR-----EKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAhgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG----MS 542
Cdd:cd06659   103 GALTDIVSQ--------------TRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGfcaqIS 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 543 RDV------YSTDYyrvgghtmlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWY 599
Cdd:cd06659   169 KDVpkrkslVGTPY------------WMAPEVISRCPYGTEVDIWSLGIMVIEMVD-GEPPYF 218
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
413-654 1.49e-15

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 77.21  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 413 VAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKflrahgpdaVLMAEGNPpteL 492
Cdd:cd14045    33 VAIKKIAKKSFTLSKRIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLND---------VLLNEDIP---L 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 493 TQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIR-WMPPE--SI 569
Cdd:cd14045   101 NWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTTYRKEDGSENASGYQQRLMQvYLPPEnhSN 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 570 MYRKFTTESDVWSLGVVLWEIFT---------YGKQPWYQLSNNEVIECITQGRVlqrprTCPQEVYELMLGCWQREPHM 640
Cdd:cd14045   181 TDTEPTQATDVYSYAIILLEIATrndpvpeddYSLDEAWCPPLPELISGKTENSC-----PCPADYVELIRRCRKNNPAQ 255
                         250
                  ....*....|....
gi 1610576541 641 RKNIKGIHTLLQNL 654
Cdd:cd14045   256 RPTFEQIKKTLHKI 269
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
384-611 1.59e-15

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 76.97  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFlaecyNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd14191     6 IEERLGSGKFGQVF-----RLVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLnkFLRAHGPDavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRN--CLVGENLLVKIGDFGM 541
Cdd:cd14191    81 VSGGEL--FERIIDED----------FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTKIKLIDFGL 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SRDVYSTDYYRVGGHTmlPiRWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECIT 611
Cdd:cd14191   149 ARRLENAGSLKVLFGT--P-EFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANVT 214
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
387-619 1.76e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 77.46  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcyNLCPEQdkiLVAVKT--LKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd07861     7 KIGEGTYGVVYKGR--NKKTGQ---IVAMKKirLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHgDLNKFLRAHGPDAVLmaegnpPTELTQSQMlhiaQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd07861    82 SM-DLKKYLDSLPKGKYM------DAELVKSYL----YQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARA 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 545 VYSTdyYRVGGHTMLPIRWMPPESIM-YRKFTTESDVWSLGVVLWEIFTygKQPWYQlSNNEVIECITQGRVLQRP 619
Cdd:cd07861   151 FGIP--VRVYTHEVVTLWYRAPEVLLgSPRYSTPVDIWSIGTIFAEMAT--KKPLFH-GDSEIDQLFRIFRILGTP 221
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
389-593 1.92e-15

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 77.71  E-value: 1.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 389 GEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVE-GDPLI-MVFEYMKH 466
Cdd:cd07842     9 GRGTYGRVYKAKRKNGKDGKEYAIKKFKGDKEQYTGISQSACREIALLRELKHENVVSLVEVFLEhADKSVyLLFDYAEH 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 gDLN---KFLRAHGPDAVlmaegnpPTELTQSqmlhIAQQIAAGMVYLASQHFVHRDLATRNCLV----GENLLVKIGDF 539
Cdd:cd07842    89 -DLWqiiKFHRQAKRVSI-------PPSMVKS----LLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 540 GMSRDVYS-------------TDYYRVgghtmlpirwmpPESIM-YRKFTTESDVWSLGVVLWEIFTY 593
Cdd:cd07842   157 GLARLFNAplkpladldpvvvTIWYRA------------PELLLgARHYTKAIDIWAIGCIFAELLTL 212
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
384-641 2.86e-15

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 78.76  E-value: 2.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTLkDASDNARKDFHR---EAELLTNLQHEHIVKFYGVCVEGDP---- 456
Cdd:PTZ00283   36 ISRVLGSGATGTVLCAK-----RVSDGEPFAVKVV-DMEGMSEADKNRaqaEVCCLLNCDFFSIVKCHEDFAKKDPrnpe 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 ----LIMVFEYMKHGDLNKFLRAHgpdavlmAEGNPPTELTQSQMLHIaqQIAAGMVYLASQHFVHRDLATRNCLVGENL 532
Cdd:PTZ00283  110 nvlmIALVLDYANAGDLRQEIKSR-------AKTNRTFREHEAGLLFI--QVLLAVHHVHSKHMIHRDIKSANILLCSNG 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECITQ 612
Cdd:PTZ00283  181 LVKLGDFGFSKMYAATVSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTL-KRPFDGENMEEVMHKTLA 259
                         250       260
                  ....*....|....*....|....*....
gi 1610576541 613 GRVLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:PTZ00283  260 GRYDPLPPSISPEMQEIVTALLSSDPKRR 288
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
384-598 3.37e-15

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 76.53  E-value: 3.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAecYNlcpEQDKILVAVKTL--------------------KDASDNARKDF------HREAELLT 437
Cdd:cd14200     4 LQSEIGKGSYGVVKLA--YN---ESDDKYYAMKVLskkkllkqygfprrppprgsKAAQGEQAKPLaplervYQEIAILK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 438 NLQHEHIVKFygVCVEGDP----LIMVFEYMKHGdlnkflrahgpdAVLMAEGNPPteLTQSQMLHIAQQIAAGMVYLAS 513
Cdd:cd14200    79 KLDHVNIVKL--IEVLDDPaednLYMVFDLLRKG------------PVMEVPSDKP--FSEDQARLYFRDIVLGIEYLHY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 514 QHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDyYRVGGHTMLPIrWMPPESIM--YRKFTTES-DVWSLGVVLWeI 590
Cdd:cd14200   143 QKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGND-ALLSSTAGTPA-FMAPETLSdsGQSFSGKAlDVWAMGVTLY-C 219

                  ....*...
gi 1610576541 591 FTYGKQPW 598
Cdd:cd14200   220 FVYGKCPF 227
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
386-615 3.84e-15

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 75.98  E-value: 3.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcynlcpeqdKILV----AVKTLKDASDNARKDfhreaelLTNLQHE-----------HIVKFYGV 450
Cdd:cd05611     2 KPISKGAFGSVYLAK---------KRSTgdyfAIKVLKKSDMIAKNQ-------VTNVKAEraimmiqgespYVAKLYYS 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 451 CVEGDPLIMVFEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGE 530
Cdd:cd05611    66 FQSKDYLYLVMEYLNGGDCASLIKTLGG-------------LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQ 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 531 NLLVKIGDFGMSRDVYSTDYYR--VGghtmLPiRWMPPESIMYRKFTTESDVWSLGVVLWEiFTYGKQPWYQLSNNEVIE 608
Cdd:cd05611   133 TGHLKLTDFGLSRNGLEKRHNKkfVG----TP-DYLAPETILGVGDDKMSDWWSLGCVIFE-FLFGYPPFHAETPDAVFD 206

                  ....*..
gi 1610576541 609 CITQGRV 615
Cdd:cd05611   207 NILSRRI 213
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
380-641 3.90e-15

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 76.07  E-value: 3.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 380 HNIVLKRELGEGAFGKVflaecYNLCPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLI 458
Cdd:cd06619     1 QDIQYQEILGHGNGGTV-----YKAYHLLTRRILAVKVIPlDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRIS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLRAhgPDAVLMaegnppteltqsqmlHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGD 538
Cdd:cd06619    76 ICTEFMDGGSLDVYRKI--PEHVLG---------------RIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCD 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 539 FGMSRD-VYSTDYYRVGGHTmlpirWMPPESIMYRKFTTESDVWSLGVVLWEIfTYGKQPWYQLSNN-------EVIECI 610
Cdd:cd06619   139 FGVSTQlVNSIAKTYVGTNA-----YMAPERISGEQYGIHSDVWSLGISFMEL-ALGRFPYPQIQKNqgslmplQLLQCI 212
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1610576541 611 TQGRVLQRPRTCPQEVY-ELMLGCWQREPHMR 641
Cdd:cd06619   213 VDEDPPVLPVGQFSEKFvHFITQCMRKQPKER 244
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
379-598 5.16e-15

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 75.74  E-value: 5.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFgkvflAECYNLCPEQDKILVAVKTLKD---ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD 455
Cdd:cd14187     6 RRRYVRGRFLGKGGF-----AKCYEITDADTKEVFAGKIVPKsllLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLnkfLRAHgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd14187    81 FVYVVLELCRRRSL---LELH----------KRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVK 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 536 IGDFGMSRDVySTDYYRVGGHTMLPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd14187   148 IGDFGLATKV-EYDGERKKTLCGTP-NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLV-GKPPF 207
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
386-602 5.38e-15

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 76.64  E-value: 5.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVflaecynlCPEQDKIL---VAVKTLKDASD---NARKDfHREAELLTNLQHEHIV------KFYGVCVE 453
Cdd:cd07855    11 ETIGSGAYGVV--------CSAIDTKSgqkVAIKKIPNAFDvvtTAKRT-LRELKILRHFKHDNIIairdilRPKVPYAD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMKhGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL 533
Cdd:cd07855    82 FKDVYVVLDLME-SDLHHIIHSDQP-------------LTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 534 VKIGDFGMSRDV---------YSTDYyrvgghtmLPIRWMPPESIMY--RKFTTESDVWSLGVVLWE------IFTyGKQ 596
Cdd:cd07855   148 LKIGDFGMARGLctspeehkyFMTEY--------VATRWYRAPELMLslPEYTQAIDMWSVGCIFAEmlgrrqLFP-GKN 218

                  ....*.
gi 1610576541 597 PWYQLS 602
Cdd:cd07855   219 YVHQLQ 224
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
387-591 5.42e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 76.15  E-value: 5.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLK--DASDNARKDFHREAELLTNLQ---HEHIVKFYGVCV-----EGDP 456
Cdd:cd07863     7 EIGVGAYGTVYKAR-----DPHSGHFVALKSVRvqTNEDGLPLSTVREVALLKRLEafdHPNIVRLMDVCAtsrtdRETK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHgDLNKFLrahgpdavlmaEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd07863    82 VTLVFEHVDQ-DLRTYL-----------DKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 537 GDFGMSRdVYStdYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIF 591
Cdd:cd07863   150 ADFGLAR-IYS--CQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMF 201
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
384-598 6.31e-15

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 75.28  E-value: 6.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECYNLCpeqdkILVAVKTL---KDASDNARKDFHREAELLTNLQHEHIVKFYGvCVE--GDPLI 458
Cdd:cd14164     4 LGTTIGEGSFSKVKLATSQKYC-----CKVAIKIVdrrRASPDFVQKFLPRELSILRRVNHPNIVQMFE-CIEvaNGRLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLRAHgpdavlmaegNPPTELTQSqmlhIAQQIAAGMVYLASQHFVHRDLATRNCLV-GENLLVKIG 537
Cdd:cd14164    78 IVMEAAATDLLQKIQEVH----------HIPKDLARD----MFAQMVGAVNYLHDMNIVHRDLKCENILLsADDRKIKIA 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 538 DFGMSRDVYStdyYRVGGHTMLPIR-WMPPESIMYRKFTTES-DVWSLGVVLWEIFTyGKQPW 598
Cdd:cd14164   144 DFGFARFVED---YPELSTTFCGSRaYTPPEVILGTPYDPKKyDVWSLGVVLYVMVT-GTMPF 202
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
388-612 6.38e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 76.25  E-value: 6.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcpEQDKILVAVKtlKDASDNARKDFH----REAELLTNLQHEHIVKFYGVC-VEGDP------ 456
Cdd:cd07865    20 IGQGTFGEVFKARH-----RKTGQIVALK--KVLMENEKEGFPitalREIKILQLLKHENVVNLIEICrTKATPynrykg 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 -LIMVFEYMKHgDLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 535
Cdd:cd07865    93 sIYLVFEFCEH-DLAGLLS------------NKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSR----------DVYS----TDYYRvgghtmlpirwmPPESIM-YRKFTTESDVWSLGVVLWEIFTygKQPWYQ 600
Cdd:cd07865   160 LADFGLARafslaknsqpNRYTnrvvTLWYR------------PPELLLgERDYGPPIDMWGAGCIMAEMWT--RSPIMQ 225
                         250
                  ....*....|....
gi 1610576541 601 lSNNEV--IECITQ 612
Cdd:cd07865   226 -GNTEQhqLTLISQ 238
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
388-592 6.99e-15

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 75.54  E-value: 6.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFlaECYNlcPEQDKIlVAVKTLKDASDNA--RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd07846     9 VGEGSYGMVM--KCRH--KETGQI-VAIKKFLESEDDKmvKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAhgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR-- 543
Cdd:cd07846    84 HTVLDDLEKY-------------PNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtl 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 544 ----DVYsTDYyrvgghtmLPIRWM-PPESIMY-RKFTTESDVWSLGVVLWEIFT 592
Cdd:cd07846   151 aapgEVY-TDY--------VATRWYrAPELLVGdTKYGKAVDVWAVGCLVTEMLT 196
pknD PRK13184
serine/threonine-protein kinase PknD;
377-608 9.12e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 78.27  E-value: 9.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVlkRELGEGAFGKVFLAecYN-LCPEQdkilVAVKTL-KDASDNA--RKDFHREAELLTNLQHEHIVKFYGVCV 452
Cdd:PRK13184    1 MQRYDII--RLIGKGGMGEVYLA--YDpVCSRR----VALKKIrEDLSENPllKKRFLREAKIAADLIHPGIVPVYSICS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 453 EGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELtqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 532
Cdd:PRK13184   73 DGDPVYYTMPYIEGYTLKSLLKSVWQKESLSKELAEKTSV--GAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFG------MSRDVYSTDYYRVGG---HTM-LP------IRWMPPESIMYRKFTTESDVWSLGVVLWEIFT---- 592
Cdd:PRK13184  151 EVVILDWGaaifkkLEEEDLLDIDVDERNicySSMtIPgkivgtPDYMAPERLLGVPASESTDIYALGVILYQMLTlsfp 230
                         250
                  ....*....|....*.
gi 1610576541 593 YGKQPWYQLSNNEVIE 608
Cdd:PRK13184  231 YRRKKGRKISYRDVIL 246
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
384-592 9.35e-15

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 74.75  E-value: 9.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAEcyNLcpEQDKiLVAVKTL---KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:cd14663     4 LGRTLGEGTFAKVKFAR--NT--KTGE-SVAIKIIdkeQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd14663    79 MELVTGGELFSKIAKNGR-------------LKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFG 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 541 MSrdvYSTDYYRVGG--HTML--PiRWMPPESIMYRKFT-TESDVWSLGVVLWEIFT 592
Cdd:cd14663   146 LS---ALSEQFRQDGllHTTCgtP-NYVAPEVLARRGYDgAKADIWSCGVILFVLLA 198
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
428-641 1.02e-14

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 75.00  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 428 DFHREAELLTNLQHEHIVKFYGVCVEgdPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNpptELTQSqmlhIAQQIAAG 507
Cdd:cd14067    56 EFRQEASMLHSLQHPCIVYLIGISIH--PLCFALELAPLGSLNTVLEENHKGSSFMPLGH---MLTFK----IAYQIAAG 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 508 MVYLASQHFVHRDLATRNCLV-----GENLLVKIGDFGMSRDVYSTDYYRVGGHTmlpiRWMPPE---SIMYRKfttESD 579
Cdd:cd14067   127 LAYLHKKNIIFCDLKSDNILVwsldvQEHINIKLSDYGISRQSFHEGALGVEGTP----GYQAPEirpRIVYDE---KVD 199
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 580 VWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGrvlQRPRTC-PQEV-----YELMLGCWQREPHMR 641
Cdd:cd14067   200 MFSYGMVLYELLS-GQRPSLGHHQLQIAKKLSKG---IRPVLGqPEEVqffrlQALMMECWDTKPEKR 263
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
378-623 1.24e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 76.98  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 378 KRHNIVLKRELGEGAFGKVFLA-ECYNlcPEQdKILVAVKTLKD--ASDNARKDFHreaeLLTNLQHEHIVKFYGVCVEG 454
Cdd:PTZ00267   65 REHMYVLTTLVGRNPTTAAFVAtRGSD--PKE-KVVAKFVMLNDerQAAYARSELH----CLAACDHFGIVKHFDDFKSD 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKHGDLNKFLRAHgpdavlMAEGNPPTELTQSQMLHiaqQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 534
Cdd:PTZ00267  138 DKLLLIMEYGSGGDLNKQIKQR------LKEHLPFQEYEVGLLFY---QIVLALDEVHSRKMMHRDLKSANIFLMPTGII 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECITQGR 614
Cdd:PTZ00267  209 KLGDFGFSKQYSDSVSLDVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTL-HRPFKGPSQREIMQQVLYGK 287

                  ....*....
gi 1610576541 615 VlqRPRTCP 623
Cdd:PTZ00267  288 Y--DPFPCP 294
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
387-592 1.61e-14

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 74.66  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd07871    12 KLGEGTYATVFKGR-----SKLTENLVALKEIRlEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 hGDLNKFLRAHGPdavLMAEGNppTELTQSQMLHiaqqiaaGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR-- 543
Cdd:cd07871    87 -SDLKQYLDNCGN---LMSMHN--VKIFMFQLLR-------GLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARak 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVYSTDYyrvgGHTMLPIRWMPPESIM-YRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd07871   154 SVPTKTY----SNEVVTLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMAT 199
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
386-590 1.69e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 74.67  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcynlcPEQDKILVAVKTLK---DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd06634    21 REIGHGSFGAVYFAR-----DVRNNEVVAIKKMSysgKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVME 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKhGDLNKFLRAHGpdavlmaegNPPTELTQSQMLHIAQQiaaGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd06634    96 YCL-GSASDLLEVHK---------KPLQEVEIAAITHGALQ---GLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSA 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 543 RDVYSTDYYrVGghtmLPIrWMPPESIMYR---KFTTESDVWSLGVVLWEI 590
Cdd:cd06634   163 SIMAPANSF-VG----TPY-WMAPEVILAMdegQYDGKVDVWSLGITCIEL 207
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
382-655 1.73e-14

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 74.78  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKRELGEGAFGKVFLAECynlcpeQDKIlVAVKTLkdaSDNARKDFHREAELLTN--LQHEHIVKFYGV-------CV 452
Cdd:cd14142     7 ITLVECIGKGRYGEVWRGQW------QGES-VAVKIF---SSRDEKSWFRETEIYNTvlLRHENILGFIASdmtsrnsCT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 453 EgdpLIMVFEYMKHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHF--------VHRDLATR 524
Cdd:cd14142    77 Q---LWLITHYHENGSLYDYLQRT--------------TLDHQEMLRLALSAASGLVHLHTEIFgtqgkpaiAHRDLKSK 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 525 NCLVGENLLVKIGDFGMS-RDVYSTDYYRVGGHTMLPI-RWMPP----ESIMYRKFTT--ESDVWSLGVVLWEIF----- 591
Cdd:cd14142   140 NILVKSNGQCCIADLGLAvTHSQETNQLDVGNNPRVGTkRYMAPevldETINTDCFESykRVDIYAFGLVLWEVArrcvs 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 592 -----TYgKQPWYQLSNNE-------VIECITQgrvlQRPrTCPQE---------VYELMLGCWQREPHMRKNIKGIHTL 650
Cdd:cd14142   220 ggiveEY-KPPFYDVVPSDpsfedmrKVVCVDQ----QRP-NIPNRwssdptltaMAKLMKECWYQNPSARLTALRIKKT 293

                  ....*
gi 1610576541 651 LQNLA 655
Cdd:cd14142   294 LLKIL 298
I-set pfam07679
Immunoglobulin I-set domain;
49-127 2.31e-14

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 68.82  E-value: 2.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  49 NLTVEEGKSITLSCSVAGDPVPNMYWDVGNlvsKHMNETSHTQ-------GSLRITNISSDDSGKqISCVAENLVGEDQD 121
Cdd:pfam07679   9 DVEVQEGESARFTCTVTGTPDPEVSWFKDG---QPLRSSDRFKvtyeggtYTLTISNVQPDDSGK-YTCVATNSAGEAEA 84

                  ....*.
gi 1610576541 122 SVNLTV 127
Cdd:pfam07679  85 SAELTV 90
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
388-590 2.52e-14

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 73.95  E-value: 2.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLCPEQDKIlVAVKTLkdaSDNARKDFHREAELLT--NLQHEHIVKFYGVCVEGDP------LIM 459
Cdd:cd14055     3 VGKGRFAEVWKAKLKQNASGQYET-VAVKIF---PYEEYASWKNEKDIFTdaSLKHENILQFLTAEERGVGldrqywLIT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 vfEYMKHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHF---------VHRDLATRNCLVGE 530
Cdd:cd14055    79 --AYHENGSLQDYLTRH--------------ILSWEDLCKMAGSLARGLAHLHSDRTpcgrpkipiAHRDLKSSNILVKN 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610576541 531 NLLVKIGDFGMSRDV---YSTDYYRVGGHTMLPiRWMPPESIMYRKFTT--ES----DVWSLGVVLWEI 590
Cdd:cd14055   143 DGTCVLADFGLALRLdpsLSVDELANSGQVGTA-RYMAPEALESRVNLEdlESfkqiDVYSMALVLWEM 210
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
386-615 2.55e-14

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 74.01  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAecynlcpeQDKILVAVKTLK--DASDNAR----KDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd05612     7 KTIGTGTFGRVHLV--------RDRISEHYYALKvmAIPEVIRlkqeQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd05612    79 LMEYVPGGELFSYLRNSG-------------RFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDF 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 540 GMSRDVYSTDYYRVGghtmLPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd05612   146 GFAKKLRDRTWTLCG----TP-EYLAPEVIQSKGHNKAVDWWALGILIYEMLV-GYPPFFDDNPFGIYEKILAGKL 215
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
384-613 2.78e-14

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 73.17  E-value: 2.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECynlcpEQDKILVAVKTLKDASDNARKD-FHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14083     7 FKEVLGTGAFSEVVLAED-----KATGKLVAIKCIDKKALKGKEDsLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLnkFLRahgpdavLMAEGNppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV---GENLLVKIGDF 539
Cdd:cd14083    82 LVTGGEL--FDR-------IVEKGS----YTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISDF 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 540 GMSR----DVYSTDYYRVGghtmlpirWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECITQG 613
Cdd:cd14083   149 GLSKmedsGVMSTACGTPG--------YVAPEVLAQKPYGKAVDCWSIGVISY-ILLCGYPPFYDENDSKLFAQILKA 217
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
386-641 4.41e-14

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 73.28  E-value: 4.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNlcpEQdkilVAVKTLKDASDnarKDFHREAELLTN--LQHEHIVKFYGVCVEGD----PLIM 459
Cdd:cd14144     1 RSVGKGRYGEVWKGKWRG---EK----VAVKIFFTTEE---ASWFRETEIYQTvlMRHENILGFIAADIKGTgswtQLYL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHF--------VHRDLATRNCLVGEN 531
Cdd:cd14144    71 ITDYHENGSLYDFLRGN--------------TLDTQSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRDIKSKNILVKKN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 532 LLVKIGDFGMS-RDVYSTDYYRVGGHTMLPI-RWMPPE----SIMYRKFTT--ESDVWSLGVVLWEI----FTYGKQPWY 599
Cdd:cd14144   137 GTCCIADLGLAvKFISETNEVDLPPNTRVGTkRYMAPEvldeSLNRNHFDAykMADMYSFGLVLWEIarrcISGGIVEEY 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 600 QL------SNNEVIECITQGRVLQRPR----------TCPQEVYELMLGCWQREPHMR 641
Cdd:cd14144   217 QLpyydavPSDPSYEDMRRVVCVERRRpsipnrwssdEVLRTMSKLMSECWAHNPAAR 274
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
48-127 4.58e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.92  E-value: 4.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541   48 PNLTVEEGKSITLSCSVAGDPVPNMYW--DVGNLVSKHMNET---SHTQGSLRITNISSDDSGkQISCVAENLVGEDQDS 122
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWykQGGKLLAESGRFSvsrSGSTSTLTISNVTPEDSG-TYTCAATNSSGSASSG 80

                   ....*
gi 1610576541  123 VNLTV 127
Cdd:smart00410  81 TTLTV 85
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
387-598 4.74e-14

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 73.22  E-value: 4.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAECYNLCPEqdkilVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd06655    26 KIGQGASGTVFTAIDVATGQE-----VAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAhgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVY 546
Cdd:cd06655   101 GSLTDVVTE--------------TCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQIT 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 547 STDYYRvggHTMLPI-RWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd06655   167 PEQSKR---STMVGTpYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 215
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
387-599 6.09e-14

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 72.76  E-value: 6.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd06658    29 KIGEGSTGIVCIAT-----EKHTGKQVAVKKMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLrAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVy 546
Cdd:cd06658   104 GALTDIV-TH-------------TRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQV- 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 547 STDYYRVGGHTMLPIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWY 599
Cdd:cd06658   169 SKEVPKRKSLVGTPY-WMAPEVISRLPYGTEVDIWSLGIMVIEMID-GEPPYF 219
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
431-641 6.25e-14

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 72.33  E-value: 6.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 431 REAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLnkflrahgpDAVLMAEGNppteLTQSQMLHIAQQIAAGMVY 510
Cdd:cd14010    43 NEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDL---------ETLLRQDGN----LPESSVRKFGRDLVRGLHY 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 511 LASQHFVHRDLATRNCLVGENLLVKIGDFGMSR---------DVYSTDYYRVGGHTMLPIR-----WMPPESIMYRKFTT 576
Cdd:cd14010   110 IHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARregeilkelFGQFSDEGNVNKVSKKQAKrgtpyYMAPELFQGGVHSF 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 577 ESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECItQGRVLQRPRT-----CPQEVYELMLGCWQREPHMR 641
Cdd:cd14010   190 ASDLWALGCVLYEMFT-GKPPFVAESFTELVEKI-LNEDPPPPPPkvsskPSPDFKSLLKGLLEKDPAKR 257
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
379-610 6.49e-14

