Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDELLRVMPSFVS-STWEVKRPLRKLLPEVNSEAIDFLE 79
Cdd:cd07854  202 MWAAGCIFAEMLTGKPLFAGAHELEQMQLILESVPVVREEDRNELLNVIPSFVRnDGGEPRRPLRDLLPGVNPEALDFLE 281

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 635574613  80 KILTFNPMDRLTAEMGLQHPYMSPYSCPEDEPTSQHPFRIEDEIDDIVLMAANQSQLSNWD 140
Cdd:cd07854  282 QILTFNPMDRLTAEEALMHPYMSCYSCPFDEPVSLHPFHIEDELDDILLMTEIHSIIYNWD 342

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDELLRVMPSFVS-STWEVKRPLRKLLPEVNSEAIDFLE 79
Cdd:cd07854  202 MWAAGCIFAEMLTGKPLFAGAHELEQMQLILESVPVVREEDRNELLNVIPSFVRnDGGEPRRPLRDLLPGVNPEALDFLE 281

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 635574613  80 KILTFNPMDRLTAEMGLQHPYMSPYSCPEDEPTSQHPFRIEDEIDDIVLMAANQSQLSNWD 140
Cdd:cd07854  282 QILTFNPMDRLTAEEALMHPYMSCYSCPFDEPVSLHPFHIEDELDDILLMTEIHSIIYNWD 342

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613     1 MWAAGCILAEMLTGRMLFAGAHELEQM-QLILETIPVIREEDkdellrvmpsfvsstwevkrplrkllPEVNSEAIDFLE 79
Cdd:smart00220 179 IWSLGVILYELLTGKPPFPGDDQLLELfKKIGKPKPPFPPPE--------------------------WDISPEAKDLIR 232

                           90       100
                   ....*....|....*....|..
gi 635574613    80 KILTFNPMDRLTAEMGLQHPYM 101
Cdd:smart00220 233 KLLVKDPEKRLTAEEALQHPFF 254

Serine/threonine protein kinase [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   2 WAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVireedkdellrvmpsfvsstwevkrPLRKLLPEVNSEAIDFLEKI 81
Cdd:COG0515  192 YSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPP-------------------------PPSELRPDLPPALDAIVLRA 246

                 ....*...
gi 635574613  82 LTFNPMDR 89
Cdd:COG0515  247 LAKDPEER 254

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDELLRVMPSFVS-STWEVKRPLRKLLPEVNSEAIDFLE 79
Cdd:cd07854  202 MWAAGCIFAEMLTGKPLFAGAHELEQMQLILESVPVVREEDRNELLNVIPSFVRnDGGEPRRPLRDLLPGVNPEALDFLE 281

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 635574613  80 KILTFNPMDRLTAEMGLQHPYMSPYSCPEDEPTSQHPFRIEDEIDDIVLMAANQSQLSNWD 140
Cdd:cd07854  282 QILTFNPMDRLTAEEALMHPYMSCYSCPFDEPVSLHPFHIEDELDDILLMTEIHSIIYNWD 342

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKD--------ELLRVMPsfvsstWEVKRPLRKLLPEVNS 72
Cdd:cd07849  193 IWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGTPSQEDLNciislkarNYIKSLP------FKPKVPWNKLFPNADP 266

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 635574613  73 EAIDFLEKILTFNPMDRLTAEMGLQHPYMSPYSCPEDEPTSQHPFRIEDEIDD 125
Cdd:cd07849  267 KALDLLDKMLTFNPHKRITVEEALAHPYLEQYHDPSDEPVAEEPFPFDMELFD 319

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDEL--------LRVMPSFVsstwevKRPLRKLLPEVNS 72
Cdd:cd07858  192 VWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGSPSEEDLGFIrnekarryIRSLPYTP------RQSFARLFPHANP 265

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 635574613  73 EAIDFLEKILTFNPMDRLTAEMGLQHPYMSPYSCPEDEPTSQHPFRIEDEIDDI 126
Cdd:cd07858  266 LAIDLLEKMLVFDPSKRITVEEALAHPYLASLHDPSDEPVCQTPFSFDFEEDAL 319

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLIL--------ETIPVIREEDKDELLRVMPSFVsstwevKRPLRKLLPEVNS 72
Cdd:cd07851  199 IWSVGCIMAELLTGKTLFPGSDHIDQLKRIMnlvgtpdeELLKKISSESARNYIQSLPQMP------KKDFKEVFSGANP 272

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 635574613  73 EAIDFLEKILTFNPMDRLTAEMGLQHPYMSPYSCPEDEPTsQHPFRIEDEIDDI 126
Cdd:cd07851  273 LAIDLLEKMLVLDPDKRITAAEALAHPYLAEYHDPEDEPV-APPYDQSFESRDL 325

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDELLRV-------MPSFVSStwevkrPLRKLLPEVNSE 73
Cdd:cd07830  182 IWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPTKQDWPEGYKLasklgfrFPQFAPT------SLHQLIPNASPE 255