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 72.37  E-value: 6.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTL-KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPL 457
Cdd:cd14167     2 RDIYDFREVLGTGAFSEVVLAE-----EKRTQKLVAIKCIaKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLnkFLRahgpdavlMAEGNPPTELTQSQMLhiaQQIAAGMVYLASQHFVHRDLATRNCL---VGENLLV 534
Cdd:cd14167    77 YLIMQLVSGGEL--FDR--------IVEKGFYTERDASKLI---FQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGMSR-----DVYSTDYYRVGghtmlpirWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIEC 609
Cdd:cd14167   144 MISDFGLSKiegsgSVMSTACGTPG--------YVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDAKLFEQ 214

                  .
gi 1610576541 610 I 610
Cdd:cd14167   215 I 215
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
388-631 6.66e-14

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 72.54  E-value: 6.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcYNLcpeqDKILVAVK--TLKDAS-DNARKDFhREAELLTNLQHEHIVKFYGVCVEgDPLIMVFEYM 464
Cdd:cd14049    14 LGKGGYGKVYKVR-NKL----DGQYYAIKkiLIKKVTkRDCMKVL-REVKVLAGLQHPNIVGYHTAWME-HVQLMLYIQM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDL---------NKFLRAHGPDAvlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV-GENLLV 534
Cdd:cd14049    87 QLCELslwdwiverNKRPCEEEFKS------APYTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLhGSDIHV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGM--------SRDVYSTDYYRVGGHT--MLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFtygkQPWYqlSNN 604
Cdd:cd14049   161 RIGDFGLacpdilqdGNDSTTMSRLNGLTHTsgVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF----QPFG--TEM 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1610576541 605 EVIECITQGRVLQRP----RTCPQEVYELML 631
Cdd:cd14049   235 ERAEVLTQLRNGQIPkslcKRWPVQAKYIKL 265
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
388-592 6.74e-14

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 72.80  E-value: 6.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynlcpeQDKI---LVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd07844     8 LGEGSYATVYKG--------RSKLtgqLVALKEIRlEHEEGAPFTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MkHGDLNKFLRAHGPdavLMAEGNppTELTQSQMLHiaqqiaaGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd07844    80 L-DTDLKQYMDDCGG---GLSMHN--VRLFLFQLLR-------GLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLAR 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 ------DVYS----TDYYRvgghtmlpirwmPPESIM-YRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd07844   147 aksvpsKTYSnevvTLWYR------------PPDVLLgSTEYSTSLDMWGVGCIFYEMAT 194
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
388-641 7.47e-14

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 73.12  E-value: 7.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKDFHR---EAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd05595     3 LGKGTFGKVILVR-----EKATGRYYAMKILRKEVIIAKDEVAHtvtESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd05595    78 NGGELFFHLSRE-------------RVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 VYSTdyyrvgGHTMLPI----RWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVlQRPR 620
Cdd:cd05595   145 GITD------GATMKTFcgtpEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHERLFELILMEEI-RFPR 216
                         250       260
                  ....*....|....*....|.
gi 1610576541 621 TCPQEVYELMLGCWQREPHMR 641
Cdd:cd05595   217 TLSPEAKSLLAGLLKKDPKQR 237
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
382-656 8.29e-14

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 72.31  E-value: 8.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKRELGEGAFGKVFLAECYNLcpeqdkilVAVKTLKDASDNAR--KDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd14152     2 IELGELIGQGRWGKVHRGRWHGE--------VAIRLLEIDGNNQDhlKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV--GENLLVKIG 537
Cdd:cd14152    74 ITSFCKGRTLYSFVR------------DPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYdnGKVVITDFG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 538 DFGMSRDVYSTdyyRVGGHTMLPIRW---MPPESImyRK-----------FTTESDVWSLGVVLWEI----FTYGKQPW- 598
Cdd:cd14152   142 LFGISGVVQEG---RRENELKLPHDWlcyLAPEIV--REmtpgkdedclpFSKAADVYAFGTIWYELqardWPLKNQPAe 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 599 ---YQLSNNEVIECITQGRVLQRprtcpqEVYELMLGCWQREPHMRKNIKGIHTLLQNLAK 656
Cdd:cd14152   217 aliWQIGSGEGMKQVLTTISLGK------EVTEILSACWAFDLEERPSFTLLMDMLEKLPK 271
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
383-604 8.36e-14

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 71.94  E-value: 8.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFlaECYNlcpEQDKILVAVKTLKDaSDNARkdfhREAEL--LTNlQHEHIVKFYGV---CVEGDP- 456
Cdd:cd14089     4 ISKQVLGLGINGKVL--ECFH---KKTGEKFALKVLRD-NPKAR----REVELhwRAS-GCPHIVRIIDVyenTYQGRKc 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLRAHGPDAvlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV---GENLL 533
Cdd:cd14089    73 LLVVMECMEGGELFSRIQERADSA-----------FTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYsskGPNAI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 534 VKIGDFGMSRDVYS---------TDYYrvgghtmlpirwMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYqlSNN 604
Cdd:cd14089   142 LKLTDFGFAKETTTkkslqtpcyTPYY------------VAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGYPPFY--SNH 206
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
388-590 8.73e-14

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 72.99  E-value: 8.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflaecynlCPEQDKIL---VAVKTLKDASDNA--RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd07856    18 VGMGAFGLV--------CSARDQLTgqnVAVKKIMKPFSTPvlAKRTYRELKLLKHLRHENIISLSDIFISPLEDIYFVT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHgpdavlmaegnpPTELTQSQmlHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd07856    90 ELLGTDLHRLLTSR------------PLEKQFIQ--YFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 543 R-------DVYSTDYYRVgghtmlpirwmpPEsIM--YRKFTTESDVWSLGVVLWEI 590
Cdd:cd07856   156 RiqdpqmtGYVSTRYYRA------------PE-IMltWQKYDVEVDIWSAGCIFAEM 199
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
386-595 9.05e-14

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 72.89  E-value: 9.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAecynLCPEQDKiLVAVK--TLKDAsdNARKDFHREAELLTNLQHEHIVKFYGVC------------ 451
Cdd:cd07854    11 RPLGCGSNGLVFSA----VDSDCDK-RVAVKkiVLTDP--QSVKHALREIKIIRRLDHDNIVKVYEVLgpsgsdltedvg 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 452 --VEGDPLIMVFEYMKhGDLnkflrahgpdAVLMAEGNPPTEltqsqmlHI---AQQIAAGMVYLASQHFVHRDLATRNC 526
Cdd:cd07854    84 slTELNSVYIVQEYME-TDL----------ANVLEQGPLSEE-------HArlfMYQLLRGLKYIHSANVLHRDLKPANV 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 527 LVG-ENLLVKIGDFGMSRdVYSTDYYRVGGHTM-LPIRWM-PPESIMY-RKFTTESDVWSLGVVLWEIFTyGK 595
Cdd:cd07854   146 FINtEDLVLKIGDFGLAR-IVDPHYSHKGYLSEgLVTKWYrSPRLLLSpNNYTKAIDMWAAGCIFAEMLT-GK 216
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
380-610 9.37e-14

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 71.87  E-value: 9.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 380 HNIVLKRELGEGAFGKVflaecyNLCPEQDKIL-VAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLI 458
Cdd:cd14193     4 YNVNKEEILGGGRFGQV------HKCEEKSSGLkLAAKIIKARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLnkFLRahgpdavLMAEGNPPTELTQSQMLhiaQQIAAGMVYLASQHFVHRDLATRN--CLVGENLLVKI 536
Cdd:cd14193    78 LVMEYVDGGEL--FDR-------IIDENYNLTELDTILFI---KQICEGIQYMHQMYILHLDLKPENilCVSREANQVKI 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 537 GDFGMSRDVYSTDYYRVGGHTmlPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECI 610
Cdd:cd14193   146 IDFGLARRYKPREKLRVNFGT--P-EFLAPEVVNYEFVSFPTDMWSLGVIAYMLLS-GLSPFLGEDDNETLNNI 215
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
388-641 9.56e-14

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 72.63  E-value: 9.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKdasdnarKDFHREAE-----------LLTNLQHEHIVKFYGVCVEGDP 456
Cdd:cd05570     3 LGKGSFGKVMLAE-----RKKTDELYAIKVLK-------KEVIIEDDdvectmtekrvLALANRHPFLTGLHACFQTEDR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLnkflrahgpdavlmaegnppteltqsqMLHIAQQ--------------IAAGMVYLASQHFVHRDLA 522
Cdd:cd05570    71 LYFVMEYVNGGDL---------------------------MFHIQRArrfteerarfyaaeICLALQFLHERGIIYRDLK 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 523 TRNCLVGENLLVKIGDFGMSR------DVYST-----DYyrvgghtmlpirwMPPESIMYRKFTTESDVWSLGVVLWEIF 591
Cdd:cd05570   124 LDNVLLDAEGHIKIADFGMCKegiwggNTTSTfcgtpDY-------------IAPEILREQDYGFSVDWWALGVLLYEML 190
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1610576541 592 TyGKQPWYQLSNNEVIECITQGRVLQrPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05570   191 A-GQSPFEGDDEDELFEAILNDEVLY-PRWLSREAVSILKGLLTKDPARR 238
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
432-595 9.79e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 72.99  E-value: 9.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 432 EAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKhGDLNKFLRahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYL 511
Cdd:PHA03209  107 EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYS-SDLYTYLT------------KRSRPLPIDQALIIEKQILEGLRYL 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 512 ASQHFVHRDLATRNCLVGENLLVKIGDFGMSR-DVYSTDYYRVGGhtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEI 590
Cdd:PHA03209  174 HAQRIIHRDVKTENIFINDVDQVCIGDLGAAQfPVVAPAFLGLAG----TVETNAPEVLARDKYNSKADIWSAGIVLFEM 249

                  ....*
gi 1610576541 591 FTYGK 595
Cdd:PHA03209  250 LAYPS 254
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
386-649 1.10e-13

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 71.65  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcYNlcpeQDKILVAVKTLKDA---SDNARKD-----FHREAELLTNLQ---HEHIVKfygvcveg 454
Cdd:cd14004     6 KEMGEGAYGQVNLAI-YK----SKGKEVVIKFIFKErilVDTWVRDrklgtVPLEIHILDTLNkrsHPNIVK-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 dpLIMVFEymkhGDLNKFL--RAHGPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 532
Cdd:cd14004    73 --LLDFFE----DDEFYYLvmEKHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFGMSRDVYSTDYYRVGGhtmlPIRWMPPESIMYRKFT-TESDVWSLGVVLWEIFtYGKQPWYQLsnNEVIEcit 611
Cdd:cd14004   147 TIKLIDFGSAAYIKSGPFDTFVG----TIDYAAPEVLRGNPYGgKEQDIWALGVLLYTLV-FKENPFYNI--EEILE--- 216
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1610576541 612 qgRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHT 649
Cdd:cd14004   217 --ADLRIPYAVSEDLIDLISRMLNRDVGDRPTIEELLT 252
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
384-600 1.19e-13

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 72.44  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECYNLCPEqdkILVAVKTLKDASDNA--RKDFHREAELLTNLQ-HEHIVKFYGV-CVEGDPLIM 459
Cdd:cd07857     4 LIKELGQGAYGIVCSARNAETSEE---ETVAIKKITNVFSKKilAKRALRELKLLRHFRgHKNITCLYDMdIVFPGNFNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMK--HGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd07857    81 LYLYEElmEADLHQIIRSGQP-------------LTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKIC 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 538 DFGMSRDvYSTDYYRVGGHTM--LPIRWMPPESIM--YRKFTTESDVWSLGVVLWEIftYGKQPWYQ 600
Cdd:cd07857   148 DFGLARG-FSENPGENAGFMTeyVATRWYRAPEIMlsFQSYTKAIDVWSVGCILAEL--LGRKPVFK 211
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
387-599 1.22e-13

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 71.98  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAECynlcpEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd06657    27 KIGEGSTGIVCIATV-----KSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAhgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVy 546
Cdd:cd06657   102 GALTDIVTH--------------TRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV- 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 547 STDYYRVGGHTMLPIrWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWY 599
Cdd:cd06657   167 SKEVPRRKSLVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPYF 217
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
388-592 1.29e-13

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 71.63  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFlaECYNLCPEQdkiLVAVKTLKDASD--NARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd07847     9 IGEGSYGVVF--KCRNRETGQ---IVAIKKFVESEDdpVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKfLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR-- 543
Cdd:cd07847    84 HTVLNE-LEKN------------PRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARil 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 544 ---DVYSTDYyrvgghtmLPIRWmppesimYR---------KFTTESDVWSLGVVLWEIFT 592
Cdd:cd07847   151 tgpGDDYTDY--------VATRW-------YRapellvgdtQYGPPVDVWAIGCVFAELLT 196
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
384-647 1.36e-13

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 71.29  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAEcYNLCPEQdkilVAVKTL-KDASDNARKD-FHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd14074     7 LEETLGRGHFAVVKLAR-HVFTGEK----VAVKVIdKTKLDDVSKAhLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLIL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAHGpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL-LVKIGDFG 540
Cdd:cd14074    82 ELGDGGDMYDYIMKHE------------NGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDvystdyYRVGghTML-----PIRWMPPESIMYRKFTTES-DVWSLGVVLWeIFTYGKQPWYQLSNNEVIECITQGR 614
Cdd:cd14074   150 FSNK------FQPG--EKLetscgSLAYSAPEILLGDEYDAPAvDIWSLGVILY-MLVCGQPPFQEANDSETLTMIMDCK 220
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1610576541 615 VLQRPRTCPqEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14074   221 YTVPAHVSP-ECKDLIRRMLIRDPKKRASLEEI 252
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
388-590 1.41e-13

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 71.95  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflaecYNLCPEQDKILVAVKTLKDASDnARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPLI-----MVF 461
Cdd:cd06639    30 IGKGTYGKV-----YKVTNKKDGSLAAVKILDPISD-VDEEIEAEYNILRSLpNHPNVVKFYGMFYKADQYVggqlwLVL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAhgpdavLMAEGNPPTELTQSQMLHIAqqiAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd06639   104 ELCNGGSVTELVKG------LLKCGQRLDEAMISYILYGA---LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGV 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 542 SRDVYSTDYYR---VGghtmLPIrWMPPESIMYRK-----FTTESDVWSLGVVLWEI 590
Cdd:cd06639   175 SAQLTSARLRRntsVG----TPF-WMAPEVIACEQqydysYDARCDVWSLGITAIEL 226
PHA02988 PHA02988
hypothetical protein; Provisional
412-647 1.44e-13

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 71.70  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 412 LVAVKTLKDASDNARK---DFHREAELLTNLQHEHIVKFYGVCVE-GDPL---IMVFEYMKHGDLNKFLRAHgpdavlma 484
Cdd:PHA02988   45 EVIIRTFKKFHKGHKVlidITENEIKNLRRIDSNNILKIYGFIIDiVDDLprlSLILEYCTRGYLREVLDKE-------- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 485 egnppTELTQSQMLHIAQQIAAGMVYL-ASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRW 563
Cdd:PHA02988  117 -----KDLSFKTKLDMAIDCCKGLYNLyKYTNKPYKNLTSVSFLVTENYKLKIICHGLEKILSSPPFKNVNFMVYFSYKM 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 564 MppeSIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRV-LQRPRTCPQEVYELMLGCWQREPHMRK 642
Cdd:PHA02988  192 L---NDIFSEYTIKDDIYSLGVVLWEIFT-GKIPFENLTTKEIYDLIINKNNsLKLPLDCPLEIKCIVEACTSHDSIKRP 267

                  ....*
gi 1610576541 643 NIKGI 647
Cdd:PHA02988  268 NIKEI 272
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
387-590 1.66e-13

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 71.99  E-value: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLK---DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd06633    28 EIGHGSFGAVYFAT-----NSHTNEVVAIKKMSysgKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEY 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKhGDLNKFLRAHGpdavlmaegNPPTELTQSQMLHIAQQiaaGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGmSR 543
Cdd:cd06633   103 CL-GSASDLLEVHK---------KPLQEVEIAAITHGALQ---GLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG-SA 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVYSTDYYRVGghtmLPIrWMPPESIMYR---KFTTESDVWSLGVVLWEI 590
Cdd:cd06633   169 SIASPANSFVG----TPY-WMAPEVILAMdegQYDGKVDIWSLGITCIEL 213
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
384-654 1.89e-13

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 70.98  E-value: 1.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECY---NLCpeqdkilvAVKTLKDASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGD---- 455
Cdd:cd13975     4 LGRELGRGQYGVVYACDSWgghFPC--------ALKSVVPPDDKHWNDLALEFHYTRSLpKHERIVSLHGSVIDYSyggg 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 ---PLIMVFEYMkHGDLNKFLRAHgpdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 532
Cdd:cd13975    76 ssiAVLLIMERL-HRDLYTGIKAG---------------LSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKN 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFG-------MSRDVYSTdyyrvgghtmlPIRwMPPEsIMYRKFTTESDVWSLGVVLWEIFTyGK----QPWYQL 601
Cdd:cd13975   140 RAKITDLGfckpeamMSGSIVGT-----------PIH-MAPE-LFSGKYDNSVDVYAFGILFWYLCA-GHvklpEAFEQC 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 602 SNNEVI-ECITQGRvlqRPRTCPQ---EVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd13975   206 ASKDHLwNNVRKGV---RPERLPVfdeECWNLMEACWSGDPSQRPLLGIVQPKLQGI 259
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
388-646 2.08e-13

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 71.51  E-value: 2.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcpEQDKILVAVKTLKD----ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd05620     3 LGKGSFGKVLLAEL-----KGKGEYFAVKALKKdvvlIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGPDAVLMAEgnppteltqsqmlHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd05620    78 LNGGDLMFHIQDKGRFDLYRAT-------------FYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 D-VYSTDyyRVGGHTMLPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGrVLQRPRTC 622
Cdd:cd05620   145 EnVFGDN--RASTFCGTP-DYIAPEILQGLKYTFSVDWWSFGVLLYEMLI-GQSPFHGDDEDELFESIRVD-TPHYPRWI 219
                         250       260
                  ....*....|....*....|....
gi 1610576541 623 PQEVYELMLGCWQREPHMRKNIKG 646
Cdd:cd05620   220 TKESKDILEKLFERDPTRRLGVVG 243
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
380-592 2.09e-13

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 71.95  E-value: 2.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 380 HNIVLKRELGEGAFGKVFLAecYNlCPEQDKilVAVK-------------TLkdasdnarkdfhREAELLTNLQHEHIVK 446
Cdd:cd07849     5 PRYQNLSYIGEGAYGMVCSA--VH-KPTGQK--VAIKkispfehqtyclrTL------------REIKILLRFKHENIIG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 447 FYGVCVEGD-----PLIMVFEYMKhGDLNKFLRahgpdavlmaegnppteltqSQML---HIAQ---QIAAGMVYLASQH 515
Cdd:cd07849    68 ILDIQRPPTfesfkDVYIVQELME-TDLYKLIK--------------------TQHLsndHIQYflyQILRGLKYIHSAN 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 516 FVHRDLATRNCLVGENLLVKIGDFGMSR-DVYSTDYYrvGGHT-MLPIRWMPPESIM--YRKFTTESDVWSLGVVLWEIF 591
Cdd:cd07849   127 VLHRDLKPSNLLLNTNCDLKICDFGLARiADPEHDHT--GFLTeYVATRWYRAPEIMlnSKGYTKAIDIWSVGCILAEML 204

                  .
gi 1610576541 592 T 592
Cdd:cd07849   205 S 205
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
387-598 2.31e-13

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 71.03  E-value: 2.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVflaecYNLCPEQDKILVAVKTLKDASDNAR-KDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd06622     8 ELGKGNYGSV-----YKVLHRPTGVTMAMKEIRLELDESKfNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKflrahgpdavLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQH-FVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd06622    83 AGSLDK----------LYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEHnIIHRDVKPTNVLVNGNGQVKLCDFGVSGN 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 545 -VYSTDYYRVGGHTmlpirWMPPESIMYR------KFTTESDVWSLGVVLWEIfTYGKQPW 598
Cdd:cd06622   153 lVASLAKTNIGCQS-----YMAPERIKSGgpnqnpTYTVQSDVWSLGLSILEM-ALGRYPY 207
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
386-592 2.47e-13

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 71.56  E-value: 2.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNLcpeqdKILVAVKTLKDASDNAR--KDFHREAELLTNLQHEHIVKFYGVCVEGDPL------ 457
Cdd:cd07851    21 SPVGSGAYGQVCSAFDTKT-----GRKVAIKKLSRPFQSAIhaKRTYRELRLLKHMKHENVIGLLDVFTPASSLedfqdv 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKhGDLNKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd07851    96 YLVTHLMG-ADLNNIVKCQ--------------KLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKIL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 538 DFGMSR--DVYSTDYyrVGghtmlpIRW-MPPEsIMY--RKFTTESDVWSLGVVLWEIFT 592
Cdd:cd07851   161 DFGLARhtDDEMTGY--VA------TRWyRAPE-IMLnwMHYNQTVDIWSVGCIMAELLT 211
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
387-611 2.52e-13

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 70.82  E-value: 2.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVflAECYNLCPEQDKILVAVKTLKDASDN---ARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd14194    12 ELGSGQFAVV--KKCREKSTGLQYAAKFIKKRRTKSSRrgvSREDIEREVSILKEIQHPNVITLHEVYENKTDVILILEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLrahgpdavlmAEGNPPTELTQSQMLhiaQQIAAGMVYLASQHFVHRDLATRNC-LVGENL---LVKIGDF 539
Cdd:cd14194    90 VAGGELFDFL----------AEKESLTEEEATEFL---KQILNGVYYLHSLQIAHFDLKPENImLLDRNVpkpRIKIIDF 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 540 GMSRDV-YSTDYYRVGGHTmlpiRWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECIT 611
Cdd:cd14194   157 GLAHKIdFGNEFKNIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANVS 224
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
387-598 2.67e-13

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 70.34  E-value: 2.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAecYNLCPEQDkilVAVKTLkDASDNARKDFH-REAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd06647    14 KIGQGASGTVYTA--IDVATGQE---VAIKQM-NLQQQPKKELIiNEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNkflrahgpDAVlmaegnPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDV 545
Cdd:cd06647    88 GGSLT--------DVV------TETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQI 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 546 YSTDYYRVgghTMLPI-RWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd06647   154 TPEQSKRS---TMVGTpYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 203
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
388-590 2.79e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 70.80  E-value: 2.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFlaECYNlcpEQDKILVAVKTLKDASDN--ARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd07848     9 VGEGAYGVVL--KCRH---KETKEIVAIKKFKDSEENeeVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLnKFLRAHgpdavlmAEGNPPTELTQsqmlHIAQQIAAgMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR-- 543
Cdd:cd07848    84 KNML-ELLEEM-------PNGVPPEKVRS----YIYQLIKA-IHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARnl 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 544 ----DVYSTDYyrvgghtmLPIRWM-PPESIMYRKFTTESDVWSLGVVLWEI 590
Cdd:cd07848   151 segsNANYTEY--------VATRWYrSPELLLGAPYGKAVDMWSVGCILGEL 194
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
388-615 2.90e-13

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 71.28  E-value: 2.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcYNLCPEQDKILvAVKTLKDAS--DNARKDFHREAE--LLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd05584     4 LGKGGYGKVFQVR-KTTGSDKGKIF-AMKVLKKASivRNQKDTAHTKAErnILEAVKHPFIVDLHYAFQTGGKLYLILEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGpdaVLMaegnpptELTQSQMLhiaQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd05584    82 LSGGELFMHLEREG---IFM-------EDTACFYL---AEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCK 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 544 DVYSTDYYRvggHTML-PIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd05584   149 ESIHDGTVT---HTFCgTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLT-GAPPFTAENRKKTIDKILKGKL 217
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
381-615 3.52e-13

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 70.51  E-value: 3.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLA------ECYNLcpeqdKILVAVKTLKDASdnaRKDFHREAELLTNLQHEHIVKFYGVCVEG 454
Cdd:cd14209     2 DFDRIKTLGTGSFGRVMLVrhketgNYYAM-----KILDKQKVVKLKQ---VEHTLNEKRILQAINFPFLVKLEYSFKDN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 534
Cdd:cd14209    74 SNLYMVMEYVPGGEMFSHLRRIG-------------RFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYI 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGMSRdvystdyyRVGGHTM----LPiRWMPPESIMYRKFTTESDVWSLGVVLWEiFTYGKQPWYQLSNNEVIECI 610
Cdd:cd14209   141 KVTDFGFAK--------RVKGRTWtlcgTP-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPFFADQPIQIYEKI 210

                  ....*
gi 1610576541 611 TQGRV 615
Cdd:cd14209   211 VSGKV 215
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
388-641 3.79e-13

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 70.88  E-value: 3.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECynlcpEQDKILVAVKTLKdasdnarKDFHREAE-----------LLTNLQHEHIVKFYGVCVEGDP 456
Cdd:cd05592     3 LGKGSFGKVMLAEL-----KGTNQYFAIKALK-------KDVVLEDDdvectmierrvLALASQHPFLTHLFCTFQTESH 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLnkflrahgpdavlmaegnppteltqsqMLHIAQQ--------------IAAGMVYLASQHFVHRDLA 522
Cdd:cd05592    71 LFFVMEYLNGGDL---------------------------MFHIQQSgrfdedrarfygaeIICGLQFLHSRGIIYRDLK 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 523 TRNCLVGENLLVKIGDFGMSR-DVY-----ST-----DYyrvgghtmlpirwMPPESIMYRKFTTESDVWSLGVVLWEIF 591
Cdd:cd05592   124 LDNVLLDREGHIKIADFGMCKeNIYgenkaSTfcgtpDY-------------IAPEILKGQKYNQSVDWWSFGVLLYEML 190
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1610576541 592 TyGKQPWYQLSNNEVIECITQGRVlQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05592   191 I-GQSPFHGEDEDELFWSICNDTP-HYPRWLTKEAASCLSLLLERNPEKR 238
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
388-603 3.88e-13

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 70.14  E-value: 3.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLCPEQdkilVAVKTLKD--ASDNARKDFHREAELLTNLQ---HEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14052     8 IGSGEFSQVYKVSERVPTGKV----YAVKKLKPnyAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQTE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHGPDAVLmaegnpptelTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd14052    84 LCENGSLDVFLSELGLLGRL----------DEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 543 rdvystdyyrvgghTMLPI----------RWMPPESIMYRKFTTESDVWSLGVVLWEIFTY-----GKQPWYQLSN 603
Cdd:cd14052   154 --------------TVWPLirgieregdrEYIAPEILSEHMYDKPADIFSLGLILLEAAANvvlpdNGDAWQKLRS 215
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
388-590 4.13e-13

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 70.42  E-value: 4.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYnlcpeQDKILVAVKTLkDASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDP------LIMV 460
Cdd:cd06636    24 VGNGTYGQVYKGRHV-----KTGQLAAIKVM-DVTEDEEEEIKLEINMLKKYsHHRNIATYYGAFIKKSPpghddqLWLV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNkflrahgpDAVLMAEGNpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd06636    98 MEFCGAGSVT--------DLVKNTKGN---ALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFG 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 541 MSRDVYSTDYYRvggHTMLPI-RWMPPESIMYRK-----FTTESDVWSLGVVLWEI 590
Cdd:cd06636   167 VSAQLDRTVGRR---NTFIGTpYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEM 219
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
384-614 4.14e-13

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 70.27  E-value: 4.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFlaECYNLCPEQDKI--LVAVKTlkdasdnARKDF-HREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:cd14104     4 IAEELGRGQFGIVH--RCVETSSKKTYMakFVKVKG-------ADQVLvKKEISILNIARHRNILRLHESFESHEELVMI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRN--CLVGENLLVKIGD 538
Cdd:cd14104    75 FEFISGVDIFERITTAR------------FELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENiiYCTRRGSYIKIIE 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 539 FGMSRDVYSTDYYRVgghTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECITQGR 614
Cdd:cd14104   143 FGQSRQLKPGDKFRL---QYTSAEFYAPEVHQHESVSTATDMWSLGCLVY-VLLSGINPFEAETNQQTIENIRNAE 214
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
369-641 4.26e-13

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 71.00  E-value: 4.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 369 KPDTfvQHIKRHNIVLKRELGEGAFGKVFLaeCYNLCPEQdkiLVAVKTLKDASDNARKDFH---REAELLTNLQHEHIV 445
Cdd:PTZ00263    9 KPDT--SSWKLSDFEMGETLGTGSFGRVRI--AKHKGTGE---YYAIKCLKKREILKMKQVQhvaQEKSILMELSHPFIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 446 KFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHG--PDAVlmaegnppteltqSQMLHiAQQIAAgMVYLASQHFVHRDLAT 523
Cdd:PTZ00263   82 NMMCSFQDENRVYFLLEFVVGGELFTHLRKAGrfPNDV-------------AKFYH-AELVLA-FEYLHSKDIIYRDLKP 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 524 RNCLVGENLLVKIGDFGMSRDVYSTDYYRVGghtmLPiRWMPPESIMYRKFTTESDVWSLGVVLWEiFTYGKQPWYQLSN 603
Cdd:PTZ00263  147 ENLLLDNKGHVKVTDFGFAKKVPDRTFTLCG----TP-EYLAPEVIQSKGHGKAVDWWTMGVLLYE-FIAGYPPFFDDTP 220
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1610576541 604 NEVIECITQGRvLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:PTZ00263  221 FRIYEKILAGR-LKFPNWFDGRARDLVKGLLQTDHTKR 257
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
384-590 4.34e-13

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 70.07  E-value: 4.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECYNLCPeqdkiLVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd06645    15 LIQRIGSGTYGDVYKARNVNTGE-----LAAIKVIKLEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd06645    90 CGGGSLQDIYHVTGP-------------LSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSA 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DVYSTDYYRvGGHTMLPIrWMPPE-SIMYRK--FTTESDVWSLGVVLWEI 590
Cdd:cd06645   157 QITATIAKR-KSFIGTPY-WMAPEvAAVERKggYNQLCDIWAVGITAIEL 204
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
388-665 4.40e-13

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 70.86  E-value: 4.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflaeCYNLCPEQDKiLVAVKTLKDASDN---ARKDFhREAELLTNLQHEHIVKFYGVCV-----EGDPLIM 459
Cdd:cd07858    13 IGRGAYGIV----CSAKNSETNE-KVAIKKIANAFDNridAKRTL-REIKLLRHLDHENVIAIKDIMPpphreAFNDVYI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKhGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd07858    87 VYELMD-TDLHQIIRSSQT-------------LSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMSR-----DVYSTDYYRVgghtmlpiRW--MPPESIMYRKFTTESDVWSLGVVLWEIFtyGKQPWYQLSnneviECITQ 612
Cdd:cd07858   153 GLARttsekGDFMTEYVVT--------RWyrAPELLLNCSEYTTAIDVWSVGCIFAELL--GRKPLFPGK-----DYVHQ 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 613 GRVLQRPRTCPQEVyELmlgCWQREPHMRKNIKGI-HTLLQNLA----KASPVYLDIL 665
Cdd:cd07858   218 LKLITELLGSPSEE-DL---GFIRNEKARRYIRSLpYTPRQSFArlfpHANPLAIDLL 271
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
387-599 4.43e-13

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 70.25  E-value: 4.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAecynlcpeQDKI---LVAVKTLKDASDN--ARKDFHREAELLTNLQHE-HIVKFygVCVE-----GD 455
Cdd:cd07837     8 KIGEGTYGKVYKA--------RDKNtgkLVALKKTRLEMEEegVPSTALREVSLLQMLSQSiYIVRL--LDVEhveenGK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 P-LIMVFEYMKHgDLNKFLRAHGpdavlMAEGNP-PTELTQSQMLhiaqQIAAGMVYLASQHFVHRDLATRNCLVG-ENL 532
Cdd:cd07837    78 PlLYLVFEYLDT-DLKKFIDSYG-----RGPHNPlPAKTIQSFMY----QLCKGVAHCHSHGVMHRDLKPQNLLVDkQKG 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 533 LVKIGDFGMSRDVysTDYYRVGGHTMLPIRWMPPESIM-YRKFTTESDVWSLGVVLWEIFTygKQPWY 599
Cdd:cd07837   148 LLKIADLGLGRAF--TIPIKSYTHEIVTLWYRAPEVLLgSTHYSTPVDMWSVGCIFAEMSR--KQPLF 211
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
390-598 4.72e-13

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 69.65  E-value: 4.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 390 EGAFGKVFLAECYNLCPEQDKILVAVKTLKDAsdnarkdfhrEAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDL 469
Cdd:cd13995    14 RGAFGKVYLAQDTKTKKRMACKLIPVEQFKPS----------DVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 470 NKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIgDFG----MSRDV 545
Cdd:cd13995    84 LEKLESCGP-------------MREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGlsvqMTEDV 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 546 YSTDYYRvgGHTMlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd13995   150 YVPKDLR--GTEI----YMSPEVILCRGHNTKADIYSLGATIIHMQT-GSPPW 195
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
436-656 5.26e-13

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 69.74  E-value: 5.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 436 LTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELTQsqmlhiaqqiaaGMVYLASQH 515
Cdd:cd14043    50 LRELRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRNDDMKLDWMFKSSLLLDLIK------------GMRYLHHRG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 516 FVHRDLATRNCLVGENLLVKIGDFGmsrdvystdYYRVGGHTMLPIR--------WMPPESI----MYRKFTTESDVWSL 583
Cdd:cd14043   118 IVHGRLKSRNCVVDGRFVLKITDYG---------YNEILEAQNLPLPepapeellWTAPELLrdprLERRGTFPGDVFSF 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610576541 584 GVVLWEIFTYGkQPW--YQLSNNEVIECITQGRVLQRPRT----CPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAK 656
Cdd:cd14043   189 AIIMQEVIVRG-APYcmLGLSPEEIIEKVRSPPPLCRPSVsmdqAPLECIQLMKQCWSEAPERRPTFDQIFDQFKSINK 266
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
388-641 5.64e-13

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 70.80  E-value: 5.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKD---ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEG-DPLIMVFEY 463
Cdd:cd05615    18 LGKGSFGKVMLAE-----RKGSDELYAIKILKKdvvIQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTvDRLYFVMEY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd05615    93 VNGGDLMYHIQQVG-------------KFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 DvystdyYRVGGHTMLPIRWMP----PESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVlQRP 619
Cdd:cd05615   160 E------HMVEGVTTRTFCGTPdyiaPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQSIMEHNV-SYP 231
                         250       260
                  ....*....|....*....|..
gi 1610576541 620 RTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05615   232 KSLSKEAVSICKGLMTKHPAKR 253
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
388-603 5.83e-13

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 69.45  E-value: 5.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflaecYNLCPEQD-KILVAVKTLKDASDNARKDFHREAELLTN-----------LQHEHIVKFYGVCVEGD 455
Cdd:cd08528     8 LGSGAFGCV-----YKVRKKSNgQTLLALKEINMTNPAFGRTEQERDKSVGDiisevniikeqLRHPNIVRYYKTFLEND 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNKFLRAhgpdavlMAEGNppTELTQSQMLHIAQQIAAGMVYL-ASQHFVHRDLATRNCLVGENLLV 534
Cdd:cd08528    83 RLYIVMELIEGAPLGEHFSS-------LKEKN--EHFTEDRIWNIFVQMVLALRYLhKEKQIVHRDLKPNNIMLGEDDKV 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 535 KIGDFGMSRDVYSTDYYR---VGghtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgkQPWYQLSN 603
Cdd:cd08528   154 TITDFGLAKQKGPESSKMtsvVG-----TILYSCPEIVQNEPYGEKADIWALGCILYQMCTL--QPPFYSTN 218
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
386-612 6.78e-13

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 70.08  E-value: 6.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcynlcPEQDKILVAVKTLK---DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd06635    31 REIGHGSFGAVYFAR-----DVRTSEVVAIKKMSysgKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVME 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKhGDLNKFLRAHGpdavlmaegNPPTELTQSQMLHIAQQiaaGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd06635   106 YCL-GSASDLLEVHK---------KPLQEIEIAAITHGALQ---GLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSA 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 543 RDVYSTDYYrVGghtmLPIrWMPPESIMYR---KFTTESDVWSLGVVLWEIfTYGKQPWYQLSNNEVIECITQ 612
Cdd:cd06635   173 SIASPANSF-VG----TPY-WMAPEVILAMdegQYDGKVDVWSLGITCIEL-AERKPPLFNMNAMSALYHIAQ 238
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
388-641 7.04e-13

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 70.03  E-value: 7.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKD----ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd05616     8 LGKGSFGKVMLAE-----RKGTDELYAVKILKKdvviQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd05616    83 VNGGDLMYHIQQVG-------------RFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 ----DVYSTDYYrvgghTMLPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVlQRP 619
Cdd:cd05616   150 eniwDGVTTKTF-----CGTP-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLA-GQAPFEGEDEDELFQSIMEHNV-AYP 221
                         250       260
                  ....*....|....*....|..
gi 1610576541 620 RTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05616   222 KSMSKEAVAICKGLMTKHPGKR 243
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
388-653 7.26e-13

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 69.65  E-value: 7.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFlaecyNLCPEQDKILVAVKTLkDASDNARKDFHREAELLTNLQ-HEHIVKFYGV-----CVEGDPLIMVF 461
Cdd:cd06638    26 IGKGTYGKVF-----KVLNKKNGSKAAVKIL-DPIHDIDEEIEAEYNILKALSdHPNVVKFYGMyykkdVKNGDQLWLVL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAhgpdavLMAEGNPPTELTQSQMLHIAqqiAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd06638   100 ELCNGGSVTDLVKG------FLKRGERMEEPIIAYILHEA---LMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SRDVYSTDYYR---VGghtmLPIrWMPPESIMYRK-----FTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQG 613
Cdd:cd06638   171 SAQLTSTRLRRntsVG----TPF-WMAPEVIACEQqldstYDARCDVWSLGITAIELGD-GDPPLADLHPMRALFKIPRN 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1610576541 614 --RVLQRPRTCPQEVYELMLGCWQREPHMRKNIKgihTLLQN 653
Cdd:cd06638   245 ppPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVS---DLLQH 283
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
383-598 7.73e-13

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 69.05  E-value: 7.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFL----AECYNLCPEQDKI-LVAVKTLKDASDNARkdFHREAELLTNLQHEHIVKFYGVCVEGDPL 457
Cdd:cd14076     4 ILGRTLGEGEFGKVKLgwplPKANHRSGVQVAIkLIRRDTQQENCQTSK--IMREINILKGLTHPNIVRLLDVLKTKKYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd14076    82 GIVLEFVSGGELFDYILAR-------------RRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVIT 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 538 DFGmsrdvYSTDYYRVGGHTMLPIRWMP----PESIMYRKF--TTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd14076   149 DFG-----FANTFDHFNGDLMSTSCGSPcyaaPELVVSDSMyaGRKADIWSCGVILYAMLA-GYLPF 209
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
379-613 7.97e-13

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 69.25  E-value: 7.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLI 458
Cdd:cd14166     2 RETFIFMEVLGSGAFSEVYLVK-----QRSTGKLYALKCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLnkFlrahgpDAVLmaEGNPPTELTQSQMLHiaqQIAAGMVYLASQHFVHRDLATRNCLV---GENLLVK 535
Cdd:cd14166    77 LVMQLVSGGEL--F------DRIL--ERGVYTEKDASRVIN---QVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIM 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 536 IGDFGMSR----DVYSTDYYRVGghtmlpirWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECIT 611
Cdd:cd14166   144 ITDFGLSKmeqnGIMSTACGTPG--------YVAPEVLAQKPYSKAVDCWSIGVITY-ILLCGYPPFYEETESRLFEKIK 214

                  ..
gi 1610576541 612 QG 613
Cdd:cd14166   215 EG 216
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
384-542 8.55e-13

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 68.90  E-value: 8.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAecyNLCPEQDKilVAVKTL-KDASDN-ARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd14075     6 IRGELGSGNFSQVKLG---IHQLTKEK--VAIKILdKTKLDQkTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd14075    81 EYASGGELYTKISTEGK-------------LSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGF 147

                  .
gi 1610576541 542 S 542
Cdd:cd14075   148 S 148
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
428-645 9.35e-13

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 69.49  E-value: 9.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 428 DFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDL--NKFLRAhgpdavlmAEGNPPTELTQSqmlHIAQQIA 505
Cdd:cd14094    51 DLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLcfEIVKRA--------DAGFVYSEAVAS---HYMRQIL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 506 AGMVYLASQHFVHRDLATRNCLVG--ENLL-VKIGDFGMSRDVYSTDYYrVGGHTMLPiRWMPPESIMYRKFTTESDVWS 582
Cdd:cd14094   120 EALRYCHDNNIIHRDVKPHCVLLAskENSApVKLGGFGVAIQLGESGLV-AGGRVGTP-HFMAPEVVKREPYGKPVDVWG 197
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 583 LGVVLWeIFTYGKQPWYQlSNNEVIECITQGRVLQRPRTCPQ---EVYELMLGCWQREPHMRKNIK 645
Cdd:cd14094   198 CGVILF-ILLSGCLPFYG-TKERLFEGIIKGKYKMNPRQWSHiseSAKDLVRRMLMLDPAERITVY 261
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
388-592 1.04e-12

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 69.50  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLaeCYNlcpEQDKILVAVKTLKDasdnaRKDFHR----EAELLTNLQH------EHIVKFYGVCVEGDPL 457
Cdd:cd14210    21 LGKGSFGQVVK--CLD---HKTGQLVAIKIIRN-----KKRFHQqalvEVKILKHLNDndpddkHNIVRYKDSFIFRGHL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEyMKHGDLNKFLRA---HGpdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATrnclvgENLL- 533
Cdd:cd14210    91 CIVFE-LLSINLYELLKSnnfQG--------------LSLSLIRKFAKQILQALQFLHKLNIIHCDLKP------ENILl 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 534 -------VKIGDFGMS----RDVYS---TDYYRVgghtmlpirwmpPESIMYRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd14210   150 kqpskssIKVIDFGSScfegEKVYTyiqSRFYRA------------PEVILGLPYDTAIDMWSLGCILAELYT 210
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
382-615 1.13e-12

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 68.80  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKRELGEGAFGKVflAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd14198    10 ILTSKELGRGKFAVV--RQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSNPRVVNLHEVYETTSEIILIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRahgPDAVLMaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGE-NLL--VKIGD 538
Cdd:cd14198    88 EYAAGGEIFNLCV---PDLAEM--------VSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiYPLgdIKIVD 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 539 FGMSRDVYSTDYYRvggHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRV 615
Cdd:cd14198   157 FGMSRKIGHACELR---EIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLT-HESPFVGEDNQETFLNISQVNV 229
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
388-619 1.14e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 69.61  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTL-KDASDNARKDFHREAE---LLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd05604     4 IGKGSFGKVLLAK-----RKRDGKYYAVKVLqKKVILNRKEQKHIMAErnvLLKNVKHPFLVGLHYSFQTTDKLYFVLDF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLnkFLRahgpdavLMAEGNPPteltQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd05604    79 VNGGEL--FFH-------LQRERSFP----EPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCK 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 544 D-VYSTDYYRVGGHTmlPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFtYGKQPWYQLSNNEVIECITQGRVLQRP 619
Cdd:cd05604   146 EgISNSDTTTTFCGT--P-EYLAPEVIRKQPYDNTVDWWCLGSVLYEML-YGLPPFYCRDTAEMYENILHKPLVLRP 218
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
386-590 1.44e-12

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 68.25  E-value: 1.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECynlcpEQDKILVAVKTLKDASDNAR---KDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd06607     7 REIGHGSFGAVYYARN-----KRTSEVVAIKKMSYSGKQSTekwQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKhGDLNKFLRAHgpdavlmaeGNPPTELTQSQMLHIAQQiaaGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGmS 542
Cdd:cd06607    82 YCL-GSASDIVEVH---------KKPLQEVEIAAICHGALQ---GLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG-S 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 543 RDVYSTDYYRVGghtmLPIrWMPPESIMYR---KFTTESDVWSLGVVLWEI 590
Cdd:cd06607   148 ASLVCPANSFVG----TPY-WMAPEVILAMdegQYDGKVDVWSLGITCIEL 193
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
388-603 1.48e-12

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 68.63  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLK---DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPL------I 458
Cdd:cd13989     1 LGSGGFGYVTLWK-----HQDTGEYVAIKKCRqelSPSDKNRERWCLEVQIMKKLNHPNVVSARDVPPELEKLspndlpL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLrahgpdavlmaegNPPTE---LTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCL---VGENL 532
Cdd:cd13989    76 LAMEYCSGGDLRKVL-------------NQPENccgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVlqqGGGRV 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 533 LVKIGDFGMSRDVystDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSN 603
Cdd:cd13989   143 IYKLIDLGYAKEL---DQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECIT-GYRPFLPNWQ 209
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
386-654 1.80e-12

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 68.48  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcyNLcpeQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCV--EGDP---LIMV 460
Cdd:cd13986     6 RLLGEGGFSFVYLVE--DL---STGRLYALKKILCHSKEDVKEAMREIENYRLFNHPNILRLLDSQIvkEAGGkkeVYLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAhgpdavLMAEGNPpteLTQSQMLHIAQQIAAGMVYLASQH---FVHRDLATRNCLVGENLLVKIG 537
Cdd:cd13986    81 LPYYKRGSLQDEIER------RLVKGTF---FPEDRILHIFLGICRGLKAMHEPElvpYAHRDIKPGNVLLSEDDEPILM 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 538 DFGMSRDVYSTDYYR---------VGGHTMLPIRwmPPESimyrkFTTES--------DVWSLGVVLWEIFtYGKQPW-Y 599
Cdd:cd13986   152 DLGSMNPARIEIEGRrealalqdwAAEHCTMPYR--APEL-----FDVKShctidektDIWSLGCTLYALM-YGESPFeR 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 600 QLSNNEVIECITQGRVLQRPRTC--PQEVYELMLGCWQREPHMRKNIKGIHTLLQNL 654
Cdd:cd13986   224 IFQKGDSLALAVLSGNYSFPDNSrySEELHQLVKSMLVVNPAERPSIDDLLSRVHDL 280
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
379-590 1.95e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 68.13  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAEcyNLcpeQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLI 458
Cdd:cd06646     8 QHDYELIQRVGSGTYGDVYKAR--NL---HTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGD 538
Cdd:cd06646    83 ICMEYCGGGSLQDIYHVTGP-------------LSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLAD 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 539 FGMSRDVYSTDYYRvGGHTMLPIrWMPPESIMYRK---FTTESDVWSLGVVLWEI 590
Cdd:cd06646   150 FGVAAKITATIAKR-KSFIGTPY-WMAPEVAAVEKnggYNQLCDIWAVGITAIEL 202
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
381-592 2.01e-12

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 68.02  E-value: 2.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVflaecyNLCPE-QDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd14190     5 SIHSKEVLGGGKFGKV------HTCTEkRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLnkFLRahgpdavLMAEGNPpteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRN--CLVGENLLVKIG 537
Cdd:cd14190    79 FMEYVEGGEL--FER-------IVDEDYH---LTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENilCVNRTGHQVKII 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 538 DFGMSRDVYSTDYYRVGGHTmlPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd14190   147 DFGLARRYNPREKLKVNFGT--P-EFLSPEVVNYDQVSFPTDMWSMGVITYMLLS 198
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
387-590 2.12e-12

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 68.48  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd07872    13 KLGEGTYATVFKGR-----SKLTENLVALKEIRlEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HgDLNKFLRAHGPdavLMAEGNPPTELTQsqmlhiaqqIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR-- 543
Cdd:cd07872    88 K-DLKQYMDDCGN---IMSMHNVKIFLYQ---------ILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARak 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1610576541 544 DVYSTDYyrvgGHTMLPIRWMPPESIM-YRKFTTESDVWSLGVVLWEI 590
Cdd:cd07872   155 SVPTKTY----SNEVVTLWYRPPDVLLgSSEYSTQIDMWGVGCIFFEM 198
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
388-598 2.30e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 68.55  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecYNLCpEQDKILVAVKTL-KDASDNARKDFH----REAELLTNLQHEHIVKFYG-VCVEGDPLIMVF 461
Cdd:cd14041    14 LGRGGFSEVYKA--FDLT-EQRYVAVKIHQLnKNWRDEKKENYHkhacREYRIHKELDHPRIVKLYDyFSLDTDSFCTVL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAHGpdavLMAEgnppteltqSQMLHIAQQIAAGMVYLASQH--FVHRDLATRNCLV------GEnll 533
Cdd:cd14041    91 EYCEGNDLDFYLKQHK----LMSE---------KEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvngtacGE--- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 534 VKIGDFGMSRDVYSTDYYRVGGHTMLP-----IRWMPPESIMY----RKFTTESDVWSLGVVLWEIFtYGKQPW 598
Cdd:cd14041   155 IKITDFGLSKIMDDDSYNSVDGMELTSqgagtYWYLPPECFVVgkepPKISNKVDVWSVGVIFYQCL-YGRKPF 227
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
387-590 2.30e-12

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 68.18  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARK-DFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMk 465
Cdd:cd07869    12 KLGEGSYATVYKGK-----SKVNGKLVALKVIRLQEEEGTPfTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYV- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR-- 543
Cdd:cd07869    86 HTDLCQYMDKH------------PGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARak 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1610576541 544 DVYSTDYyrvgGHTMLPIRWMPPESIM-YRKFTTESDVWSLGVVLWEI 590
Cdd:cd07869   154 SVPSHTY----SNEVVTLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEM 197
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
387-592 2.36e-12

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 68.11  E-value: 2.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd07873     9 KLGEGTYATVYKGR-----SKLTDNLVALKEIRlEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HgDLNKFLRAHGpDAVLMAEgnppTELTQSQMLHiaqqiaaGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR-D 544
Cdd:cd07873    84 K-DLKQYLDDCG-NSINMHN----VKLFLFQLLR-------GLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARaK 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1610576541 545 VYSTDYYrvgGHTMLPIRWMPPESIM-YRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd07873   151 SIPTKTY---SNEVVTLWYRPPDILLgSTDYSTQIDMWGVGCIFYEMST 196
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
384-599 2.44e-12