                         90       100
                 ....*....|....*....|....*...
gi 635574613  74 AIDFLEKILTFNPMDRLTAEMGLQHPYM 101
Cdd:cd07830  256 AIDLIKDMLRWDPKKRPTASQALQHPYF 283

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDELLRVMP-SFVSSTwevKRPLRKLLPEVNSEAIDFLE 79
Cdd:cd07838  189 MWSVGCIFAELFNRRPLFRGSSEADQLGKIFDVIGLPSEEEWPRNSALPRsSFPSYT---PRPFKSFVPEIDEEGLDLLK 265

                         90       100
                 ....*....|....*....|.
gi 635574613  80 KILTFNPMDRLTAEMGLQHPY 100
Cdd:cd07838  266 KMLTFNPHKRISAFEALQHPY 286

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDELLRvMPSFVSSTWEVKRPLRKLLPEVNSEAIDFLEK 80
Cdd:cd07841  186 MWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTEENWPGVTS-LPDYVEFKPFPPTPLKQIFPAASDDALDLLQR 264

                         90       100       110
                 ....*....|....*....|....*....|..
gi 635574613  81 ILTFNPMDRLTAEMGLQHPYMS--PYSCPEDE 110
Cdd:cd07841  265 LLTLNPNKRITARQALEHPYFSndPAPTPPSQ 296

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLIL--------ETIPVIREEDKDELLRVMPSFVsstwevKRPLRKLLPEVNS 72
Cdd:cd07880  199 IWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMkvtgtpskEFVQKLQSEDAKNYVKKLPRFR------KKDFRSLLPNANP 272

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 635574613  73 EAIDFLEKILTFNPMDRLTAEMGLQHPYMSPYSCPEDEPTSQhPFriEDEIDDI 126
Cdd:cd07880  273 LAVNVLEKMLVLDAESRITAAEALAHPYFEEFHDPEDETEAP-PY--DDSFDEV 323

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDELLRvMPSF--VSSTWEVKRPLRKLLPEVNSE-AIDF 77
Cdd:cd07840  189 MWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEENWPGVSD-LPWFenLKPKKPYKRRLREVFKNVIDPsALDL 267

                         90       100
                 ....*....|....*....|...
gi 635574613  78 LEKILTFNPMDRLTAEMGLQHPY 100
Cdd:cd07840  268 LDKLLTLDPKKRISADQALQHEY 290

Protein kinase domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613    1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILetipvireedkDELLRvmpsfvsstwevkrpLRKLLPEVNSEAIDFLEK 80
Cdd:pfam00069 143 VWSLGCILYELLTGKPPFPGINGNEIYELII-----------DQPYA---------------FPELPSNLSEEAKDLLKK 196

                          90       100
                  ....*....|....*....|.
gi 635574613   81 ILTFNPMDRLTAEMGLQHPYM 101
Cdd:pfam00069 197 LLKKDPSKRLTATQALQHPWF 217

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613     1 MWAAGCILAEMLTGRMLFAGAHELEQM-QLILETIPVIREEDkdellrvmpsfvsstwevkrplrkllPEVNSEAIDFLE 79
Cdd:smart00220 179 IWSLGVILYELLTGKPPFPGDDQLLELfKKIGKPKPPFPPPE--------------------------WDISPEAKDLIR 232

                           90       100
                   ....*....|....*....|..
gi 635574613    80 KILTFNPMDRLTAEMGLQHPYM 101
Cdd:smart00220 233 KLLVKDPEKRLTAEEALQHPFF 254

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETI-----PVI-----REEDKDELLRvmPSFVSSTWEVKRP-----LRK 65
Cdd:cd14210  198 MWSLGCILAELYTGYPLFPGENEEEQLACIMEVLgvppkSLIdkasrRKKFFDSNGK--PRPTTNSKGKKRRpgsksLAQ 275

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 635574613  66 LLPEVNSEAIDFLEKILTFNPMDRLTAEMGLQHPYM 101
Cdd:cd14210  276 VLKCDDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETI-PVIREEdkDELLRVMPSFVSSTW-EVKRPL---RKLLPEVNSEAI 75
Cdd:cd07833  185 VWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLgPLPPSH--QELFSSNPRFAGVAFpEPSQPEsleRRYPGKVSSPAL 262

                         90       100
                 ....*....|....*....|....*
gi 635574613  76 DFLEKILTFNPMDRLTAEMGLQHPY 100
Cdd:cd07833  263 DFLKACLRMDPKERLTCDELLQHPY 287

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETI--PvirEEDKDELLRVMPSFVSS--TWEvKRPLRKLLPEVNSEAID 76
Cdd:cd07835  183 IWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLgtP---DEDVWPGVTSLPDYKPTfpKWA-RQDLSKVVPSLDEDGLD 258

                         90       100
                 ....*....|....*....|....
gi 635574613  77 FLEKILTFNPMDRLTAEMGLQHPY 100
Cdd:cd07835  259 LLSQMLVYDPAKRISAKAALQHPY 282

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDElLRVMPSF--VSSTWEVKRPLRKLLPEVNSEAIDFL 78
Cdd:cd07866  210 IWGIGCVFAEMFTRRPILQGKSDIDQLHLIFKLCGTPTEETWPG-WRSLPGCegVHSFTNYPRTLEERFGKLGPEGLDLL 288

                         90       100
                 ....*....|....*....|..
gi 635574613  79 EKILTFNPMDRLTAEMGLQHPY 100
Cdd:cd07866  289 SKLLSLDPYKRLTASDALEHPY 310

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPvireedkdellrvmpsfvsstwevkrplrkllpevNSEAIDFLEK 80
Cdd:cd05118  184 IWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLG-----------------------------------TPEALDLLSK 228

                         90       100
                 ....*....|....*....|
gi 635574613  81 ILTFNPMDRLTAEMGLQHPY 100
Cdd:cd05118  229 MLKYDPAKRITASQALAHPY 248

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREedkdellRVMPSF-----VSSTWEVKRP---LRKLLPEVNS 72
Cdd:cd07845  192 MWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPNE-------SIWPGFsdlplVGKFTLPKQPynnLKHKFPWLSE 264

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 635574613  73 EAIDFLEKILTFNPMDRLTAEMGLQHPYM--SPYSC-PEDEPT 112
Cdd:cd07845  265 AGLRLLNFLLMYDPKKRATAEEALESSYFkeKPLPCePEMMPT 307

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAgAHE----LEQMQLILETIP--VIREEDKDEL------LRVMPSFVSST----WEVKRPLR 64
Cdd:cd14134  214 VWSIGCILVELYTGELLFQ-THDnlehLAMMERILGPLPkrMIRRAKKGAKyfyfyhGRLDWPEGSSSgrsiKRVCKPLK 292

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 635574613  65 KLLPEVNSEA---IDFLEKILTFNPMDRLTAEMGLQHPY 100
Cdd:cd14134  293 RLMLLVDPEHrllFDLIRKMLEYDPSKRITAKEALKHPF 331

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDELLRvMPSFVSS--TWEvKRPLRKLLPEVNSEAIDFL 78
Cdd:cd07861  185 IWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTPTEDIWPGVTS-LPDYKNTfpKWK-KGSLRTAVKNLDEDGLDLL 262

                         90       100
                 ....*....|....*....|..
gi 635574613  79 EKILTFNPMDRLTAEMGLQHPY 100
Cdd:cd07861  263 EKMLIYDPAKRISAKKALVHPY 284

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   2 WAAGCILAEMLTGRMLFAGAHELEQMQLILETIpvireedKDELLRVMPSFVSSTW---------EVKRPLRKLLPEVNS 72
Cdd:cd07847  185 WAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTL-------GDLIPRHQQIFSTNQFfkglsipepETREPLESKFPNISS 257

                         90       100
                 ....*....|....*....|....*....
gi 635574613  73 EAIDFLEKILTFNPMDRLTAEMGLQHPYM 101
Cdd:cd07847  258 PALSFLKGCLQMDPTERLSCEELLEHPYF 286

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDELLRVMPSFvsstwevkrplrkllpevnseaIDFLEK 80
Cdd:cd14133  184 MWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLDQGKADDELF----------------------VDFLKK 241

                         90       100
                 ....*....|....*....|.
gi 635574613  81 ILTFNPMDRLTAEMGLQHPYM 101
Cdd:cd14133  242 LLEIDPKERPTASQALSHPWL 262

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLI--------LETIPVIREEDKDELLRV---MPSFVSstwevkrpLRKLLPE 69
Cdd:cd07853  188 IWSVGCIFAELLGRRILFQAQSPIQQLDLItdllgtpsLEAMRSACEGARAHILRGphkPPSLPV--------LYTLSSQ 259

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 635574613  70 VNSEAIDFLEKILTFNPMDRLTAEMGLQHPYM--------------------SPYSCPEDEPTSQHPFRIEDE 122
Cdd:cd07853  260 ATHEAVHLLCRMLVFDPDKRISAADALAHPYLdegrlryhtcmckccyttsgGRVYTSDFEPSANPPFDDEYE 332

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635574613   1 MWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDELLRvMPSFVSSTWEVKRP--LRKLLPEVNSEAIDFL 78
Cdd:cd07873  184 MWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILS-NEEFKSYNYPKYRAdaLHNHAPRLDSDGADLL 262

                         90       100
                 ....*....|....*....|..
gi 635574613  79 EKILTFNPMDRLTAEMGLQHPY 100
Cdd:cd07873  263 SKLLQFEGRKRISAEEAMKHPY 284