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 68.22  E-value: 2.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVflAECYNLCPEQDkilVAVK--TLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd14086     5 LKEELGKGAFSVV--RRCVQKSTGQE---FAAKiiNTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLnkFlrahgpDAVLMAEgnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVG---ENLLVKIGD 538
Cdd:cd14086    80 DLVTGGEL--F------EDIVARE-----FYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLAsksKGAAVKLAD 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 539 FGMSRDVySTDYYRVGGHTMLPIrWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWY 599
Cdd:cd14086   147 FGLAIEV-QGDQQAWFGFAGTPG-YLSPEVLRKDPYGKPVDIWACGVILY-ILLVGYPPFW 204
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
388-592 3.27e-12

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 68.53  E-value: 3.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflaecynlCPEQDK---ILVAVKTLKDASDNA--RKDFHREAELLTNLQHEHIVKFYGVCVEGDPL----- 457
Cdd:cd07877    25 VGSGAYGSV--------CAAFDTktgLRVAVKKLSRPFQSIihAKRTYRELRLLKHMKHENVIGLLDVFTPARSLeefnd 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd07877    97 VYLVTHLMGADLNNIVKCQ--------------KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKIL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 538 DFGMSRdvySTDYYRVGghtMLPIRWMPPESIM--YRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd07877   163 DFGLAR---HTDDEMTG---YVATRWYRAPEIMlnWMHYNQTVDIWSVGCIMAELLT 213
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
376-665 3.54e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 68.12  E-value: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 376 HIKRHNIVLKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTL-KDASDNARKDFHREAE---LLTNLQHEHIVKFYGVC 451
Cdd:cd05602     3 HAKPSDFHFLKVIGKGSFGKVLLAR-----HKSDEKFYAVKVLqKKAILKKKEEKHIMSErnvLLKNVKHPFLVGLHFSF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 452 VEGDPLIMVFEYMKHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGEN 531
Cdd:cd05602    78 QTTDKLYFVLDYINGGELFYHLQRE-------------RCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQ 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 532 LLVKIGDFGMSRDvySTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFtYGKQPWYQLSNNEVIECIT 611
Cdd:cd05602   145 GHIVLTDFGLCKE--NIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEML-YGLPPFYSRNTAEMYDNIL 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 612 QgRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDIL 665
Cdd:cd05602   222 N-KPLQLKPNITNSARHLLEGLLQKDRTKRLGAKDDFTEIKNHIFFSPINWDDL 274
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
380-613 3.58e-12

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 67.46  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 380 HNIVLKRELGEGAFGKVFLAECYNLCPEQdkilVAVKTLKDA---SDN----ARKDFHREAELLTNLQHEHIVKFYGVCV 452
Cdd:cd14096     1 ENYRLINKIGEGAFSNVYKAVPLRNTGKP----VAIKVVRKAdlsSDNlkgsSRANILKEVQIMKRLSHPNIVKLLDFQE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 453 EGDPLIMVFEYMKHGDL-NKFLRAhgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV--- 528
Cdd:cd14096    77 SDEYYYIVLELADGGEIfHQIVRL--------------TYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFepi 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 529 ------------------------------GENLLVKIGDFGMSRDVYSTdyyrvggHTMLP---IRWMPPESIMYRKFT 575
Cdd:cd14096   143 pfipsivklrkadddetkvdegefipgvggGGIGIVKLADFGLSKQVWDS-------NTKTPcgtVGYTAPEVVKDERYS 215
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1610576541 576 TESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQG 613
Cdd:cd14096   216 KKVDMWALGCVLYTLLC-GFPPFYDESIETLTEKISRG 252
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
388-592 3.68e-12

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 67.22  E-value: 3.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLCpeqdkilVAVKTLKDASDNARKD----FHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd14160     1 IGEGEIFEVYRVRIGNRS-------YAVKLFKQEKKMQWKKhwkrFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGPDavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQH---FVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd14160    74 MQNGTLFDRLQCHGVT----------KPLSWHERINILIGIAKAIHYLHNSQpctVICGNISSANILLDDQMQPKLTDFA 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 541 MSR------DVYSTDYYRVGGHTMLpiRWMPPESIMYRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd14160   144 LAHfrphleDQSCTINMTTALHKHL--WYMPEEYIRQGKLSVKTDVYSFGIVIMEVLT 199
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
388-656 4.71e-12

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 66.96  E-value: 4.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLcpeqdkilVAVKTLKDASDNAR--KDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd14153     8 IGKGRFGQVYHGRWHGE--------VAIRLIDIERDNEEqlKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRahgpDAVLMAEGNppteltqsQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVgENLLVKIGDFGM---- 541
Cdd:cd14153    80 GRTLYSVVR----DAKVVLDVN--------KTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLftis 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 ------SRDvystDYYRV--GGHTMLP---IRWMPPESIMYR-KFTTESDVWSLGVVLWEIftYGKQPWYQLSNNEVIec 609
Cdd:cd14153   147 gvlqagRRE----DKLRIqsGWLCHLApeiIRQLSPETEEDKlPFSKHSDVFAFGTIWYEL--HAREWPFKTQPAEAI-- 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 610 ITQGRVLQRPRTCP----QEVYELMLGCWQREPHMRKNIKGIHTLLQNLAK 656
Cdd:cd14153   219 IWQVGSGMKPNLSQigmgKEISDILLFCWAYEQEERPTFSKLMEMLEKLPK 269
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
386-590 5.42e-12

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 67.85  E-value: 5.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVflaecYNLCPEQDKILVAVKTLKDASDN--ARKDFHREAELLTNLQHEHIVKfyGVCVEGDPLIMVFEY 463
Cdd:cd07853     6 RPIGYGAFGVV-----WSVTDPRDGKRVALKKMPNVFQNlvSCKRVFRELKMLCFFKHDNVLS--ALDILQPPHIDPFEE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 M------KHGDLNKFLRAhgpdavlmaegnpPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd07853    79 IyvvtelMQSDLHKIIVS-------------PQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKIC 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 538 DFG------------MSRDVYsTDYYRVgghtmlpirwmpPESIM-YRKFTTESDVWSLGVVLWEI 590
Cdd:cd07853   146 DFGlarveepdeskhMTQEVV-TQYYRA------------PEILMgSRHYTSAVDIWSVGCIFAEL 198
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
386-592 5.68e-12

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 67.67  E-value: 5.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVflaeCYNLcPEQDKILVAVKTLKD--ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPL------ 457
Cdd:cd07880    21 KQVGSGAYGTV----CSAL-DRRTGAKVAIKKLYRpfQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLdrfhdf 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKhGDLNKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd07880    96 YLVMPFMG-TDLGKLMKHE--------------KLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKIL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 538 DFGMSRdvySTDYYRVGghtMLPIRWM-PPESIM-YRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd07880   161 DFGLAR---QTDSEMTG---YVVTRWYrAPEVILnWMHYTQTVDIWSVGCIMAEMLT 211
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
381-592 6.72e-12

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 66.38  E-value: 6.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVflAECYNLcPEQDKILVAVKTLKDASDNA--RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLI 458
Cdd:cd14070     3 SYLIGRKLGEGSFAKV--REGLHA-VTGEKVAIKVIDKKKAKKDSyvTKNLRREGRIQQMIRHPNITQLLDILETENSYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDL-NKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd14070    80 LVMELCPGGNLmHRIYDKK--------------RLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLI 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1610576541 538 DFGMSRDV----YSTDYYRVGGHTMlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd14070   146 DFGLSNCAgilgYSDPFSTQCGSPA----YAAPELLARKKYGPKVDVWSIGVNMYAMLT 200
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
388-598 7.25e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 66.62  E-value: 7.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecYNLCpEQDKILVAVKTL-KDASDNARKDFH----REAELLTNLQHEHIVKFYG-VCVEGDPLIMVF 461
Cdd:cd14040    14 LGRGGFSEVYKA--FDLY-EQRYAAVKIHQLnKSWRDEKKENYHkhacREYRIHKELDHPRIVKLYDyFSLDTDTFCTVL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAHGpdavLMAEgnppteltqSQMLHIAQQIAAGMVYL--ASQHFVHRDLATRNCLVGENLL---VKI 536
Cdd:cd14040    91 EYCEGNDLDFYLKQHK----LMSE---------KEARSIVMQIVNALRYLneIKPPIIHYDLKPGNILLVDGTAcgeIKI 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSR----DVYSTDYYRVGGHTMLPIRWMPPESIMY----RKFTTESDVWSLGVVLWEIFtYGKQPW 598
Cdd:cd14040   158 TDFGLSKimddDSYGVDGMDLTSQGAGTYWYLPPECFVVgkepPKISNKVDVWSVGVIFFQCL-YGRKPF 226
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
388-641 7.32e-12

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 67.41  E-value: 7.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKDFHR---EAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd05593    23 LGKGTFGKVILVR-----EKASGKYYAMKILKKEVIIAKDEVAHtltESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd05593    98 NGGELFFHLSRE-------------RVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 VYsTDYYRVGGHTMLPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRVlQRPRTCPQ 624
Cdd:cd05593   165 GI-TDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELILMEDI-KFPRTLSA 240
                         250
                  ....*....|....*..
gi 1610576541 625 EVYELMLGCWQREPHMR 641
Cdd:cd05593   241 DAKSLLSGLLIKDPNKR 257
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
387-612 9.11e-12

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 66.23  E-value: 9.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVflaecYNLCPEQDKILVAVKTLKDASDN-ARKDFHREAELLTNLQH-EHIVKFYGVCV-EGDPLIMVfEY 463
Cdd:cd06616    13 EIGRGAFGTV-----NKMLHKPSGTIMAVKRIRSTVDEkEQKRLLMDLDVVMRSSDcPYIVKFYGALFrEGDCWICM-EL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHgDLNKFLRahgpdavlMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQ-HFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd06616    87 MDI-SLDKFYK--------YVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGIS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 ----------RDVYSTDYyrvgghtMLPIRWMPpeSIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLsnNEVIECITQ 612
Cdd:cd06616   158 gqlvdsiaktRDAGCRPY-------MAPERIDP--SASRDGYDVRSDVWSLGITLYEVAT-GKFPYPKW--NSVFDQLTQ 225
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
388-610 1.17e-11

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 65.37  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflaecyNLCPEQDKIL-VAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd14192    12 LGGGRFGQV------HKCTELSTGLtLAAKIIKVKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLnkFLRAHgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRN--CLVGENLLVKIGDFGMSRD 544
Cdd:cd14192    86 GEL--FDRIT----------DESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENilCVNSTGNQIKIIDFGLARR 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 545 VYSTDYYRVGGHTmlPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECI 610
Cdd:cd14192   154 YKPREKLKVNFGT--P-EFLAPEVVNYDFVSFPTDMWSVGVITYMLLS-GLSPFLGETDAETMNNI 215
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
387-598 1.19e-11

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 65.90  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAecYNLCPEQDkilVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd06656    26 KIGQGASGTVYTA--IDIATGQE---VAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAhgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVY 546
Cdd:cd06656   101 GSLTDVVTE--------------TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 547 STDYYRvggHTMLPI-RWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd06656   167 PEQSKR---STMVGTpYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPY 215
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
425-611 1.43e-11

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 65.41  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 425 ARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLrahgpdavlmAEGNPPTELTQSQMLhiaQQI 504
Cdd:cd14195    51 SREEIEREVNILREIQHPNIITLHDIFENKTDVVLILELVSGGELFDFL----------AEKESLTEEEATQFL---KQI 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 505 AAGMVYLASQHFVHRDLATRNCLVGE----NLLVKIGDFGMSRDVYSTDYYRvggHTMLPIRWMPPESIMYRKFTTESDV 580
Cdd:cd14195   118 LDGVHYLHSKRIAHFDLKPENIMLLDknvpNPRIKLIDFGIAHKIEAGNEFK---NIFGTPEFVAPEIVNYEPLGLEADM 194
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1610576541 581 WSLGVVLWeIFTYGKQPWYQLSNNEVIECIT 611
Cdd:cd14195   195 WSIGVITY-ILLSGASPFLGETKQETLTNIS 224
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
386-641 1.44e-11

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 66.08  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECynlcpEQDKILVAVKTLKD----ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd05590     1 RVLGKGSFGKVMLARL-----KESGRLYAVKVLKKdvilQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLnkflrahgpdavlMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd05590    76 EFVNGGDL-------------MFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGM 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SRD------VYST-----DYyrvgghtmlpirwMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECI 610
Cdd:cd05590   143 CKEgifngkTTSTfcgtpDY-------------IAPEILQEMLYGPSVDWWAMGVLLYEMLC-GHAPFEAENEDDLFEAI 208
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1610576541 611 TQGRVLQrPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05590   209 LNDEVVY-PTWLSQDAVDILKAFMTKNPTMR 238
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
413-645 1.54e-11

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 65.37  E-value: 1.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 413 VAVK-TLKDASDNARkdfhREAELLTNL-QHEHIVKFYgvCVEGDPLIM----------VFEYMKHGDLNKFLRAHGPDa 480
Cdd:cd13982    28 VAVKrLLPEFFDFAD----REVQLLRESdEHPNVIRYF--CTEKDRQFLyialelcaasLQDLVESPRESKLFLRPGLE- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 481 vlmaegnppteltqsqMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV-----GENLLVKIGDFGMSRDVySTDYYRVGG 555
Cdd:cd13982   101 ----------------PVRLLRQIASGLAHLHSLNIVHRDLKPQNILIstpnaHGNVRAMISDFGLCKKL-DVGRSSFSR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 556 HTMLP--IRWMPPESIM---YRKFTTESDVWSLGVVLWEIFTYGKQPW---YQLSNNeviecITQGRV----LQRPRTCP 623
Cdd:cd13982   164 RSGVAgtSGWIAPEMLSgstKRRQTRAVDIFSLGCVFYYVLSGGSHPFgdkLEREAN-----ILKGKYsldkLLSLGEHG 238
                         250       260
                  ....*....|....*....|..
gi 1610576541 624 QEVYELMLGCWQREPHMRKNIK 645
Cdd:cd13982   239 PEAQDLIERMIDFDPEKRPSAE 260
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
387-613 1.65e-11

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 65.20  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVflaecyNLCPEQDKILV-AVKTLKDASDNA------RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd14105    12 ELGSGQFAVV------KKCREKSTGLEyAAKFIKKRRSKAsrrgvsREDIEREVSILRQVLHPNIITLHDVFENKTDVVL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLrahgpdavlmAEGNPPTELTQSQMLhiaQQIAAGMVYLASQHFVHRDLATRNCLVGE----NLLVK 535
Cdd:cd14105    86 ILELVAGGELFDFL----------AEKESLSEEEATEFL---KQILDGVNYLHTKNIAHFDLKPENIMLLDknvpIPRIK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 536 IGDFGMSRDVYSTDYYRVGGHTmlPiRWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECITQG 613
Cdd:cd14105   153 LIDFGLAHKIEDGNEFKNIFGT--P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANITAV 226
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
387-598 1.79e-11

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 65.52  E-value: 1.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAecYNLCPEQDkilVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd06654    27 KIGQGASGTVYTA--MDVATGQE---VAIRQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAhgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVY 546
Cdd:cd06654   102 GSLTDVVTE--------------TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 547 STDYYRvggHTMLPI-RWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd06654   168 PEQSKR---STMVGTpYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPY 216
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
388-592 2.00e-11

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 64.99  E-value: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYnlcpeQDKILVAVKTLKDASDNARKDFH-REAELLTNLQ-HEHIVKFYGVCVEGDP--LIMVFEY 463
Cdd:cd07831     7 IGEGTFSEVLKAQSR-----KTGKYYAIKCMKKHFKSLEQVNNlREIQALRRLSpHPNILRLIEVLFDRKTgrLALVFEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MkhgDLNKFlrahgpdaVLMAEGNPPteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLvKIGDFGMSR 543
Cdd:cd07831    82 M---DMNLY--------ELIKGRKRP--LPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDIL-KLADFGSCR 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 544 DVYS----TDYyrvgghtmLPIRWM-PPESIM---YrkFTTESDVWSLGVVLWEIFT 592
Cdd:cd07831   148 GIYSkppyTEY--------ISTRWYrAPECLLtdgY--YGPKMDIWAVGCVFFEILS 194
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
384-647 2.14e-11

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 64.57  E-value: 2.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVflaecYNLCPEQDKILVAVKTLKDASDNARKDFHRE----AE-----LLTNLQHEHIVKFYGVCVEG 454
Cdd:cd14005     4 VGDLLGKGGFGTV-----YSGVRIRDGLPVAVKFVPKSRVTEWAMINGPvpvpLEialllKASKPGVPGVIRLLDWYERP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEY----MkhgDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVG- 529
Cdd:cd14005    79 DGFLLIMERpepcQ---DLFDFITERGA-------------LSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINl 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 530 ENLLVKIGDFG---MSRDVYSTDY--YRVGghtmlpirwMPPESIMYRKF-TTESDVWSLGVVLWEIFTyGKQPWYQLSN 603
Cdd:cd14005   143 RTGEVKLIDFGcgaLLKDSVYTDFdgTRVY---------SPPEWIRHGRYhGRPATVWSLGILLYDMLC-GDIPFENDEQ 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1610576541 604 neviecITQGRVLQRPRTCPqEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14005   213 ------ILRGNVLFRPRLSK-ECCDLISRCLQFDPSKRPSLEQI 249
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
386-588 2.42e-11

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 64.58  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVflAECYnlcPEQDKILVAVKTLKDASDNARKDF-HREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd14185     6 RTIGDGNFAVV--KECR---HWNENQEYAMKIIDKSKLKGKEDMiESEILIIKSLSHPNIVKLFEVYETEKEIYLILEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDL----NKFLRAHGPDAVLMAegnppTELTQSqmlhiaqqiaagMVYLASQHFVHRDLATRNCLVGEN----LLVKI 536
Cdd:cd14185    81 RGGDLfdaiIESVKFTEHDAALMI-----IDLCEA------------LVYIHSKHIVHRDLKPENLLVQHNpdksTTLKL 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 537 GDFGMSRDVYSTDYYRVGGHTmlpirWMPPESIMYRKFTTESDVWSLGVVLW 588
Cdd:cd14185   144 ADFGLAKYVTGPIFTVCGTPT-----YVAPEILSEKGYGLEVDMWAAGVILY 190
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
388-590 3.23e-11

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 64.77  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynLCPEqdkiLVAVKTLkdaSDNARKDFHREAELLTN--LQHEHIVKFygvcVEGD--------PL 457
Cdd:cd14143     3 IGKGRFGEVWRGR---WRGE----DVAVKIF---SSREERSWFREAEIYQTvmLRHENILGF----IAADnkdngtwtQL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQ--------HFVHRDLATRNCLVG 529
Cdd:cd14143    69 WLVSDYHEHGSLFDYLNRY--------------TVTVEGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDLKSKNILVK 134
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 530 ENLLVKIGDFGMS-RDVYSTDY------YRVGGHtmlpiRWMPPE----SIMYRKFTT--ESDVWSLGVVLWEI 590
Cdd:cd14143   135 KNGTCCIADLGLAvRHDSATDTidiapnHRVGTK-----RYMAPEvlddTINMKHFESfkRADIYALGLVFWEI 203
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
426-588 3.24e-11

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 64.30  E-value: 3.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 426 RKDFHREAELLTNLQ-HEHIVKFYGVcVEGDPLI-MVFEYMKHGDLNKFLrahgpdavlmaegNPPTELTQSQMLHIAQQ 503
Cdd:cd14093    52 REATRREIEILRQVSgHPNIIELHDV-FESPTFIfLVFELCRKGELFDYL-------------TEVVTLSEKKTRRIMRQ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 504 IAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTmlPiRWMPPESI---MYRK---FTTE 577
Cdd:cd14093   118 LFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGEKLRELCGT--P-GYLAPEVLkcsMYDNapgYGKE 194
                         170
                  ....*....|.
gi 1610576541 578 SDVWSLGVVLW 588
Cdd:cd14093   195 VDMWACGVIMY 205
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
386-666 3.59e-11

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 65.07  E-value: 3.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAecYNLCPEQDkilVAVKTLK---DASDNARKDFhREAELLTNLQHEHIVKFYGV-----CVEGDPL 457
Cdd:cd07878    21 TPVGSGAYGSVCSA--YDTRLRQK---VAVKKLSrpfQSLIHARRTY-RELRLLKHMKHENVIGLLDVftpatSIENFNE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd07878    95 VYLVTNLMGADLNNIVKCQ--------------KLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRIL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 538 DFGMSRdvySTDYYRVGghtMLPIRWMPPESIM--YRKFTTESDVWSLGVVLWEIFTyGKQpwyQLSNNEVIECITqgRV 615
Cdd:cd07878   161 DFGLAR---QADDEMTG---YVATRWYRAPEIMlnWMHYNQTVDIWSVGCIMAELLK-GKA---LFPGNDYIDQLK--RI 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 616 LQRPRTCPQEVYELMlgcwqREPHMRKNIKGI-HTLLQNLAK----ASPVYLDILG 666
Cdd:cd07878   229 MEVVGTPSPEVLKKI-----SSEHARKYIQSLpHMPQQDLKKifrgANPLAIDLLE 279
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
388-621 3.65e-11

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 65.03  E-value: 3.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynlCPEQDKILVAVKTLKDASDNARKDF-HREAE--LLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd05598     9 IGVGAFGEVSLV-----RKKDTNALYAMKTLRKKDVLKRNQVaHVKAErdILAEADNEWVVKLYYSFQDKENLYFVMDYI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNkflrahgpdAVLMAEGNPPTELTQsqmLHIAQQIAAgmvyLASQH---FVHRDLATRNCLVGENLLVKIGDFGM 541
Cdd:cd05598    84 PGGDLM---------SLLIKKGIFEEDLAR---FYIAELVCA----IESVHkmgFIHRDIKPDNILIDRDGHIKLTDFGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 S---RDVYSTDYYRvgGHTML--PiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEvieciTQGRVL 616
Cdd:cd05598   148 CtgfRWTHDSKYYL--AHSLVgtP-NYIAPEVLLRTGYTQLCDWWSVGVILYEMLV-GQPPFLAQTPAE-----TQLKVI 218

                  ....*
gi 1610576541 617 QRPRT 621
Cdd:cd05598   219 NWRTT 223
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
426-597 3.83e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 64.76  E-value: 3.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 426 RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLnkflrahgpDAVLMAEGNPPTELtqsqMLHIAQQIA 505
Cdd:cd06615    43 RNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSL---------DQVLKKAGRIPENI----LGKISIAVL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 506 AGMVYLASQH-FVHRDLATRNCLVGENLLVKIGDFGMSRDVY-STDYYRVGGHTmlpirWMPPESIMYRKFTTESDVWSL 583
Cdd:cd06615   110 RGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIdSMANSFVGTRS-----YMSPERLQGTHYTVQSDIWSL 184
                         170
                  ....*....|....
gi 1610576541 584 GVVLWEIFTyGKQP 597
Cdd:cd06615   185 GLSLVEMAI-GRYP 197
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
388-615 4.09e-11

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 64.63  E-value: 4.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflAECYNLCPEQDkilVAVKTLkdasdNARKDFHREAELLTNLQ-HEHIVKFYGVCVegDPL--IMVFEYM 464
Cdd:cd14092    14 LGDGSFSVC--RKCVHKKTGQE---FAVKIV-----SRRLDTSREVQLLRLCQgHPNIVKLHEVFQ--DELhtYLVMELL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV---GENLLVKIGDFGM 541
Cdd:cd14092    82 RGGELLERIRKK-------------KRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SRdvystdyYRVGGHTM------LPirWMPPEsIMYRKFTT----ES-DVWSLGVVLWEIFTyGKQPW----YQLSNNEV 606
Cdd:cd14092   149 AR-------LKPENQPLktpcftLP--YAAPE-VLKQALSTqgydEScDLWSLGVILYTMLS-GQVPFqspsRNESAAEI 217

                  ....*....
gi 1610576541 607 IECITQGRV 615
Cdd:cd14092   218 MKRIKSGDF 226
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
387-611 4.13e-11

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 64.21  E-value: 4.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVflaecyNLCPEQDK-ILVAVKTLKDASDNA------RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd14196    12 ELGSGQFAIV------KKCREKSTgLEYAAKFIKKRQSRAsrrgvsREEIEREVSILRQVLHPNIITLHDVYENRTDVVL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL----VK 535
Cdd:cd14196    86 ILELVSGGELFDFLAQK-------------ESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 536 IGDFGMSRDVYS-TDYYRVGGHTmlpiRWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECIT 611
Cdd:cd14196   153 LIDFGLAHEIEDgVEFKNIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANIT 224
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
388-665 4.27e-11

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 64.61  E-value: 4.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKD-FHREAE---LLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd05603     3 IGKGSFGKVLLAK-----RKCDGKFYAVKVLQKKTILKKKEqNHIMAErnvLLKNLKHPFLVGLHYSFQTSEKLYFVLDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd05603    78 VNGGELFFHLQRE-------------RCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 D-VYSTDYYRVGGHTmlPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFtYGKQPWYQLSNNEVIECITQgRVLQRPRTC 622
Cdd:cd05603   145 EgMEPEETTSTFCGT--P-EYLAPEVLRKEPYDRTVDWWCLGAVLYEML-YGLPPFYSRDVSQMYDNILH-KPLHLPGGK 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1610576541 623 PQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDIL 665
Cdd:cd05603   220 TVAACDLLQGLLHKDQRRRLGAKADFLEIKNHVFFSPINWDDL 262
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
388-590 4.49e-11

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 64.35  E-value: 4.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYnlcpeQDKILVAVKTLkDASDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDP------LIMV 460
Cdd:cd06637    14 VGNGTYGQVYKGRHV-----KTGQLAAIKVM-DVTGDEEEEIKQEINMLKKYsHHRNIATYYGAFIKKNPpgmddqLWLV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNkflrahgpDAVLMAEGNpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd06637    88 MEFCGAGSVT--------DLIKNTKGN---TLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFG 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 541 MSRDVYSTDYYRvggHTMLPI-RWMPPESIMYRK-----FTTESDVWSLGVVLWEI 590
Cdd:cd06637   157 VSAQLDRTVGRR---NTFIGTpYWMAPEVIACDEnpdatYDFKSDLWSLGITAIEM 209
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
388-595 4.69e-11

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 64.80  E-value: 4.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflaecynlCPEQDKI---LVAVKTLKDASDNArKDFHR---EAELLTNLQHEHIVKFYGVCVEGDP----- 456
Cdd:cd07859     8 IGKGSYGVV--------CSAIDTHtgeKVAIKKINDVFEHV-SDATRilrEIKLLRLLRHPDIVEIKHIMLPPSRrefkd 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKhGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKI 536
Cdd:cd07859    79 IYVVFELME-SDLHQVIKAN-------------DDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKI 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSR--------DVYSTDYyrvgghtmLPIRWM-PPE--SIMYRKFTTESDVWSLGVVLWEIFTyGK 595
Cdd:cd07859   145 CDFGLARvafndtptAIFWTDY--------VATRWYrAPElcGSFFSKYTPAIDIWSIGCIFAEVLT-GK 205
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
48-114 4.73e-11

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 59.12  E-value: 4.73e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541  48 PNLTVEEGKSITLSCSVAGDPVPNMYWDVGNLVSKH----MNETSHTQGSLRITNISSDDSGKqISCVAEN 114
Cdd:pfam13927   9 SSVTVREGETVTLTCEATGSPPPTITWYKNGEPISSgstrSRSLSGSNSTLTISNVTRSDAGT-YTCVASN 78
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
386-641 4.92e-11

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 63.91  E-value: 4.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECynlcpEQDKILVAVK-TLKDASdnarkdFHREAELLTN--LQHEHIVKFYGVCVEGD----PLI 458
Cdd:cd14220     1 RQIGKGRYGEVWMGKW-----RGEKVAVKVFfTTEEAS------WFRETEIYQTvlMRHENILGFIAADIKGTgswtQLY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLRAhgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHF--------VHRDLATRNCLVGE 530
Cdd:cd14220    70 LITDYHENGSLYDFLKC--------------TTLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKK 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 531 NLLVKIGDFGMS----RDVYSTDY---YRVGGHtmlpiRWMPP----ESIMYRKFTT--ESDVWSLGVVLWEI----FTY 593
Cdd:cd14220   136 NGTCCIADLGLAvkfnSDTNEVDVplnTRVGTK-----RYMAPevldESLNKNHFQAyiMADIYSFGLIIWEMarrcVTG 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 594 G-----KQPWYQLSNN--------EVIeCITQGRVLQRPR----TCPQEVYELMLGCWQREPHMR 641
Cdd:cd14220   211 GiveeyQLPYYDMVPSdpsyedmrEVV-CVKRLRPTVSNRwnsdECLRAVLKLMSECWAHNPASR 274
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
388-595 5.51e-11

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 64.54  E-value: 5.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynlCPEQDKILVAVKTLKDA--SDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPL------IM 459
Cdd:cd07879    23 VGSGAYGSVCSA-----IDKRTGEKVAIKKLSRPfqSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGdefqdfYL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKhGDLNKfLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd07879    98 VMPYMQ-TDLQK-IMGH--------------PLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDF 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMSR--DVYSTDYyrvgghtmLPIRWM-PPESIM-YRKFTTESDVWSLGVVLWEIFTyGK 595
Cdd:cd07879   162 GLARhaDAEMTGY--------VVTRWYrAPEVILnWMHYNQTVDIWSVGCIMAEMLT-GK 212
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
387-647 6.43e-11

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 63.59  E-value: 6.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVflaecYNLCPEQDKILVAVKTLKDA--SDNARKDFHREAELLTNLQHEHIVKFY----GVCVEGDPLIMV 460
Cdd:cd14031    17 ELGRGAFKTV-----YKGLDTETWVEVAWCELQDRklTKAEQQRFKEEAEMLKGLQHPNIVRFYdsweSVLKGKKCIVLV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHI-AQQIAAGMVYLASQH--FVHRDLATRNCLV-GENLLVKI 536
Cdd:cd14031    92 TELMTSGTLKTYLKRF--------------KVMKPKVLRSwCRQILKGLQFLHTRTppIIHRDLKCDNIFItGPTGSVKI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSRDVYSTDYYRVGGHTmlpiRWMPPEsiMYRKFTTES-DVWSLGVVLWEIFTyGKQPWYQLSN-NEVIECITQG- 613
Cdd:cd14031   158 GDLGLATLMRTSFAKSVIGTP----EFMAPE--MYEEHYDESvDVYAFGMCMLEMAT-SEYPYSECQNaAQIYRKVTSGi 230
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1610576541 614 RVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14031   231 KPASFNKVTDPEVKEIIEGCIRQNKSERLSIKDL 264
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
388-614 7.12e-11

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 64.05  E-value: 7.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAecynlcpeQDKI---LVAVKTLKDASDNARKDFH-REAELLTNLQHEHIVKFYGVCVE----GDPLIM 459
Cdd:cd13988     1 LGQGATANVFRG--------RHKKtgdLYAVKVFNNLSFMRPLDVQmREFEVLKKLNHKNIVKLFAIEEElttrHKVLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 vfEYMKHGDLNKFL----RAHGpdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCL--VGEN-- 531
Cdd:cd13988    73 --ELCPCGSLYTVLeepsNAYG--------------LPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDgq 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 532 LLVKIGDFGMSRD---------VYSTDYYRvggHTMLPIRWMPPESIMyRKFTTESDVWSLGVVLWEIFTyGKQPWYQLS 602
Cdd:cd13988   137 SVYKLTDFGAAREleddeqfvsLYGTEEYL---HPDMYERAVLRKDHQ-KKYGATVDLWSIGVTFYHAAT-GSLPFRPFE 211
                         250
                  ....*....|....*.
gi 1610576541 603 ----NNEVIECITQGR 614
Cdd:cd13988   212 gprrNKEVMYKIITGK 227
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
431-641 8.34e-11

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 62.76  E-value: 8.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 431 REAELLTNLQHEHIVKFYGVCVE--GDP----LIMVFEYMKHGDLNKFLRAHGPdaVLMAEGNppteltqsqmlHIAQQI 504
Cdd:cd14012    47 KELESLKKLRHPNLVSYLAFSIErrGRSdgwkVYLLTEYAPGGSLSELLDSVGS--VPLDTAR-----------RWTLQL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 505 AAGMVYLASQHFVHRDLATRNCLVGENLL---VKIGDFGMSRDVYSTDyYRVGGHTMLPIRWMPPESI-MYRKFTTESDV 580
Cdd:cd14012   114 LEALEYLHRNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLLDMC-SRGSLDEFKQTYWLPPELAqGSKSPTRKTDV 192
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 581 WSLGVVLWEIFTyGKQPW-YQLSNNEVIEcitqgrvlqrPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd14012   193 WDLGLLFLQMLF-GLDVLeKYTSPNPVLV----------SLDLSASLQDFLSKCLSLDPKKR 243
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
387-597 9.44e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 63.54  E-value: 9.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFlaecyNLCPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd06650    12 ELGAGNGGVVF-----KVSHKPSGLVMARKLIHlEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLnkflrahgpDAVLMAEGNPPTELtqsqMLHIAQQIAAGMVYLASQH-FVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd06650    87 GGSL---------DQVLKKAGRIPEQI----LGKVSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQ 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 545 VY-STDYYRVGGHTmlpirWMPPESIMYRKFTTESDVWSLGVVLWEIfTYGKQP 597
Cdd:cd06650   154 LIdSMANSFVGTRS-----YMSPERLQGTHYSVQSDIWSMGLSLVEM-AVGRYP 201
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
379-593 9.93e-11

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 63.07  E-value: 9.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAECynlcpEQDKILVAVKTLKDASDNARKDFHREAELLTNLQ-HEHIVKF---YGVCVEG 454
Cdd:cd14037     2 SHHVTIEKYLAEGGFAHVYLVKT-----SNGGNRAALKRVYVNDEHDLNVCKREIEIMKRLSgHKNIVGYidsSANRSGN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 D--PLIMVFEYMKHGDLNKFL--RAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYL--ASQHFVHRDLATRNCLV 528
Cdd:cd14037    77 GvyEVLLLMEYCKGGGVIDLMnqRLQ-------------TGLTESEILKIFCDVCEAVAAMhyLKPPLIHRDLKVENVLI 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 529 GENLLVKIGDFGMS-------RDVYSTDYYR--VGGHTMLPIRwmPPESI-MYRK--FTTESDVWSLGVVLWEIFTY 593
Cdd:cd14037   144 SDSGNYKLCDFGSAttkilppQTKQGVTYVEedIKKYTTLQYR--APEMIdLYRGkpITEKSDIWALGCLLYKLCFY 218
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
432-615 1.27e-10

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 62.34  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 432 EAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDL-------NKFLRahgPDAVLMaegnppteltqsqMLHIAQQI 504
Cdd:cd14095    48 EVAILRRVKHPNIVQLIEEYDTDTELYLVMELVKGGDLfdaitssTKFTE---RDASRM-------------VTDLAQAL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 505 AagmvYLASQHFVHRDLATRNCLVGEN----LLVKIGDFGMSRDVYSTDYYRVGGHTmlpirWMPPESIMYRKFTTESDV 580
Cdd:cd14095   112 K----YLHSLSIVHRDIKPENLLVVEHedgsKSLKLADFGLATEVKEPLFTVCGTPT-----YVAPEILAETGYGLKVDI 182
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1610576541 581 WSLGVVLWeIFTYGKQPWYQLSNN--EVIECITQGRV 615
Cdd:cd14095   183 WAAGVITY-ILLCGFPPFRSPDRDqeELFDLILAGEF 218
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
383-591 1.48e-10

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 62.74  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFgkvflAECYNLCPEQDKILVAVKTLkdasDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd14175     4 VVKETIGVGSY-----SVCKRCVHKATNMEYAVKVI----DKSKRDPSEEIEILLRYgQHPNIITLKDVYDDGKHVYLVT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDL-NKFLRAhgpdavlmaegNPPTELTQSQMLHiaqQIAAGMVYLASQHFVHRDLATRNCLV----GENLLVKI 536
Cdd:cd14175    75 ELMRGGELlDKILRQ-----------KFFSEREASSVLH---TICKTVEYLHSQGVVHRDLKPSNILYvdesGNPESLRI 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 537 GDFGMSRDVYSTDyyrvgGHTMLPI---RWMPPESIMYRKFTTESDVWSLGVVLWEIF 591
Cdd:cd14175   141 CDFGFAKQLRAEN-----GLLMTPCytaNFVAPEVLKRQGYDEGCDIWSLGILLYTML 193
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
388-599 1.52e-10

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 62.43  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflAECYNLCPEQDkilVAVKTLKDASDNARKDFHREAELLTNLQ-HEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd14090    10 LGEGAYASV--QTCINLYTGKE---YAVKIIEKHPGHSRSRVFREVETLHQCQgHPNILQLIEYFEDDERFYLVFEKMRG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFLRAHGPDavlmaegnppTELTQSQmlhIAQQIAAGMVYLASQHFVHRDLATRNCL---VGENLLVKIGDFGMSR 543
Cdd:cd14090    85 GPLLSHIEKRVHF----------TEQEASL---VVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGS 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 544 DVystdyyRVGGHTMLPIR------------WMPPESImyRKFTTES-------DVWSLGVVLWeIFTYGKQPWY 599
Cdd:cd14090   152 GI------KLSSTSMTPVTtpelltpvgsaeYMAPEVV--DAFVGEAlsydkrcDLWSLGVILY-IMLCGYPPFY 217
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
386-600 1.62e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 62.35  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVflaecynlCPEQDKI---LVAVKTLKDASDNARKDFH---REAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd05630     6 RVLGKGGFGEV--------CACQVRAtgkMYACKKLEKKRIKKRKGEAmalNEKQILEKVNSRFVVSLAYAYETKDALCL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLnKFLRAHgpdavlMAEGNPPteltQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd05630    78 VLTLMNGGDL-KFHIYH------MGQAGFP----EARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDL 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 540 GMSRDVY--STDYYRVGghtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQ 600
Cdd:cd05630   147 GLAVHVPegQTIKGRVG-----TVGYMAPEVVKNERYTFSPDWWALGCLLYEMIA-GQSPFQQ 203
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
49-127 1.68e-10

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 57.79  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  49 NLTVEEGKSITLSCSVAGDPVPNMYW--DVGNL-VSKHMNETSHtqgSLRITNISSDDSGKQIsCVAENLVGEDQDSVNL 125
Cdd:cd05725     6 NQVVLVDDSAEFQCEVGGDPVPTVRWrkEDGELpKGRYEILDDH---SLKIRKVTAGDMGSYT-CVAENMVGKIEASATL 81

                  ..
gi 1610576541 126 TV 127
Cdd:cd05725    82 TV 83
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
386-598 1.74e-10

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 62.44  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVflaecYNLCPEQDKILVAVKTLKdASDNARKDFHREAELLTNLQHEH---IVKFYGVCV-EGDPLIMVf 461
Cdd:cd06617     7 EELGRGAYGVV-----DKMRHVPTGTIMAVKRIR-ATVNSQEQKRLLMDLDISMRSVDcpyTVTFYGALFrEGDVWICM- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKhGDLNKFLRAhgpdaVLmaegNPPTELTQSQMLHIAQQIAAGMVYLASQ-HFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd06617    80 EVMD-TSLDKFYKK-----VY----DKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFG 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 541 MS----------RDVYSTDYyrvgghtmlpirwMPPESI----MYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd06617   150 ISgylvdsvaktIDAGCKPY-------------MAPERInpelNQKGYDVKSDVWSLGITMIELAT-GRFPY 207
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
383-599 1.83e-10

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 61.93  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFlaECYNLCPEQDkilVAVKTLKDASDNARK-DFHREAellTNLQH-EHIVKFYGVCVEGDP-LIM 459
Cdd:cd14172     7 LSKQVLGLGVNGKVL--ECFHRRTGQK---CALKLLYDSPKARREvEHHWRA---SGGPHiVHILDVYENMHHGKRcLLI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHGPDAvlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVG---ENLLVKI 536
Cdd:cd14172    79 IMECMEGGELFSRIQERGDQA-----------FTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTskeKDAVLKL 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 537 GDFGMSRDVYSTDYYRVGGHTMLpirWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWY 599
Cdd:cd14172   148 TDFGFAKETTVQNALQTPCYTPY---YVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGFPPFY 206
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
386-599 1.98e-10

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 62.69  E-value: 1.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNlcpeQDKILVAVKTLKDASDNARKDFHR---EAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:PTZ00426   36 RTLGTGSFGRVILATYKN----EDFPPVAIKRFEKSKIIKQKQVDHvfsERKILNYINHPFCVNLYGSFKDESYLYLVLE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:PTZ00426  112 FVIGGEFFTFLRRN-------------KRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFA 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 543 RDVYSTDYYRVGGHtmlpiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWY 599
Cdd:PTZ00426  179 KVVDTRTYTLCGTP-----EYIAPEILLNVGHGKAADWWTLGIFIYEILV-GCPPFY 229
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
387-592 2.00e-10

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 62.14  E-value: 2.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAecynlcpeQDKI---LVAVKT--LKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:PLN00009    9 KIGEGTYGVVYKA--------RDRVtneTIALKKirLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHgDLNKFLrahgpDAVLMAEGNPptELTQSQMLhiaqQIAAGMVYLASQHFVHRDLATRNCLVGE--NLLvKIGDF 539
Cdd:PLN00009   81 EYLDL-DLKKHM-----DSSPDFAKNP--RLIKTYLY----QILRGIAYCHSHRVLHRDLKPQNLLIDRrtNAL-KLADF 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 540 GMSRDVYSTdyYRVGGHTMLPIRWMPPESIM-YRKFTTESDVWSLGVVLWEIFT 592
Cdd:PLN00009  148 GLARAFGIP--VRTFTHEVVTLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVN 199
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
381-552 2.11e-10

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 61.70  E-value: 2.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAecYNLcpeQDKILVAVKTlkDASDNARKDFHREAELLTNLQ-HEHI--VKFYGvcVEGDPL 457
Cdd:cd14016     1 RYKLVKKIGSGSFGEVYLG--IDL---KTGEEVAIKI--EKKDSKHPQLEYEAKVYKLLQgGPGIprLYWFG--QEGDYN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHgDLNKFLRAHG----PDAVLM-AEgnppteltqsQMLHIAQqiaagmvYLASQHFVHRDLATRNCLVG--- 529
Cdd:cd14016    72 VMVMDLLGP-SLEDLFNKCGrkfsLKTVLMlAD----------QMISRLE-------YLHSKGYIHRDIKPENFLMGlgk 133
                         170       180
                  ....*....|....*....|....
gi 1610576541 530 -ENLLVKIgDFGMSRdvystdYYR 552
Cdd:cd14016   134 nSNKVYLI-DFGLAK------KYR 150
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
384-613 2.74e-10

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 61.99  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTL-KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14168    14 FKEVLGTGAFSEVVLAE-----ERATGKLFAVKCIpKKALKGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLnkFLRahgpdavlMAEGNPPTELTQSQMLhiaQQIAAGMVYLASQHFVHRDLATRNCLV---GENLLVKIGDF 539
Cdd:cd14168    89 LVSGGEL--FDR--------IVEKGFYTEKDASTLI---RQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDF 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610576541 540 GMSR-----DVYSTDYYRVGghtmlpirWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECITQG 613
Cdd:cd14168   156 GLSKmegkgDVMSTACGTPG--------YVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSKLFEQILKA 225
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
388-641 2.85e-10

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 62.32  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcYNlcpeQDKILVAVKTLKDASDNARKDFH------REAELLTNLQHEHIVKFYGVCVEGDPLIMVF 461
Cdd:cd05589     7 LGRGHFGKVLLAE-YK----PTGELFAIKALKKGDIIARDEVEslmcekRIFETVNSARHPFLVNLFACFQTPEHVCFVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLnkflrahgpdavlmaegnppteltqsqMLHIAQQI---------AA----GMVYLASQHFVHRDLATRNCLV 528
Cdd:cd05589    82 EYAAGGDL---------------------------MMHIHEDVfsepravfyAAcvvlGLQFLHEHKIVYRDLKLDNLLL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 529 GENLLVKIGDFGMSRD--VYSTdyyRVGGHTMLPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEV 606
Cdd:cd05589   135 DTEGYVKIADFGLCKEgmGFGD---RTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLIYEMLV-GESPFPGDDEEEV 209
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1610576541 607 IECITQGRVlQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05589   210 FDSIVNDEV-RYPRFLSTEAISIMRRLLRKNPERR 243
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
389-599 3.08e-10

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 61.86  E-value: 3.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 389 GEGAFGKVflaecyNLCPEQD-KILVAVKTLKDaSDNARKD--FHREAE--LLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd05599    10 GRGAFGEV------RLVRKKDtGHVYAMKKLRK-SEMLEKEqvAHVRAErdILAEADNPWVVKLYYSFQDEENLYLIMEF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNkflrahgpdAVLMAEGNPPTELTQsqmLHIAQQIAAgmvyLASQH---FVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd05599    83 LPGGDMM---------TLLMKKDTLTEEETR---FYIAETVLA----IESIHklgYIHRDIKPDNLLLDARGHIKLSDFG 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610576541 541 M------SRDVYST----DYyrvgghtmlpirwMPPESIMYRKFTTESDVWSLGVVLWEIFtYGKQPWY 599
Cdd:cd05599   147 LctglkkSHLAYSTvgtpDY-------------IAPEVFLQKGYGKECDWWSLGVIMYEML-IGYPPFC 201
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
387-645 3.70e-10

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 61.17  E-value: 3.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVflaecYNLCPEQDKILVAVKTL--KDASDNARKDFHREAELLTNLQHEHIVKFYG---------VCVegd 455
Cdd:cd14033     8 EIGRGSFKTV-----YRGLDTETTVEVAWCELqtRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDswkstvrghKCI--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 plIMVFEYMKHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQH--FVHRDLATRNCLV-GENL 532
Cdd:cd14033    80 --ILVTELMTSGTLKTYLKRF-------------REMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFItGPTG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFGMSRDVYSTDYYRVGGHTmlpiRWMPPEsiMY-RKFTTESDVWSLGVVLWEIFTyGKQPWYQLSN-NEVIECI 610
Cdd:cd14033   145 SVKIGDLGLATLKRASFAKSVIGTP----EFMAPE--MYeEKYDEAVDVYAFGMCILEMAT-SEYPYSECQNaAQIYRKV 217
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1610576541 611 TQGRvlqRPRTCPQ----EVYELMLGCWQREPHMRKNIK 645
Cdd:cd14033   218 TSGI---KPDSFYKvkvpELKEIIEGCIRTDKDERFTIQ 253
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
388-598 4.04e-10

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 61.20  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflAECYNLCPEQDkilVAVKTLKDASDNARKDFHREAELLTNLQ-HEHIVKFYGVCVEGDPLIMVFEYMKH 466
Cdd:cd14173    10 LGEGAYARV--QTCINLITNKE---YAVKIIEKRPGHSRSRVFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMRG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 467 GDLNKFL--RAHgpdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV---GENLLVKIGDFGM 541
Cdd:cd14173    85 GSILSHIhrRRH---------------FNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFDL 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610576541 542 SRDV-YSTDYYRVGGHTML----PIRWMPPESImyRKFTTES-------DVWSLGVVLWeIFTYGKQPW 598
Cdd:cd14173   150 GSGIkLNSDCSPISTPELLtpcgSAEYMAPEVV--EAFNEEAsiydkrcDLWSLGVILY-IMLSGYPPF 215
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
384-610 4.07e-10

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 61.06  E-value: 4.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAEcyNLCPEQdkiLVAVKTL-KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14169     7 LKEKLGEGAFSEVVLAQ--ERGSQR---LVALKCIpKKALRGKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLnkFLRahgpdavlMAEGNPPTELTQSQMLHiaqQIAAGMVYLASQHFVHRDLATRNCLVG---ENLLVKIGDF 539
Cdd:cd14169    82 LVTGGEL--FDR--------IIERGSYTEKDASQLIG---QVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDF 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 540 GMSR----DVYSTDYYRVGghtmlpirWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECI 610
Cdd:cd14169   149 GLSKieaqGMLSTACGTPG--------YVAPELLEQKPYGKAVDVWAIGVISY-ILLCGYPPFYDENDSELFNQI 214
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
407-654 4.41e-10

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 60.58  E-value: 4.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 407 EQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLraHGPDAVLmaeg 486
Cdd:cd14057    17 QGNDIVAKILKVRDVTTRISRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVL--HEGTGVV---- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 487 nppteLTQSQMLHIAQQIAAGMVYLAS-QHFVHR-DLATRNCLVGENLLVKI--GDFGMSrdvystdyYRVGGHTMLPIr 562
Cdd:cd14057    91 -----VDQSQAVKFALDIARGMAFLHTlEPLIPRhHLNSKHVMIDEDMTARInmADVKFS--------FQEPGKMYNPA- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 563 WMPPESI------MYRKfttESDVWSLGVVLWEIFTYgKQPWYQLSNNEV-IECITQG-RVLQRPRTCPQeVYELMLGCW 634
Cdd:cd14057   157 WMAPEALqkkpedINRR---SADMWSFAILLWELVTR-EVPFADLSNMEIgMKIALEGlRVTIPPGISPH-MCKLMKICM 231
                         250       260
                  ....*....|....*....|
gi 1610576541 635 QREPHMRKNIKGIHTLLQNL 654
Cdd:cd14057   232 NEDPGKRPKFDMIVPILEKM 251
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
384-588 4.71e-10

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 61.11  E-value: 4.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFgkvflAECYNLCPEQDKILVAVKTLkdasDNARKDFHREAE-LLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14091     4 IKEEIGKGSY-----SVCKRCIHKATGKEYAVKII----DKSKRDPSEEIEiLLRYGQHPNIITLRDVYDDGNSVYLVTE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDL-NKFLRahgpdavlmaEGNppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV----GENLLVKIG 537
Cdd:cd14091    75 LLRGGELlDRILR----------QKF----FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYadesGDPESLRIC 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 538 DFGMSRDVYSTDyyrvgGHTMLPI---RWMPPESIMYRKFTTESDVWSLGVVLW 588
Cdd:cd14091   141 DFGFAKQLRAEN-----GLLMTPCytaNFVAPEVLKKQGYDAACDIWSLGVLLY 189
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
382-662 4.92e-10

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 61.22  E-value: 4.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 382 IVLKRELGEGAFGKVFLAECynlcpEQDKILVAVK-TLKDASdnarkdFHREAELLTN--LQHEHIVKFYGVCVEGD--- 455
Cdd:cd14219     7 IQMVKQIGKGRYGEVWMGKW-----RGEKVAVKVFfTTEEAS------WFRETEIYQTvlMRHENILGFIAADIKGTgsw 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 -PLIMVFEYMKHGDLNKFLRAhgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHF--------VHRDLATRNC 526
Cdd:cd14219    76 tQLYLITDYHENGSLYDYLKS--------------TTLDTKAMLKLAYSSVSGLCHLHTEIFstqgkpaiAHRDLKSKNI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 527 LVGENLLVKIGDFGMS-RDVYSTDYYRVGGHTMLPI-RWMPP----ESIMYRKFTT--ESDVWSLGVVLWEI----FTYG 594
Cdd:cd14219   142 LVKKNGTCCIADLGLAvKFISDTNEVDIPPNTRVGTkRYMPPevldESLNRNHFQSyiMADMYSFGLILWEVarrcVSGG 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 595 KQPWYQLSNNEVIE------------CITQGRVLQRPR----TCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKAS 658
Cdd:cd14219   222 IVEEYQLPYHDLVPsdpsyedmreivCIKRLRPSFPNRwssdECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQ 301

                  ....
gi 1610576541 659 PVYL 662
Cdd:cd14219   302 DIKL 305
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
384-592 4.96e-10

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 61.57  E-value: 4.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFgkvflAECYNLCPEQDKILVAVKTLkdasDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14176    23 VKEDIGVGSY-----SVCKRCIHKATNMEFAVKII----DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDL-NKFLRAhgpdavlmaegNPPTELTQSQMLHiaqQIAAGMVYLASQHFVHRDLATRNCLV----GENLLVKIG 537
Cdd:cd14176    94 LMKGGELlDKILRQ-----------KFFSEREASAVLF---TITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRIC 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 538 DFGMSRDVYSTDyyrvgGHTMLPI---RWMPPESIMYRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd14176   160 DFGFAKQLRAEN-----GLLMTPCytaNFVAPEVLERQGYDAACDIWSLGVLLYTMLT 212
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
388-641 5.94e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 60.62  E-value: 5.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLCPeqdkiLVAVKTLKDASDNARKDFH---REAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYM 464
Cdd:cd05577     1 LGRGGFGEVCACQVKATGK-----MYACKKLDKKRIKKKKGETmalNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHGPDAvlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRD 544
Cdd:cd05577    76 NGGDLKYHIYNVGTRG-----------FSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 545 VYS--TDYYRVGGHTmlpirWMPPESIMY-RKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQgRVLQRPRT 621
Cdd:cd05577   145 FKGgkKIKGRVGTHG-----YMAPEVLQKeVAYDFSVDWFALGCMLYEMIA-GRSPFRQRKEKVDKEELKR-RTLEMAVE 217
                         250       260
                  ....*....|....*....|....
gi 1610576541 622 CPQ----EVYELMLGCWQREPHMR 641
Cdd:cd05577   218 YPDsfspEARSLCEGLLQKDPERR 241
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
371-598 6.00e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 61.14  E-value: 6.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 371 DTFVQHikrhnivlkRELGEGAFGKVflaecynlCPEQDKI---LVAVKTLKDASDNARKDFH---REAELLTNLQHEHI 444
Cdd:cd05632     2 NTFRQY---------RVLGKGGFGEV--------CACQVRAtgkMYACKRLEKKRIKKRKGESmalNEKQILEKVNSQFV 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 445 VKFYGVCVEGDPLIMVFEYMKHGDLnKFlraHgpdavLMAEGNPPTEltQSQMLHIAQQIAAGMVYLASQHFVHRDLATR 524
Cdd:cd05632    65 VNLAYAYETKDALCLVLTIMNGGDL-KF---H-----IYNMGNPGFE--EERALFYAAEILCGLEDLHRENTVYRDLKPE 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 525 NCLVGENLLVKIGDFGMSRDVYSTDYY--RVGghtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd05632   134 NILLDDYGHIRISDLGLAVKIPEGESIrgRVG-----TVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIE-GQSPF 203
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
373-615 6.06e-10

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 60.32  E-value: 6.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 373 FVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVavktlkdasdnarkdfhREAELLTNLQHEHIVKFYGVCV 452
Cdd:cd14110     7 FQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLVL-----------------REYQVLRRLSHPRIAQLHSAYL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 453 EGDPLIMVFEYmkhgdlnkflrAHGPDAVL-MAEGNPPTELTQSQMLhiaQQIAAGMVYLASQHFVHRDLATRNCLVGEN 531
Cdd:cd14110    70 SPRHLVLIEEL-----------CSGPELLYnLAERNSYSEAEVTDYL---WQILSAVDYLHSRRILHLDLRSENMIITEK 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 532 LLVKIGDFGmSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSNNEVIECIT 611
Cdd:cd14110   136 NLLKIVDLG-NAQPFNQGKVLMTDKKGDYVETMAPELLEGQGAGPQTDIWAIGVTAF-IMLSADYPVSSDLNWERDRNIR 213

                  ....
gi 1610576541 612 QGRV 615
Cdd:cd14110   214 KGKV 217
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
356-590 6.10e-10

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 61.58  E-value: 6.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 356 ENPQYFGItnsQLKPDTFVQhIKRHNIVlkRELGEGAFGKVflaecynlCPEQDKIL---VAVKTLKDASDNAR--KDFH 430
Cdd:cd07876     3 EDSQFYSV---QVADSTFTV-LKRYQQL--KPIGSGAQGIV--------CAAFDTVLginVAVKKLSRPFQNQThaKRAY 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 431 REAELLTNLQHEHIVKFYGVCV------EGDPLIMVFEYMkhgDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQI 504
Cdd:cd07876    69 RELVLLKCVNHKNIISLLNVFTpqksleEFQDVYLVMELM---DANLCQVIH-------------MELDHERMSYLLYQM 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 505 AAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYS---------TDYYRVgghtmlpirwmpPESIMYRKFT 575
Cdd:cd07876   133 LCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTnfmmtpyvvTRYYRA------------PEVILGMGYK 200
                         250
                  ....*....|....*
gi 1610576541 576 TESDVWSLGVVLWEI 590
Cdd:cd07876   201 ENVDIWSVGCIMGEL 215
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
379-598 6.83e-10

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 60.38  E-value: 6.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVlkRELGEGAFGKVFLaecynLCPEQDKILVAVKTLkDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLI 458
Cdd:cd14665     1 RYELV--KDIGSGNFGVARL-----MRDKQTKELVAVKYI-ERGEKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 459 MVFEYMKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL--VKI 536
Cdd:cd14665    73 IVMEYAAGGELFERICNAG-------------RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKI 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 537 GDFGMSRD--VYSTDYYRVGGHTmlpirWMPPESIMYRKFTTE-SDVWSLGVVLWeIFTYGKQPW 598
Cdd:cd14665   140 CDFGYSKSsvLHSQPKSTVGTPA-----YIAPEVLLKKEYDGKiADVWSCGVTLY-VMLVGAYPF 198
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
360-602 7.14e-10

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 61.56  E-value: 7.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 360 YFGITNSQLKPDTFVQ----------------HIKRHNIVLKRELGEGAFGKVFLAECYnlCPEQ---DKILVAVKTLKD 420
Cdd:cd05624    36 YTECSHSPLRRDKYVSeflewakpftqlvkemQLHRDDFEIIKVIGRGAFGEVAVVKMK--NTERiyaMKILNKWEMLKR 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 421 ASDNArkdFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHgpdavlmaEGNPPTELTQsqmLHI 500
Cdd:cd05624   114 AETAC---FREERNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGGDLLTLLSKF--------EDKLPEDMAR---FYI 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 501 AQQIAAgMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG----MSRDVYSTDYYRVGGHTmlpirWMPPESIMYR---- 572
Cdd:cd05624   180 GEMVLA-IHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGsclkMNDDGTVQSSVAVGTPD-----YISPEILQAMedgm 253
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1610576541 573 -KFTTESDVWSLGVVLWEIFtYGKQPWYQLS 602
Cdd:cd05624   254 gKYGPECDWWSLGVCMYEML-YGETPFYAES 283
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
388-641 7.49e-10

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 60.87  E-value: 7.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKdaSDNARKDFHREAELLTN----LQHE--HIVKFYGVCVEGDPLIMVF 461
Cdd:cd05587     4 LGKGSFGKVMLAE-----RKGTDELYAIKILK--KDVIIQDDDVECTMVEKrvlaLSGKppFLTQLHSCFQTMDRLYFVM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 462 EYMKHGDLNKFLRAHG----PDAVLMAegnppteltqsqmlhiaQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIG 537
Cdd:cd05587    77 EYVNGGDLMYHIQQVGkfkePVAVFYA-----------------AEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIA 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 538 DFGMSRDVYStdyyrvGGHTMLPIRWMP----PESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQG 613
Cdd:cd05587   140 DFGMCKEGIF------GGKTTRTFCGTPdyiaPEIIAYQPYGKSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQSIMEH 212
                         250       260
                  ....*....|....*....|....*...
gi 1610576541 614 RVlQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05587   213 NV-SYPKSLSKEAVSICKGLLTKHPAKR 239
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
377-641 8.89e-10

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 60.81  E-value: 8.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARKDFHR---EAELLTNLQHEHIVKFYGVCVE 453
Cdd:cd05594    22 VTMNDFEYLKLLGKGTFGKVILVK-----EKATGRYYAMKILKKEVIVAKDEVAHtltENRVLQNSRHPFLTALKYSFQT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMKHGDLNKFLRAhgpDAVLmaegnpptelTQSQMLHIAQQIAAGMVYL-ASQHFVHRDLATRNCLVGENL 532
Cdd:cd05594    97 HDRLCFVMEYANGGELFFHLSR---ERVF----------SEDRARFYGAEIVSALDYLhSEKNVVYRDLKLENLMLDKDG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFGMSRDVYSTdyyrvgGHTMLPI----RWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIE 608
Cdd:cd05594   164 HIKITDFGLCKEGIKD------GATMKTFcgtpEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFE 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1610576541 609 CITQGRVlQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd05594   237 LILMEEI-RFPRTLSPEAKSLLSGLLKKDPKQR 268
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
384-657 1.24e-09

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 59.83  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVFLAECYNLCPEqdkilVAVKTLKDASDNARKDFHREAELLTNLQ-HEHIVKFYGVCVEG-------- 454
Cdd:cd14036     4 IKRVIAEGGFAFVYEAQDVGTGKE-----YALKRLLSNEEEKNKAIIQEINFMKKLSgHPNIVQFCSAASIGkeesdqgq 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKhGDLNKFLRahgpdavlmaEGNPPTELTQSQMLHIAQQIAAGMVYLASQH--FVHRDLATRNCLVGENL 532
Cdd:cd14036    79 AEYLLLTELCK-GQLVDFVK----------KVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 LVKIGDFG-MSRDVYSTDY-YRVGGHTML---------PIrWMPPESI-MYRKF--TTESDVWSLGVVLWeIFTYGKQPW 598
Cdd:cd14036   148 QIKLCDFGsATTEAHYPDYsWSAQKRSLVedeitrnttPM-YRTPEMIdLYSNYpiGEKQDIWALGCILY-LLCFRKHPF 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 599 yqlsnneviECITQGRVLQRPRTCPQE------VYELMLGCWQREPHMRKNIKGIHTLLQNLAKA 657
Cdd:cd14036   226 ---------EDGAKLRIINAKYTIPPNdtqytvFHDLIRSTLKVNPEERLSITEIVEQLQELAAA 281
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
386-592 1.40e-09

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 59.90  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLaeCYNLcpeQDKILVAVKTLKDASD--NARKDfhrEAELL--------TNLQHEHIVKFYG------ 449
Cdd:cd14136    16 RKLGWGHFSTVWL--CWDL---QNKRFVALKVVKSAQHytEAALD---EIKLLkcvreadpKDPGREHVVQLLDdfkhtg 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 450 -----VCvegdpliMVFEYMKHgDLNKFLRAHGPDAVlmaegnpPTELTQSqmlhIAQQIAAGMVYLASQ-HFVHRDLAT 523
Cdd:cd14136    88 pngthVC-------MVFEVLGP-NLLKLIKRYNYRGI-------PLPLVKK----IARQVLQGLDYLHTKcGIIHTDIKP 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 524 RNCLVGENLL-VKIGDFGMSRDVY-------STDYYRVgghtmlpirwmpPESIMYRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd14136   149 ENVLLCISKIeVKIADLGNACWTDkhftediQTRQYRS------------PEVILGAGYGTPADIWSTACMAFELAT 213
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
384-591 1.41e-09

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 59.64  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFgkvflAECYNLCPEQDKILVAVKTLkdasDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14178     7 IKEDIGIGSY-----SVCKRCVHKATSTEYAVKII----DKSKRDPSEEIEILLRYgQHPNIITLKDVYDDGKFVYLVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDL-NKFLRAHGpdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCL----VGENLLVKIG 537
Cdd:cd14178    78 LMRGGELlDRILRQKC--------------FSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILymdeSGNPESIRIC 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 538 DFGMSRDVYSTDyyrvgGHTMLPI---RWMPPESIMYRKFTTESDVWSLGVVLWEIF 591
Cdd:cd14178   144 DFGFAKQLRAEN-----GLLMTPCytaNFVAPEVLKRQGYDAACDIWSLGILLYTML 195
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
49-127 1.49e-09

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 55.09  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  49 NLTVEEGKSITLSCSVAGDPVPNMYW-DVGNLVSKHMNETSHTQGSLRITNISSDDSGKQIsCVAENLVGEDQDSVNLTV 127
Cdd:cd20978    10 NVVVKGGQDVTLPCQVTGVPQPKITWlHNGKPLQGPMERATVEDGTLTIINVQPEDTGYYG-CVATNEIGDIYTETLLHV 88
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
391-590 1.50e-09

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 59.67  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 391 GAFGKVFLAECYNlcpeqDKILVAVKTLKDasdnaRKDFHREAEL--LTNLQHEHIVKFYGVCVEGD----PLIMVFEYM 464
Cdd:cd14141     6 GRFGCVWKAQLLN-----EYVAVKIFPIQD-----KLSWQNEYEIysLPGMKHENILQFIGAEKRGTnldvDLWLITAFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQ----------HFVHRDLATRNCLVGENLLV 534
Cdd:cd14141    76 EKGSLTDYLKAN--------------VVSWNELCHIAQTMARGLAYLHEDipglkdghkpAIAHRDIKSKNVLLKNNLTA 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 535 KIGDFGMSRDVYSTdyyRVGGHTMLPI---RWMPPESI-----MYRKFTTESDVWSLGVVLWEI 590
Cdd:cd14141   142 CIADFGLALKFEAG---KSAGDTHGQVgtrRYMAPEVLegainFQRDAFLRIDMYAMGLVLWEL 202
IgI_4_MYLK-like cd20976
Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a ...
41-127 1.65e-09

Fourth Ig-like domain from smooth muscle myosin light chain kinase and similar domains ; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain from smooth muscle myosin light chain kinase (MYLK) and similar domains. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of this group shows that the fourth Ig-like domain from myosin light chain kinase lacks this strand and thus belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409568 [Multi-domain]  Cd Length: 90  Bit Score: 54.95  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  41 PSANLAAPNLTVEEGKSITLSCSVAGDPVPNMYWdvgNLVSKHMN-ETSHTQ-----GSLRITNISSDDSGkQISCVAEN 114
Cdd:cd20976     2 PSFSSVPKDLEAVEGQDFVAQCSARGKPVPRITW---IRNAQPLQyAADRSTceagvGELHIQDVLPEDHG-TYTCLAKN 77
                          90
                  ....*....|...
gi 1610576541 115 LVGEDQDSVNLTV 127
Cdd:cd20976    78 AAGQVSCSAWVTV 90
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
386-597 1.85e-09

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 59.29  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVflaecynlCPEQDKI---LVAVKTLKDASDNARKDFH---REAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd05605     6 RVLGKGGFGEV--------CACQVRAtgkMYACKKLEKKRIKKRKGEAmalNEKQILEKVNSRFVVSLAYAYETKDALCL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLnKFlraHgpdavLMAEGNPptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd05605    78 VLTIMNGGDL-KF---H-----IYNMGNP--GFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDL 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMSRDVYSTDYY--RVGghtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQP 597
Cdd:cd05605   147 GLAVEIPEGETIrgRVG-----TVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIE-GQAP 200
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
369-614 1.98e-09

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 58.68  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 369 KPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVavktlkdasdnarkdfhREAELLTNLQHEHIVKFY 448
Cdd:cd14111     3 KPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVL-----------------QEYEILKSLHHERIMALH 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 449 GVCVEGDPLIMVFEY-----MKHGDLNKFlRAHGPDAVlmaegnppteltqSQMLHIAQqiaaGMVYLASQHFVHRDLAT 523
Cdd:cd14111    66 EAYITPRYLVLIAEFcsgkeLLHSLIDRF-RYSEDDVV-------------GYLVQILQ----GLEYLHGRRVLHLDIKP 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 524 RNCLVGENLLVKIGDFGmSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWYQLSN 603
Cdd:cd14111   128 DNIMVTNLNAIKIVDFG-SAQSFNPLSLRQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTY-IMLSGRSPFEDQDP 205
                         250
                  ....*....|.
gi 1610576541 604 NEVIECITQGR 614
Cdd:cd14111   206 QETEAKILVAK 216
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
386-619 2.00e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 60.03  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAecynlCPEQDKILVAVKTLKDASD-NARKDFHREAE--LLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd05626     7 KTLGIGAFGEVCLA-----CKVDTHALYAMKTLRKKDVlNRNQVAHVKAErdILAEADNEWVVKLYYSFQDKDNLYFVMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNkflrahgpdAVLMAEGNPPTELTQsqmLHIAQQIAAgmvyLASQH---FVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd05626    82 YIPGGDMM---------SLLIRMEVFPEVLAR---FYIAELTLA----IESVHkmgFIHRDIKPDNILIDLDGHIKLTDF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMS---RDVYSTDYYRVGGH----TMLPI--------------------------------------RWMPPESIMYRKF 574
Cdd:cd05626   146 GLCtgfRWTHNSKYYQKGSHirqdSMEPSdlwddvsncrcgdrlktleqratkqhqrclahslvgtpNYIAPEVLLRKGY 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1610576541 575 TTESDVWSLGVVLWEIFTyGKQPWYQLSNNEV-IECITQGRVLQRP 619
Cdd:cd05626   226 TQLCDWWSVGVILFEMLV-GQPPFLAPTPTETqLKVINWENTLHIP 270
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
378-612 2.06e-09

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 58.79  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 378 KRHNIVLKRELGEGAFGKVflAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPL 457
Cdd:cd14197     7 ERYSLSPGRELGRGKFAVV--RKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAQANPWVINLHEVYETASEM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLNKFLRAHGPDAvlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV-GENLL--V 534
Cdd:cd14197    85 ILVLEYAAGGEIFNQCVADREEA-----------FKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLtSESPLgdI 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610576541 535 KIGDFGMSRDVYSTDYYRvggHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQ 612
Cdd:cd14197   154 KIVDFGLSRILKNSEELR---EIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLT-GISPFLGDDKQETFLNISQ 227
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
388-591 2.14e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 59.72  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflAECYNlcpEQDKILVAVKTLKDASDNARKDfHREAELLTNLQHEH-----IVKFYGVCVEGDPLIMVFE 462
Cdd:cd14228    23 LGRGTFGQV--AKCWK---RSTKEIVAIKILKNHPSYARQG-QIEVSILSRLSSENadeynFVRSYECFQHKNHTCLVFE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHgDLNKFLRAhgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCL----VGENLLVKIGD 538
Cdd:cd14228    97 MLEQ-NLYDFLKQ-----------NKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMlvdpVRQPYRVKVID 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 539 FG----MSRDVYST----DYYRVgghtmlpirwmpPESIMYRKFTTESDVWSLGVVLWEIF 591
Cdd:cd14228   165 FGsashVSKAVCSTylqsRYYRA------------PEIILGLPFCEAIDMWSLGCVIAELF 213
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
388-591 2.26e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 59.27  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflAECYNlcpEQDKILVAVKTLKDASDNARKDfHREAELLTNLQHEH-----IVKFYGVCVEGDPLIMVFE 462
Cdd:cd14229     8 LGRGTFGQV--VKCWK---RGTNEIVAVKILKNHPSYARQG-QIEVGILARLSNENadefnFVRAYECFQHRNHTCLVFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHgDLNKFLRAhgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCL----VGENLLVKIGD 538
Cdd:cd14229    82 MLEQ-NLYDFLKQ-----------NKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMlvdpVRQPYRVKVID 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 539 FG----MSRDVYST----DYYRVgghtmlpirwmpPESIMYRKFTTESDVWSLGVVLWEIF 591
Cdd:cd14229   150 FGsashVSKTVCSTylqsRYYRA------------PEIILGLPFCEAIDMWSLGCVIAELF 198
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
387-621 2.56e-09

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 59.66  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLAEcynlcpEQD-KILVAVKTLKDASDNARKDFHR---EAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd05600    18 QVGQGGYGSVFLAR------KKDtGEICALKIMKKKVLFKLNEVNHvltERDILTTTNSPWLVKLLYAFQDPENVYLAME 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNKFLRAHGpdaVLMAEgnppteltqSQMLHIAQQIAAgmvyLASQH---FVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd05600    92 YVPGGDFRTLLNNSG---ILSEE---------HARFYIAEMFAA----ISSLHqlgYIHRDLKPENFLIDSSGHIKLTDF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMSR----------------------DVYSTDYYRVGG-HTML-------------PiRWMPPESIMYRKFTTESDVWSL 583
Cdd:cd05600   156 GLASgtlspkkiesmkirleevkntaFLELTAKERRNIyRAMRkedqnyansvvgsP-DYMAPEVLRGEGYDLTVDYWSL 234
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1610576541 584 GVVLWEIFTyGKQPWYQLSNNEVIECITQGR-VLQRPRT 621
Cdd:cd05600   235 GCILFECLV-GFPPFSGSTPNETWANLYHWKkTLQRPVY 272
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
388-591 3.14e-09

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 58.80  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFlaECYNLcpeQDKILVAVKTLKdasdNARKDFHR---EAELLTNLQ-------HEHIVKFYGVCVEGDPL 457
Cdd:cd14212     7 LGQGTFGQVV--KCQDL---KTNKLVAVKVLK----NKPAYFRQamlEIAILTLLNtkydpedKHHIVRLLDHFMHHGHL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFE--------YMKhgdLNKFlraHGpdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVG 529
Cdd:cd14212    78 CIVFEllgvnlyeLLK---QNQF---RG--------------LSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLV 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 530 ENLL--VKIGDFGMS----RDVYS---TDYYRvgghtmlpirwmPPESIMYRKFTTESDVWSLGVVLWEIF 591
Cdd:cd14212   138 NLDSpeIKLIDFGSAcfenYTLYTyiqSRFYR------------SPEVLLGLPYSTAIDMWSLGCIAAELF 196
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
426-597 4.21e-09

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 58.52  E-value: 4.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 426 RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLnkflrahgpDAVLMAEGNPPTELtqsqMLHIAQQIA 505
Cdd:cd06649    47 RNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSL---------DQVLKEAKRIPEEI----LGKVSIAVL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 506 AGMVYLASQH-FVHRDLATRNCLVGENLLVKIGDFGMSRD-VYSTDYYRVGGHTmlpirWMPPESIMYRKFTTESDVWSL 583
Cdd:cd06649   114 RGLAYLREKHqIMHRDVKPSNILVNSRGEIKLCDFGVSGQlIDSMANSFVGTRS-----YMSPERLQGTHYSVQSDIWSM 188
                         170
                  ....*....|....
gi 1610576541 584 GVVLWEIfTYGKQP 597
Cdd:cd06649   189 GLSLVEL-AIGRYP 201
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
387-652 4.83e-09

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 58.14  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVflaecYNLCPEQDKILVAVKTLKDA--SDNARKDFHREAELLTNLQHEHIVKFYG---VCVEGDP-LIMV 460
Cdd:cd14030    32 EIGRGSFKTV-----YKGLDTETTVEVAWCELQDRklSKSERQRFKEEAGMLKGLQHPNIVRFYDsweSTVKGKKcIVLV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHI-AQQIAAGMVYLASQH--FVHRDLATRNCLV-GENLLVKI 536
Cdd:cd14030   107 TELMTSGTLKTYLKRF--------------KVMKIKVLRSwCRQILKGLQFLHTRTppIIHRDLKCDNIFItGPTGSVKI 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 537 GDFGMSRDVYSTDYYRVGGHTmlpiRWMPPEsiMYRKFTTES-DVWSLGVVLWEIFTyGKQPWYQLSN-NEVIECITQG- 613
Cdd:cd14030   173 GDLGLATLKRASFAKSVIGTP----EFMAPE--MYEEKYDESvDVYAFGMCMLEMAT-SEYPYSECQNaAQIYRRVTSGv 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1610576541 614 RVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGI--HTLLQ 652
Cdd:cd14030   246 KPASFDKVAIPEVKEIIEGCIRQNKDERYAIKDLlnHAFFQ 286
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
387-603 5.75e-09

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 57.39  E-value: 5.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFLA---ECY---NLCPEQDKILVAVKtlkdasdnaRKDFHREAELLTNLQHEHIVKFYGV---CVEGDP- 456
Cdd:cd14032     8 ELGRGSFKTVYKGldtETWvevAWCELQDRKLTKVE---------RQRFKEEAEMLKGLQHPNIVRFYDFwesCAKGKRc 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLRAHgpdavlmaegnpptELTQSQMLHI-AQQIAAGMVYLASQH--FVHRDLATRNCLV-GENL 532
Cdd:cd14032    79 IVLVTELMTSGTLKTYLKRF--------------KVMKPKVLRSwCRQILKGLLFLHTRTppIIHRDLKCDNIFItGPTG 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 533 LVKIGDFGMSRDVYSTDYYRVGGHTmlpiRWMPPEsiMYRKFTTES-DVWSLGVVLWEIFTyGKQPWYQLSN 603
Cdd:cd14032   145 SVKIGDLGLATLKRASFAKSVIGTP----EFMAPE--MYEEHYDESvDVYAFGMCMLEMAT-SEYPYSECQN 209
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
388-598 5.93e-09

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 57.66  E-value: 5.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGV------CVEGDPLIMV 460
Cdd:cd14038     2 LGTGGFGNVLRWI-----NQETGEQVAIKQCRqELSPKNRERWCLEIQIMKRLNHPNVVAARDVpeglqkLAPNDLPLLA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHgPDAVLMAEGnppteltqsQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV--GENLLV-KIG 537
Cdd:cd14038    77 MEYCQGGDLRKYLNQF-ENCCGLREG---------AILTLLSDISSALRYLHENRIIHRDLKPENIVLqqGEQRLIhKII 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 538 DFGMSRDVystDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd14038   147 DLGYAKEL---DQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPF 203
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
390-592 6.13e-09

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 57.54  E-value: 6.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 390 EGAFGKVFLAEcynlcpeQDKILVAVKTLKDASDNARKD----FHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd14157     3 EGTFADIYKGY-------RHGKQYVIKRLKETECESPKSterfFQTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHGpdavlmaeGNPPteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSrdV 545
Cdd:cd14157    76 NGSLQDRLQQQG--------GSHP--LPWEQRLSISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSGLR--L 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 546 YSTDYYRVggHTMLPIR-------WMPPESIMYRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd14157   144 CPVDKKSV--YTMMKTKvlqislaYLPEDFVRHGQLTEKVDIFSCGVVLAEILT 195
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
386-598 7.87e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 57.31  E-value: 7.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVflaecynlCPEQDKI---LVAVKTLKDASDNARKDFH---REAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd05631     6 RVLGKGGFGEV--------CACQVRAtgkMYACKKLEKKRIKKRKGEAmalNEKRILEKVNSRFVVSLAYAYETKDALCL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLnKFlraHgpdavLMAEGNPPTEltQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd05631    78 VLTIMNGGDL-KF---H-----IYNMGNPGFD--EQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDL 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 540 GMSRDVYSTDYYR--VGghtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd05631   147 GLAVQIPEGETVRgrVG-----TVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQ-GQSPF 201
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
388-591 8.19e-09

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 57.84  E-value: 8.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflAECYNlcpEQDKILVAVKTLKDASDNARKDfHREAELLTNLQHE-----HIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14211     7 LGRGTFGQV--VKCWK---RGTNEIVAIKILKNHPSYARQG-QIEVSILSRLSQEnadefNFVRAYECFQHKNHTCLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 yMKHGDLNKFLRAhgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCL----VGENLLVKIGD 538
Cdd:cd14211    81 -MLEQNLYDFLKQ-----------NKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMlvdpVRQPYRVKVID 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 539 FG----MSRDVYST----DYYRVgghtmlpirwmpPESIMYRKFTTESDVWSLGVVLWEIF 591
Cdd:cd14211   149 FGsashVSKAVCSTylqsRYYRA------------PEIILGLPFCEAIDMWSLGCVIAELF 197
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
388-615 8.26e-09

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 56.89  E-value: 8.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflAECYNLCPEQDkilVAVKTLKDASDNARKDFHrEAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHG 467
Cdd:cd14115     1 IGRGRFSIV--KKCLHKATRKD---VAVKFVSKKMKKKEQAAH-EAALLQHLQHPQYITLHDTYESPTSYILVLELMDDG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 468 DLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL---LVKIGDFGMSrd 544
Cdd:cd14115    75 RLLDYLMNH-------------DELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDA-- 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 545 VYSTDYYRVggHTML--PiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVieCITQGRV 615
Cdd:cd14115   140 VQISGHRHV--HHLLgnP-EFAAPEVIQGTPVSLATDIWSIGVLTYVMLS-GVSPFLDESKEET--CINVCRV 206
LRRCT_2 pfam16920
Leucine rich repeat C-terminal motif; This entry represents the Leucine Rich Repeat C-terminal ...
1-39 8.81e-09

Leucine rich repeat C-terminal motif; This entry represents the Leucine Rich Repeat C-terminal (LRRCT) capping motif from TRK receptors.


Pssm-ID: 465313  Cd Length: 45  Bit Score: 51.49  E-value: 8.81e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1610576541   1 MWIKTLQEAKSS-PDTQDLYCLNESSKnIPLANLQIPNCG 39
Cdd:pfam16920   7 RWLQLWQEEGLAgLGTQQLYCLNDGSK-IPLQSMNIPNCG 45
IgI_5_Robo cd20952
Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the ...
49-127 1.06e-08

Fifth Ig-like domain of Roundabout (Robo) homolog 1/2, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fifth Ig-like domain of Roundabout (Robo) homolog 1/2 and similar domains. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, -2, and -3), and three mammalian Slit homologs (Slit-1,-2, -3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, -2, and -3 are expressed by commissural neurons in the vertebrate spinal cord and Slits 1, -2, -3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of slit responsiveness, antagonizes slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be is the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. The fifth Ig-like domain of Robo 1 and 2 is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors


Pssm-ID: 409544 [Multi-domain]  Cd Length: 87  Bit Score: 52.88  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  49 NLTVEEGKSITLSCSVAGDPVPNMYW--DVGNLVSKHMNETSHTQGSLRITNISSDDSGKqISCVAENLVGEDQDSVNLT 126
Cdd:cd20952     8 NQTVAVGGTVVLNCQATGEPVPTISWlkDGVPLLGKDERITTLENGSLQIKGAEKSDTGE-YTCVALNLSGEATWSAVLD 86

                  .
gi 1610576541 127 V 127
Cdd:cd20952    87 V 87
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
502-647 1.10e-08

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 56.50  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 502 QQIAAGMVYLASQHFVHRDLATRNCLV----GENLLVKIGDFGMSRDVYSTDY--YRVgghtmlpirWMPPESIMYRKFT 575
Cdd:cd14102   112 RQVLEAVRHCYSCGVVHRDIKDENLLVdlrtGELKLIDFGSGALLKDTVYTDFdgTRV---------YSPPEWIRYHRYH 182
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 576 TES-DVWSLGVVLWEIfTYGKQPWYQlsnnevIECITQGRVLQRPRTCPqEVYELMLGCWQREPHMRKNIKGI 647
Cdd:cd14102   183 GRSaTVWSLGVLLYDM-VCGDIPFEQ------DEEILRGRLYFRRRVSP-ECQQLIKWCLSLRPSDRPTLEQI 247
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
432-615 1.14e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 57.98  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 432 EAELLTNLQHEHIVKFYGV-CVEGDPLIMVFEYmkHGDLNKFLrahgpdavlmaeGNPPTELTQSQMLHIAQQIAAGMVY 510
Cdd:PHA03211  210 EARLLRRLSHPAVLALLDVrVVGGLTCLVLPKY--RSDLYTYL------------GARLRPLGLAQVTAVARQLLSAIDY 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 511 LASQHFVHRDLATRNCLVGENLLVKIGDFG---MSRDVYSTD-YYRVGGhtmlPIRWMPPESIMYRKFTTESDVWSLGVV 586
Cdd:PHA03211  276 IHGEGIIHRDIKTENVLVNGPEDICLGDFGaacFARGSWSTPfHYGIAG----TVDTNAPEVLAGDPYTPSVDIWSAGLV 351
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1610576541 587 LWE-------IFTYGKQPWYQLSNNEVIECITQGRV 615
Cdd:PHA03211  352 IFEaavhtasLFSASRGDERRPYDAQILRIIRQAQV 387
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
377-602 1.24e-08

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 57.72  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVFLAECYNlcpeQDKILvAVKTLKDASDNARKD---FHREAELLTNLQHEHIVKFYGVCVE 453
Cdd:cd05623    69 LHKEDFEILKVIGRGAFGEVAVVKLKN----ADKVF-AMKILNKWEMLKRAEtacFREERDVLVNGDSQWITTLHYAFQD 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMKHGDLNKFLRAHgpdavlmaEGNPPTELTQsqmLHIAQQIAAgMVYLASQHFVHRDLATRNCLVGENLL 533
Cdd:cd05623   144 DNNLYLVMDYYVGGDLLTLLSKF--------EDRLPEDMAR---FYLAEMVLA-IDSVHQLHYVHRDIKPDNILMDMNGH 211
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 534 VKIGDFGMSRDVYSTDYYRVGGHTMLPiRWMPPESIMYR-----KFTTESDVWSLGVVLWEIFtYGKQPWYQLS 602
Cdd:cd05623   212 IRLADFGSCLKLMEDGTVQSSVAVGTP-DYISPEILQAMedgkgKYGPECDWWSLGVCMYEML-YGETPFYAES 283
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
383-592 1.27e-08

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 57.19  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFlaECYNlcpEQDKILVAVKTLKDASDnARKDFHREAELLTNLQHE------HIVKFYG------- 449
Cdd:cd14134    15 KILRLLGEGTFGKVL--ECWD---RKRKRYVAVKIIRNVEK-YREAAKIEIDVLETLAEKdpngksHCVQLRDwfdyrgh 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 450 VCvegdpliMVFEymKHG-DLNKFLRAH--GPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNC 526
Cdd:cd14134    89 MC-------IVFE--LLGpSLYDFLKKNnyGP-------------FPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 527 L-------------------VGENLLVKIGDFG------MSR-DVYSTDYYRvgghtmlpirwmPPESIMYRKFTTESDV 580
Cdd:cd14134   147 LlvdsdyvkvynpkkkrqirVPKSTDIKLIDFGsatfddEYHsSIVSTRHYR------------APEVILGLGWSYPCDV 214
                         250
                  ....*....|..
gi 1610576541 581 WSLGVVLWEIFT 592
Cdd:cd14134   215 WSIGCILVELYT 226
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
384-604 1.44e-08

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 56.56  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFgkvflAECYNLCPEQDKILVAVKTLkdasDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14177     8 LKEDIGVGSY-----SVCKRCIHRATNMEFAVKII----DKSKRDPSEEIEILMRYgQHPNIITLKDVYDDGRYVYLVTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDL-NKFLRAhgpdavlmaegNPPTELTQSQMLHIaqqIAAGMVYLASQHFVHRDLATRNCLV----GENLLVKIG 537
Cdd:cd14177    79 LMKGGELlDRILRQ-----------KFFSEREASAVLYT---ITKTVDYLHCQGVVHRDLKPSNILYmddsANADSIRIC 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 538 DFGMSRDVYSTDyyrvgGHTMLPI---RWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNN 604
Cdd:cd14177   145 DFGFAKQLRGEN-----GLLLTPCytaNFVAPEVLMRQGYDAACDIWSLGVLLYTMLA-GYTPFANGPND 208
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
363-599 1.63e-08

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 57.00  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 363 ITNSQLKPDTFvQHIKRhnivlkreLGEGAFGKVFLA------ECYNLcpeqdKILVAVKTLKdASDNARkdFHREAELL 436
Cdd:cd05596    18 ITKLRMNAEDF-DVIKV--------IGRGAFGEVQLVrhkstkKVYAM-----KLLSKFEMIK-RSDSAF--FWEERDIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 437 TNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLnkflrahgpdAVLMAEGNPPTELTQsqmLHIAQQIAAgMVYLASQHF 516
Cdd:cd05596    81 AHANSEWIVQLHYAFQDDKYLYMVMDYMPGGDL----------VNLMSNYDVPEKWAR---FYTAEVVLA-LDAIHSMGF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 517 VHRDLATRNCLVGENLLVKIGDFG----MSRD--------VYSTDYyrvgghtmlpirwMPPESIMYR----KFTTESDV 580
Cdd:cd05596   147 VHRDVKPDNMLLDASGHLKLADFGtcmkMDKDglvrsdtaVGTPDY-------------ISPEVLKSQggdgVYGRECDW 213
                         250
                  ....*....|....*....
gi 1610576541 581 WSLGVVLWEIFtYGKQPWY 599
Cdd:cd05596   214 WSVGVFLYEML-VGDTPFY 231
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
386-588 1.74e-08

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 55.93  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASdnaRKDFHREAELLTN--LQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd14662     6 KDIGSGNFGVARLMR-----NKETKELVAVKYIERGL---KIDENVQREIINHrsLRHPNIIRFKEVVLTPTHLAIVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL--VKIGDFGM 541
Cdd:cd14662    78 AAGGELFERICNAG-------------RFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGY 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1610576541 542 SRD--VYSTDYYRVGGHTmlpirWMPPESIMYRKFTTE-SDVWSLGVVLW 588
Cdd:cd14662   145 SKSsvLHSQPKSTVGTPA-----YIAPEVLSRKEYDGKvADVWSCGVTLY 189
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
387-605 1.90e-08

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 55.75  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVflaecyNLCPEQ-DKILVAVKTLkDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd14113    14 ELGRGRFSVV------KKCDQRgTKRAVATKFV-NKKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMAD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL---LVKIGDFGMS 542
Cdd:cd14113    87 QGRLLDYVVRWG-------------NLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLskpTIKLADFGDA 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 543 RDVYSTDYYrvggHTML-PIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNE 605
Cdd:cd14113   154 VQLNTTYYI----HQLLgSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLS-GVSPFLDESVEE 212
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
386-598 1.95e-08

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 56.98  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDAS---DNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd05625     7 KTLGIGAFGEVCLAR-----KVDTKALYATKTLRKKDvllRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHGDLNkflrahgpdAVLMAEGNPPTELTQsqmLHIAQqIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 542
Cdd:cd05625    82 YIPGGDMM---------SLLIRMGVFPEDLAR---FYIAE-LTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLC 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 ---RDVYSTDYYRVGGH----------------------TMLPIRW--------------------MPPESIMYRKFTTE 577
Cdd:cd05625   149 tgfRWTHDSKYYQSGDHlrqdsmdfsnewgdpencrcgdRLKPLERraarqhqrclahslvgtpnyIAPEVLLRTGYTQL 228
                         250       260
                  ....*....|....*....|.
gi 1610576541 578 SDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd05625   229 CDWWSVGVILFEMLV-GQPPF 248
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
386-588 2.14e-08

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 55.77  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVflAECYNLCPEQDKILVAVKtlKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 465
Cdd:cd14183    12 RTIGDGNFAVV--KECVERSTGREYALKIIN--KSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNkflrahgpDAVLMAegNPPTELTQSQMLHiaqQIAAGMVYLASQHFVHRDLATRNCLVGENL----LVKIGDFGM 541
Cdd:cd14183    88 GGDLF--------DAITST--NKYTERDASGMLY---NLASAIKYLHSLNIVHRDIKPENLLVYEHQdgskSLKLGDFGL 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1610576541 542 SRDVYSTDYYRVGGHTmlpirWMPPESIMYRKFTTESDVWSLGVVLW 588
Cdd:cd14183   155 ATVVDGPLYTVCGTPT-----YVAPEIIAETGYGLKVDIWAAGVITY 196
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
388-641 2.34e-08

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 56.17  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNlcpeqDKILVAVKTLKDASDNARKDF-HREAE---LLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd05575     3 IGKGSFGKVLLARHKA-----EGKLYAVKVLQKKAILKRNEVkHIMAErnvLLKNVKHPFLVGLHYSFQTKDKLYFVLDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLnkFLraHgpdavLMAEgnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR 543
Cdd:cd05575    78 VNGGEL--FF--H-----LQRE----RHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 544 -DVYSTDYYRVGGHTmlPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFtYGKQPWYQLSNNEVIECITQgRVLQRPRTC 622
Cdd:cd05575   145 eGIEPSDTTSTFCGT--P-EYLAPEVLRKQPYDRTVDWWCLGAVLYEML-YGLPPFYSRDTAEMYDNILH-KPLRLRTNV 219
                         250
                  ....*....|....*....
gi 1610576541 623 PQEVYELMLGCWQREPHMR 641
Cdd:cd05575   220 SPSARDLLEGLLQKDRTKR 238
IgI_SALM5_like cd05764
Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; ...
48-127 2.58e-08

Immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins; member of the I-set of IgSF domains; This group contains the immunoglobulin domain of human Synaptic Adhesion-Like Molecule 5 (SALM5) and similar proteins. The SALM (for synaptic adhesion-like molecules; also known as Lrfn for leucine-rich repeat and fibronectin type III domain containing) family of adhesion molecules consists of five known members: SALM1/Lrfn2, SALM2/Lrfn1, SALM3/Lrfn4, SALM4/Lrfn3, and SALM5/Lrfn5. SALMs share a similar domain structure, containing leucine-rich repeats (LRRs), an immunoglobulin (Ig) domain, and a fibronectin III (FNIII) domain, followed by a transmembrane domain and a C-terminal PDZ-binding motif. SALM5 is implicated in autism spectrum disorders (ASDs) and schizophrenia, induces presynaptic differentiation in contacting axons. SALM5 interacts with the Ig domains of LAR (Leukocyte common Antigen-Related) family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTPsigma). In addition, PTPdelta is implicated in ASDs, ADHD, bipolar disorder, and restless leg syndrome. Studies have shown that LAR-RPTPs are novel and splicing-dependent presynaptic ligands for SALM5, and that they mediate SALM5-dependent presynaptic differentiation. Furthermore, SALM5 maintains AMPA receptor (AMPAR)-mediated excitatory synaptic transmission through mechanisms involving the interaction of SALM5 with LAR-RPTPs. This group belongs to the I-set of immunoglobulin superfamily (IgSF) domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409421 [Multi-domain]  Cd Length: 88  Bit Score: 51.71  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  48 PNLTVEEGKSITLSCSVAGDPVPNMYWDV--GNLVSKHMNETSHTQGSLRITNISSDDSGkQISCVAENLVGEDQDSVNL 125
Cdd:cd05764     8 HELRVLEGQRATLRCKARGDPEPAIHWISpeGKLISNSSRTLVYDNGTLDILITTVKDTG-AFTCIASNPAGEATARVEL 86

                  ..
gi 1610576541 126 TV 127
Cdd:cd05764    87 HI 88
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
381-636 2.65e-08

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 55.78  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 381 NIVLKRELGEGAFGKVFLAEcyNLCPEQDKILVAVKTLKDAS--DNARKDFHR--EAELLTNL-QHEHIVKFYGVCVEGD 455
Cdd:cd05613     1 NFELLKVLGTGAYGKVFLVR--KVSGHDAGKLYAMKVLKKATivQKAKTAEHTrtERQVLEHIrQSPFLVTLHYAFQTDT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLNkflrahgpdavlmaegnppTELTQSQMLHIAQ-QIAAGMVYLASQHF-----VHRDLATRNCLVG 529
Cdd:cd05613    79 KLHLILDYINGGELF-------------------THLSQRERFTENEvQIYIGEIVLALEHLhklgiIYRDIKLENILLD 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 530 ENLLVKIGDFGMSRDVYSTDY---YRVGGhtmlPIRWMPPESIMYRKFTTES--DVWSLGVVLWEIFTyGKQPWYQLSNN 604
Cdd:cd05613   140 SSGHVVLTDFGLSKEFLLDENeraYSFCG----TIEYMAPEIVRGGDSGHDKavDWWSLGVLMYELLT-GASPFTVDGEK 214
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1610576541 605 EVIECITQgRVLQRPRTCPQEVYELMLGCWQR 636
Cdd:cd05613   215 NSQAEISR-RILKSEPPYPQEMSALAKDIIQR 245
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
383-592 3.09e-08

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 56.04  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFLAECYNlcpeqDKILVAVKTLKDA---SDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd05610     7 VIVKPISRGAFGKVYLGRKKN-----NSKLYAVKVVKKAdmiNKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHGPDAVLMAegnppteltqsqMLHIAQqIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd05610    82 VMEYLIGGDVKSLLHIYGYFDEEMA------------VKYISE-VALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 540 GMSR----------DVYST--------DYYRVGGH-----------TMLPIR----------------------WMPPES 568
Cdd:cd05610   149 GLSKvtlnrelnmmDILTTpsmakpknDYSRTPGQvlslisslgfnTPTPYRtpksvrrgaarvegerilgtpdYLAPEL 228
                         250       260
                  ....*....|....*....|....
gi 1610576541 569 IMYRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd05610   229 LLGKPHGPAVDWWALGVCLFEFLT 252
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
432-603 3.41e-08

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 55.04  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 432 EAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNkflrahgpDAVlmAEGNPPTELTQSQMLHiaqQIAAGMVYL 511
Cdd:cd14184    49 EVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGGDLF--------DAI--TSSTKYTERDASAMVY---NLASALKYL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 512 ASQHFVHRDLATRNCLVGE----NLLVKIGDFGMSRDVYSTDYYRVGGHTmlpirWMPPESIMYRKFTTESDVWSLGVVL 587
Cdd:cd14184   116 HGLCIVHRDIKPENLLVCEypdgTKSLKLGDFGLATVVEGPLYTVCGTPT-----YVAPEIIAETGYGLKVDIWAAGVIT 190
                         170
                  ....*....|....*.
gi 1610576541 588 WeIFTYGKQPWYQLSN 603
Cdd:cd14184   191 Y-ILLCGFPPFRSENN 205
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
386-592 3.82e-08

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 54.91  E-value: 3.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGkvFLAECYNLCPEQD--KILVAVKTLKDASdnARkdfhREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd14108     8 KEIGRGAFS--YLRRVKEKSSDLSfaAKFIPVRAKKKTS--AR----RELALLAELDHKSIVRFHDAFEKRRVVIIVTEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAhgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV--GENLLVKIGDFGM 541
Cdd:cd14108    80 CHEELLERITKR--------------PTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGN 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 542 SRDVYSTD--YYRVGghtmLPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd14108   146 AQELTPNEpqYCKYG----TP-EFVAPEIVNQSPVSKVTDIWPVGVIAYLCLT 193
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
377-615 5.06e-08

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 54.66  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 377 IKRHNIVLKRELGEGAFGKVflAECYNLcpeQDKILVAVKTLKD---ASDNARKDFHREAELLTNLQHEHIVKFYGVCVE 453
Cdd:cd14106     5 INEVYTVESTPLGRGKFAVV--RKCIHK---ETGKEYAAKFLRKrrrGQDCRNEILHEIAVLELCKDCPRVVNLHEVYET 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 454 GDPLIMVFEYMKHGDLNKFLrahgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV-GENL 532
Cdd:cd14106    80 RSELILILELAAGGELQTLL-------------DEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtSEFP 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 533 L--VKIGDFGMSRDV-YSTDYYRVGGhtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIEC 609
Cdd:cd14106   147 LgdIKLCDFGISRVIgEGEEIREILG----TPDYVAPEILSYEPISLATDMWSIGVLTYVLLT-GHSPFGGDDKQETFLN 221

                  ....*.
gi 1610576541 610 ITQGRV 615
Cdd:cd14106   222 ISQCNL 227
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
499-643 5.19e-08

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 55.07  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 499 HIAQQIAAGMVYLASQHFV-HRDLATRNCLVGENLLVKIGDFGMS-RDVYSTDYYRVGGHT--MLPIRWMPPEsimYRKF 574
Cdd:cd06618   118 KMTVSIVKALHYLKEKHGViHRDVKPSNILLDESGNVKLCDFGISgRLVDSKAKTRSAGCAayMAPERIDPPD---NPKY 194
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 575 TTESDVWSLGVVLWEIFTyGKQPwYQLSNNEvIECITqgRVLQRPRTCP-------QEVYELMLGCWQREPHMRKN 643
Cdd:cd06618   195 DIRADVWSLGISLVELAT-GQFP-YRNCKTE-FEVLT--KILNEEPPSLppnegfsPDFCSFVDLCLTKDHRYRPK 265
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
379-600 5.39e-08

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 54.44  E-value: 5.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 379 RHNIVLKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTLkdasdnARKDFHREaELLT--NLQHEHIVKFYGVCVEGDP 456
Cdd:cd13991     5 VHWATHQLRIGRGSFGEVHRME-----DKQTGFQCAVKKV------RLEVFRAE-ELMAcaGLTSPRVVPLYGAVREGPW 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 457 LIMVFEYMKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGEN----L 532
Cdd:cd13991    73 VNIFMDLKEGGSLGQLIKEQG-------------CLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDgsdaF 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 533 LVKIG------DFGMSRDVYSTDYYRvGGHTMlpirwMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQ 600
Cdd:cd13991   140 LCDFGhaecldPDGLGKSLFTGDYIP-GTETH-----MAPEVVLGKPCDAKVDVWSSCCMMLHMLN-GCHPWTQ 206
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
383-590 6.10e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 55.09  E-value: 6.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKR-----ELGEGAFGKVflaecynlCPEQDKIL---VAVKTLKDASDNAR--KDFHREAELLTNLQHEHIVKFYGVCV 452
Cdd:cd07874    15 VLKRyqnlkPIGSGAQGIV--------CAAYDAVLdrnVAIKKLSRPFQNQThaKRAYRELVLMKCVNHKNIISLLNVFT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 453 egdPLIMVFEYMKHGDLNKFLRAHGPDAVLMaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 532
Cdd:cd07874    87 ---PQKSLEEFQDVYLVMELMDANLCQVIQM-------ELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 533 LVKIGDFGMSRDVYS---------TDYYRVgghtmlpirwmpPESIMYRKFTTESDVWSLGVVLWEI 590
Cdd:cd07874   157 TLKILDFGLARTAGTsfmmtpyvvTRYYRA------------PEVILGMGYKENVDIWSVGCIMGEM 211
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
373-666 6.94e-08

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 54.66  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 373 FVQHikrHNIVLK-RELGEGAFgkvflAECYNLCPEQDKILVAVKTLkdaSDNARKDFHREAELLTNLQ-HEHIVKFYGV 450
Cdd:cd14179     2 FYQH---YELDLKdKPLGEGSF-----SICRKCLHKKTNQEYAVKIV---SKRMEANTQREIAALKLCEgHPNIVKLHEV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 451 CVEGDPLIMVFEYMKHGDLNKFLRAHgpdavlmaegnppTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV-- 528
Cdd:cd14179    71 YHDQLHTFLVMELLKGGELLERIKKK-------------QHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtd 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 529 -GENLLVKIGDFGMSRdVYSTDYYRVGGhTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQ------- 600
Cdd:cd14179   138 eSDNSEIKIIDFGFAR-LKPPDNQPLKT-PCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLS-GQVPFQChdksltc 214
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610576541 601 LSNNEVIECITQGRVL---QRPRTCPQEVYELMLGCWQREPHMRKNIKGI--HTLLQNLAKASPVYL---DILG 666
Cdd:cd14179   215 TSAEEIMKKIKQGDFSfegEAWKNVSQEAKDLIQGLLTVDPNKRIKMSGLryNEWLQDGSQLSSNPLmtpDILG 288
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
45-125 7.15e-08

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 50.27  E-value: 7.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  45 LAAPNLTVEEGKSITLSCSV-AGDPVPNMYW----DVGNLVSKHM-NETSHTQGSLRITNISSDDSGKqISCVAENLVGE 118
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSAsTGSPGPDVTWskegGTLIESLKVKhDNGRTTQSSLLISNVTKEDAGT-YTCVVNNPGGS 79

                  ....*..
gi 1610576541 119 DQDSVNL 125
Cdd:pfam00047  80 ATLSTSL 86
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
383-594 7.98e-08

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 55.05  E-value: 7.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKR-----ELGEGAFGKVflaecynlCPEQDKIL---VAVKTLKDASDNAR--KDFHREAELLTNLQHEHIVKFYGVCV 452
Cdd:cd07875    22 VLKRyqnlkPIGSGAQGIV--------CAAYDAILernVAIKKLSRPFQNQThaKRAYRELVLMKCVNHKNIIGLLNVFT 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 453 egdPLIMVFEYMKHGDLNKFLRAHGPDAVLMaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 532
Cdd:cd07875    94 ---PQKSLEEFQDVYIVMELMDANLCQVIQM-------ELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 533 LVKIGDFGMSRDVYS---------TDYYRVgghtmlpirwmpPESIMYRKFTTESDVWSLGVVLWEIFTYG 594
Cdd:cd07875   164 TLKILDFGLARTAGTsfmmtpyvvTRYYRA------------PEVILGMGYKENVDIWSVGCIMGEMIKGG 222
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
388-590 1.08e-07

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 54.66  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNlCPEQdkilVAVKtlKDASDNARKDfhREAELLTNLQHEHIV----KFYGVCVEGDP----LIM 459
Cdd:PTZ00036   74 IGNGSFGVVYEAICID-TSEK----VAIK--KVLQDPQYKN--RELLIMKNLNHINIIflkdYYYTECFKKNEknifLNV 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHgDLNKFLRAHgpdavlmAEGNPPTELTQSQMLhiAQQIAAGMVYLASQHFVHRDLATRNCLVGENL-LVKIGD 538
Cdd:PTZ00036  145 VMEFIPQ-TVHKYMKHY-------ARNNHALPLFLVKLY--SYQLCRALAYIHSKFICHRDLKPQNLLIDPNThTLKLCD 214
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541 539 FGMSRDVYS---------TDYYRVgghtmlpirwmpPESIM-YRKFTTESDVWSLGVVLWEI 590
Cdd:PTZ00036  215 FGSAKNLLAgqrsvsyicSRFYRA------------PELMLgATNYTTHIDLWSLGCIIAEM 264
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
387-586 1.09e-07

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 53.74  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFG-----------KVFLAECYNLCPEQDKILVavktlkdasdnarkdfHREAELLTNLQHEHIVKFYGVCVEGD 455
Cdd:cd14114     9 ELGTGAFGvvhrcteratgNNFAAKFIMTPHESDKETV----------------RKEIQIMNQLHHPKLINLHDAFEDDN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 456 PLIMVFEYMKHGDLnkFLRahgpdavLMAEGNpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRN--CLVGENLL 533
Cdd:cd14114    73 EMVLILEFLSGGEL--FER-------IAAEHY---KMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENimCTTKRSNE 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 534 VKIGDFGMSRDVYSTDYYRVgghTMLPIRWMPPESIMYRKFTTESDVWSLGVV 586
Cdd:cd14114   141 VKLIDFGLATHLDPKESVKV---TTGTAEFAAPEIVEREPVGFYTDMWAVGVL 190
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
58-118 1.11e-07

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 49.25  E-value: 1.11e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541  58 ITLSCSVAGDPVPNMYW----DVGNLVSKHMNETSHTQGSLRITNISSDDSGKqISCVAENLVGE 118
Cdd:cd00096     1 VTLTCSASGNPPPTITWykngKPLPPSSRDSRRSELGNGTLTISNVTLEDSGT-YTCVASNSAGG 64
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
387-630 1.23e-07

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 53.49  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 387 ELGEGAFGKVFlaECYNlcpEQDKILVAVKTLKDA------SDNARKDFHREAELLtnlQHEHIVKFYGVCVEGDPLIMV 460
Cdd:cd14138    12 KIGSGEFGSVF--KCVK---RLDGCIYAIKRSKKPlagsvdEQNALREVYAHAVLG---QHSHVVRYYSAWAEDDHMLIQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNkflrahgpDAVlmAEGNPPTE-LTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV----------- 528
Cdd:cd14138    84 NEYCNGGSLA--------DAI--SENYRIMSyFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFIsrtsipnaase 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 529 --------GENLLVKIGDFGMSRDVYSTDYYRvgGHTmlpiRWMPPEsIMYRKFT--TESDVWSLGVVLWEifTYGKQPW 598
Cdd:cd14138   154 egdedewaSNKVIFKIGDLGHVTRVSSPQVEE--GDS----RFLANE-VLQENYThlPKADIFALALTVVC--AAGAEPL 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1610576541 599 yqLSNNEVIECITQGRVLQRPRTCPQEVYELM 630
Cdd:cd14138   225 --PTNGDQWHEIRQGKLPRIPQVLSQEFLDLL 254
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
455-641 1.30e-07

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 53.90  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 534
Cdd:cd14223    76 DKLSFILDLMNGGDLHYHLSQHGV-------------FSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHV 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGMSRDVYSTD-YYRVGGHTmlpirWMPPESIMYR-KFTTESDVWSLGVVLWEIFTyGKQPWYQ--LSNNEVIECI 610
Cdd:cd14223   143 RISDLGLACDFSKKKpHASVGTHG-----YMAPEVLQKGvAYDSSADWFSLGCMLFKLLR-GHSPFRQhkTKDKHEIDRM 216
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1610576541 611 TQGRVLQRPRTCPQEVYELMLGCWQREPHMR 641
Cdd:cd14223   217 TLTMAVELPDSFSPELRSLLEGLLQRDVNRR 247
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
432-599 1.36e-07

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 53.56  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 432 EAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPdavlmaegnPPTELTQsqmLHIAQQIAAgMVYL 511
Cdd:cd05609    50 ERDILTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDCATLLKNIGP---------LPVDMAR---MYFAETVLA-LEYL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 512 ASQHFVHRDLATRNCLVGENLLVKIGDFGMSR---DVYSTDYYRvgGHTMLPIR------------WMPPESIMYRKFTT 576
Cdd:cd05609   117 HSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKiglMSLTTNLYE--GHIEKDTRefldkqvcgtpeYIAPEVILRQGYGK 194
                         170       180
                  ....*....|....*....|...
gi 1610576541 577 ESDVWSLGVVLWEiFTYGKQPWY 599
Cdd:cd05609   195 PVDWWAMGIILYE-FLVGCVPFF 216
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
426-614 1.37e-07

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 53.44  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 426 RKDFHREAELLTNLQ-HEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLrahgPDAVLMAEGNpptelTQSQMLHIAQQI 504
Cdd:cd14181    59 RSSTLKEIHILRQVSgHPSIITLIDSYESSTFIFLVFDLMRRGELFDYL----TEKVTLSEKE-----TRSIMRSLLEAV 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 505 AagmvYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS---------RDVYSTDYYrvgghtmlpirwMPPESI------ 569
Cdd:cd14181   130 S----YLHANNIVHRDLKPENILLDDQLHIKLSDFGFSchlepgeklRELCGTPGY------------LAPEILkcsmde 193
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1610576541 570 MYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGR 614
Cdd:cd14181   194 THPGYGKEVDLWACGVILFTLLA-GSPPFWHRRQMLMLRMIMEGR 237
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
385-607 1.39e-07

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 53.42  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 385 KRELGEGAFGKVFLAEcynlcPEQDKILVAVKT-LKDASDNARKdfhREAELLTNLQ-HEHIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14017     5 VKKIGGGGFGEIYKVR-----DVVDGEEVAMKVeSKSQPKQVLK---MEVAVLKKLQgKPHFCRLIGCGRTERYNYIVMT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMkhgdlnkflrahGPD--AVLMAEgnPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLL----VKI 536
Cdd:cd14017    77 LL------------GPNlaELRRSQ--PRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSdertVYI 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 537 GDFGMSRDVY--STDYYRVGGHT---MLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVI 607
Cdd:cd14017   143 LDFGLARQYTnkDGEVERPPRNAagfRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVT-GQLPWRKLKDKEEV 217
IgI_NCAM-1 cd05869
Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members ...
46-127 1.59e-07

Immunoglobulin (Ig)-like I-set domain of Neural Cell Adhesion Molecule 1 (NCAM-1); The members here are composed of the fourth Ig domain of Neural Cell Adhesion Molecule 1(NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM) interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions), through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain. One of the unique features of I-set domains is the lack of a C" strand. The structures of this group show that the Ig domain lacks this strand and thus is a member of the I-set of Ig domains.


Pssm-ID: 143277 [Multi-domain]  Cd Length: 97  Bit Score: 49.59  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  46 AAPNLTVEEGKS-------ITLSCSVAGDPVPNMYWDVG--NLVSK------HMNETSHTQ-GSLRITNISSDDSGKQIs 109
Cdd:cd05869     1 AKPKITYVENQTameleeqITLTCEASGDPIPSITWRTStrNISSEektldgHIVVRSHARvSSLTLKYIQYTDAGEYL- 79
                          90
                  ....*....|....*...
gi 1610576541 110 CVAENLVGEDQDSVNLTV 127
Cdd:cd05869    80 CTASNTIGQDSQSMYLEV 97
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
391-592 1.70e-07

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 53.50  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 391 GAFGKVFLAECYNlcpeqDKILVAVKTLKDasdnaRKDFHREAELLTN--LQHEHIVKFYGVCVEGDPLIMVF----EYM 464
Cdd:cd14140     6 GRFGCVWKAQLMN-----EYVAVKIFPIQD-----KQSWQSEREIFSTpgMKHENLLQFIAAEKRGSNLEMELwlitAFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 465 KHGDLNKFLRahgpdavlmaeGNPpteLTQSQMLHIAQQIAAGMVYLASQ-----------HFVHRDLATRNCLVGENLL 533
Cdd:cd14140    76 DKGSLTDYLK-----------GNI---VSWNELCHIAETMARGLSYLHEDvprckgeghkpAIAHRDFKSKNVLLKNDLT 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610576541 534 VKIGDFGMSRDVY-----STDYYRVGGHtmlpiRWMPPESI-----MYRKFTTESDVWSLGVVLWEIFT 592
Cdd:cd14140   142 AVLADFGLAVRFEpgkppGDTHGQVGTR-----RYMAPEVLegainFQRDSFLRIDMYAMGLVLWELVS 205
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
414-592 1.77e-07

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 53.17  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 414 AVKTL-KDASDNARKDF-HR---EAELLTNLQHEHIVKFYGVCVEGD-PLIMVFEYMkHGDLNKFLRAHgpdavlMAEGN 487
Cdd:cd14001    32 AVKKInSKCDKGQRSLYqERlkeEAKILKSLNHPNIVGFRAFTKSEDgSLCLAMEYG-GKSLNDLIEER------YEAGL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 488 PPteLTQSQMLHIAQQIAAGMVYLasqHFV----HRDLATRNCLV-GENLLVKIGDFG--------MSRDVYSTDYYrVG 554
Cdd:cd14001   105 GP--FPAATILKVALSIARALEYL---HNEkkilHGDIKSGNVLIkGDFESVKLCDFGvslpltenLEVDSDPKAQY-VG 178
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1610576541 555 GHTmlpirWMPPESIMYRK-FTTESDVWSLGVVLWEIFT 592
Cdd:cd14001   179 TEP-----WKAKEALEEGGvITDKADIFAYGLVLWEMMT 212
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
386-598 1.99e-07

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 52.98  E-value: 1.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 386 RELGEGAFGKVFLAECYNL-----CPEQDKilvavKTLKdaSDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMV 460
Cdd:cd05607     8 RVLGKGGFGEVCAVQVKNTgqmyaCKKLDK-----KRLK--KKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 461 FEYMKHGDLNKFLRAHGPDAVLMaegnppteltqSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFG 540
Cdd:cd05607    81 MSLMNGGDLKYHIYNVGERGIEM-----------ERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLG 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 541 MSRDVY--STDYYRVGGHTmlpirWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPW 598
Cdd:cd05607   150 LAVEVKegKPITQRAGTNG-----YMAPEILKEESYSYPVDWFAMGCSIYEMVA-GRTPF 203
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
384-585 2.02e-07

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 53.45  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGK--VFLAECynlcpEQDKILVAVK--TLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIM 459
Cdd:cd08216     2 LLYEIGKCFKGGgvVHLAKH-----KPTNTLVAVKkiNLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 460 VFEYMKHGDLNKFLRAHGPdavlmaEGNPPTELTQsqmlhIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDF 539
Cdd:cd08216    77 VTPLMAYGSCRDLLKTHFP------EGLPELAIAF-----ILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGL 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1610576541 540 gmsRDVYS----------TDYYRVGGHTMLPirWMPPEsIMY---RKFTTESDVWSLGV 585
Cdd:cd08216   146 ---RYAYSmvkhgkrqrvVHDFPKSSEKNLP--WLSPE-VLQqnlLGYNEKSDIYSVGI 198
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
383-599 2.09e-07

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 53.11  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 383 VLKRELGEGAFGKVFlaECYNLcPEQDKIlvAVKTLKDASDNARK-DFHREAElltnlQHEHIVKF---YGVCVEGDP-L 457
Cdd:cd14170     5 VTSQVLGLGINGKVL--QIFNK-RTQEKF--ALKMLQDCPKARREvELHWRAS-----QCPHIVRIvdvYENLYAGRKcL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 458 IMVFEYMKHGDLNKFLRAHGPDAvlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGE---NLLV 534
Cdd:cd14170    75 LIVMECLDGGELFSRIQDRGDQA-----------FTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSkrpNAIL 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 535 KIGDFGMSRDvySTDYYRVGGHTMLPIrWMPPESIMYRKFTTESDVWSLGVVLWeIFTYGKQPWY 599
Cdd:cd14170   144 KLTDFGFAKE--TTSHNSLTTPCYTPY-YVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGYPPFY 204
IgI_2_MuSK cd20968
agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ...
49-117 2.11e-07

agrin-responsive second immunoglobulin-like domains (Ig2) of the Muscle-specific kinase (MuSK) ectodomain; a member of the I-set of Ig superfamily domains; The members here are composed of the second immunoglobulin-like (Ig) domains of the Muscle-specific kinase (MuSK) ectodomain. MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409560 [Multi-domain]  Cd Length: 88  Bit Score: 49.16  E-value: 2.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  49 NLTVEEGKSITLSCSVAGDPVPNMYWDVGNLVSKHMNETSHTQ-GSLRITNISSDDSGkQISCVAENLVG 117
Cdd:cd20968     8 NVTIIEGLKAVLPCTTMGNPKPSVSWIKGDDLIKENNRIAVLEsGSLRIHNVQKEDAG-QYRCVAKNSLG 76
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
388-591 2.12e-07

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 53.56  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVflAECYNLCPEQdkiLVAVKTLKDASDNARKDfHREAELLTNLQHE-----HIVKFYGVCVEGDPLIMVFE 462
Cdd:cd14227    23 LGRGTFGQV--VKCWKRGTNE---IVAIKILKNHPSYARQG-QIEVSILARLSTEsaddyNFVRAYECFQHKNHTCLVFE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 463 YMKHgDLNKFLRAhgpdavlmaegNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV----GENLLVKIGD 538
Cdd:cd14227    97 MLEQ-NLYDFLKQ-----------NKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpsRQPYRVKVID 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576541 539 FG----MSRDVYST----DYYRVgghtmlpirwmpPESIMYRKFTTESDVWSLGVVLWEIF 591
Cdd:cd14227   165 FGsashVSKAVCSTylqsRYYRA------------PEIILGLPFCEAIDMWSLGCVIAELF 213
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
503-629 2.24e-07

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 53.09  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 503 QIAAGMVYL-ASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDV-------YSTDYYRVGGH--TMLPIRWMPPESIMYR 572
Cdd:cd14011   122 QISEALSFLhNDVKLVHGNICPESVVINSNGEWKLAGFDFCISSeqatdqfPYFREYDPNLPplAQPNLNYLAPEYILSK 201
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610576541 573 KFTTESDVWSLGVVLWEIFTYGKQPW----YQLSNNEVIECITQGR--VLQRPrtcPQEVYEL 629
Cdd:cd14011   202 TCDPASDMFSLGVLIYAIYNKGKPLFdcvnNLLSYKKNSNQLRQLSlsLLEKV---PEELRDH 261
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
45-127 2.26e-07

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 48.55  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  45 LAAPNLTVEEGKSITLSCSVAGDPVPNMYWD-VGNLVSKHMNETshtqgslrITNISSDDSGKqISCVAEN-LVGEDQDS 122
Cdd:pfam13895   4 LTPSPTVVTEGEPVTLTCSAPGNPPPSYTWYkDGSAISSSPNFF--------TLSVSAEDSGT-YTCVARNgRGGKVSNP 74

                  ....*
gi 1610576541 123 VNLTV 127
Cdd:pfam13895  75 VELTV 79
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
384-588 2.78e-07

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 52.94  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVflaecYNLCPEQDKILVAVKTLK-DASDNARKDFhREAELLTNLQ--HEHIVKF------------- 447
Cdd:cd13977     4 LIREVGRGSYGVV-----YEAVVRRTGARVAVKKIRcNAPENVELAL-REFWALSSIQrqHPNVIQLeecvlqrdglaqr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 448 --YG------------VCVEG----DP-----LIMVFEYMKHGDLNKFLRAHGPDAvlmaegnpptELTQSQMLhiaqQI 504
Cdd:cd13977    78 msHGssksdlylllveTSLKGercfDPrsacyLWFVMEFCDGGDMNEYLLSRRPDR----------QTNTSFML----QL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 505 AAGMVYLASQHFVHRDLATRNCLVGENL---LVKIGDFGMSRDVYS---------------------TDYYrvgghtmlp 560
Cdd:cd13977   144 SSALAFLHRNQIVHRDLKPDNILISHKRgepILKVADFGLSKVCSGsglnpeepanvnkhflssacgSDFY--------- 214
                         250       260
                  ....*....|....*....|....*...
gi 1610576541 561 irwMPPEsIMYRKFTTESDVWSLGVVLW 588
Cdd:cd13977   215 ---MAPE-VWEGHYTAKADIFALGIIIW 238
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
388-606 2.96e-07

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 52.41  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 388 LGEGAFGKVFLAECYNLCPEqdkilVAVKTLKDA--SDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMk 465
Cdd:cd14082    11 LGSGQFGIVYGGKHRKTGRD-----VAIKVIDKLrfPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 466 HGDLNKFLRAHgpdavlmAEGNPPTELTQsqmlHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL---LVKIGDFGMS 542
Cdd:cd14082    85 HGDMLEMILSS-------EKGRLPERITK----FLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 543 RDVYSTDYYR--VGGHTMLPirwmpPESIMYRKFTTESDVWSLGVVLW-------------EI--------FTYGKQPWY 599
Cdd:cd14082   154 RIIGEKSFRRsvVGTPAYLA-----PEVLRNKGYNRSLDMWSVGVIIYvslsgtfpfnedeDIndqiqnaaFMYPPNPWK 228

                  ....*..
gi 1610576541 600 QLSNNEV 606
Cdd:cd14082   229 EISPDAI 235
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
384-615 3.17e-07

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 52.20  E-value: 3.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 384 LKRELGEGAFGKVflaecYNLCPEQDKILVAVKTLKDASdNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEY 463
Cdd:cd14107     6 VKEEIGRGTFGFV-----KRVTHKGNGECCAAKFIPLRS-STRARAFQERDILARLSHRRLTCLLDQFETRKTLILILEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 464 MKHGDLNKFLRAHGpdavlmaegnpptELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLV--GENLLVKIGDFGM 541
Cdd:cd14107    80 CSSEELLDRLFLKG-------------VVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGF 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 542 SRDVYSTD--YYRVGGhtmlPiRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYgKQPWYQLSNNEVIECITQGRV 615
Cdd:cd14107   147 AQEITPSEhqFSKYGS----P-EFVAPEIVHQEPVSAATDIWALGVIAYLSLTC-HSPFAGENDRATLLNVAEGVV 216
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
40-126 3.55e-07

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 48.51  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541  40 LPSANLAAP-NLTVEEGKSITLSCSVAGDPVPNMYW-DVGNLVS---KHMNETSHTQGSLRITNISSDDSGkQISCVAEN 114
Cdd:cd05747     2 LPATILTKPrSLTVSEGESARFSCDVDGEPAPTVTWmREGQIIVssqRHQITSTEYKSTFEISKVQMSDEG-NYTVVVEN 80
                          90
                  ....*....|..
gi 1610576541 115 LVGEDQDSVNLT 126
Cdd:cd05747    81 SEGKQEAQFTLT 92
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
455-646 3.98e-07

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 52.76  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 455 DPLIMVFEYMKHGDLNKFLRAHGPdavlmaegnppteLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLV 534
Cdd:cd05633    81 DKLCFILDLMNGGDLHYHLSQHGV-------------FSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHV 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 535 KIGDFGMSRDVYSTD-YYRVGGHTmlpirWMPPESIMY-RKFTTESDVWSLGVVLWEIFTyGKQPWYQ--LSNNEVIECI 610
Cdd:cd05633   148 RISDLGLACDFSKKKpHASVGTHG-----YMAPEVLQKgTAYDSSADWFSLGCMLFKLLR-GHSPFRQhkTKDKHEIDRM 221
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1610576541 611 TQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKG 646
Cdd:cd05633   222 TLTVNVELPDSFSPELKSLLEGLLQRDVSKRLGCHG 257
I-set pfam07679
Immunoglobulin I-set domain;
150-216 8.24e-07

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 47.25  E-value: 8.24e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610576541 150 TVKGNPKPALQWFYNGAILNESKyictKIHVTNhTEYHGCLQLDNPTHMNNGDYTLIAKNEYGKDEK 216
Cdd:pfam07679  23 TVTGTPDPEVSWFKDGQPLRSSD----RFKVTY-EGGTYTLTISNVQPDDSGKYTCVATNSAGEAEA 84
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
147-221 2.97e-06

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 45.85  E-value: 2.97e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610576541 147 IPFTVKGNPKPALQWFYNGAILNESKYictKIHVTNHTeyhgcLQLDNPTHMNNGDYTLIAKNEYGKDEKQISAH 221
Cdd:cd20978    21 LPCQVTGVPQPKITWLHNGKPLQGPME---RATVEDGT-----LTIINVQPEDTGYYGCVATNEIGDIYTETLLH 87
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
147-212 1.08e-05

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 43.86  E-value: 1.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610576541 147 IPFTVKGNPKPALQWFYNGAILNESKYICTKIHVTNHTeyhgcLQLDNPTHMNNGDYTLIAKNEYG 212
Cdd:cd00096     3 LTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGT-----LTISNVTLEDSGTYTCVASNSAG 63
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
151-219 2.91e-04

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 40.42  E-value: 2.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610576541 151 VKGNPKPALQWFYNGAILNESKYictkiHVTNHTEYHGCLQLDNPTHMNNGDYTLIAKNEYGKDEKQIS 219
Cdd:cd05747    27 VDGEPAPTVTWMREGQIIVSSQR-----HQITSTEYKSTFEISKVQMSDEGNYTVVVENSEGKQEAQFT 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
150-209 3.62e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 39.47  E-value: 3.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576541 150 TVKGNPKPALQWFYNGAILNESKYICTKIHVTNHTeyhgcLQLDNPTHMNNGDYTLIAKN 209
Cdd:pfam13927  24 EATGSPPPTITWYKNGEPISSGSTRSRSLSGSNST-----LTISNVTRSDAGTYTCVASN 78
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
147-218 6.60e-03

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 36.33  E-value: 6.60e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610576541  147 IPFTVKGNPKPALQWFYNGAILNESKyicTKIHVTNHTeYHGCLQLDNPTHMNNGDYTLIAKNEYGKDEKQI 218
Cdd:smart00410  14 LSCEASGSPPPEVTWYKQGGKLLAES---GRFSVSRSG-STSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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