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Conserved domains on  [gi|530387683|ref|XP_005273515|]
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kinesin-like protein KIF13B isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
4-360 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


:

Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 602.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNLSKGDARGQPKVFAYDHCFWSMDeSVKEKYAGQDIVFKC 82
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLkNPKQADKNNKATREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  163 DPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSG 240
Cdd:cd01365   160 NPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  241 TSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01365   240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSFIPYRDSVLTWLLKENL 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 530387683  319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:cd01365   320 GGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
447-545 4.13e-68

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


:

Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 224.02  E-value: 4.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22730     1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80
                          90
                  ....*....|....*....
gi 530387683  527 HHGDRILWGNNHFFRLNLP 545
Cdd:cd22730    81 HHGDRILWGNNHFFRINLP 99
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
1683-1746 3.22e-30

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


:

Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 114.42  E-value: 3.22e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530387683  1683 GEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRV 1746
Cdd:pfam01302    2 GDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
Kinesin_assoc super family cl24686
Kinesin-associated;
357-469 5.41e-25

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 103.77  E-value: 5.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   357 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 391
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   392 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 454
Cdd:pfam16183   81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160
                          170
                   ....*....|....*
gi 530387683   455 ADPALNELLVYYLKE 469
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
756-802 1.85e-13

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


:

Pssm-ID: 463574  Cd Length: 43  Bit Score: 66.09  E-value: 1.85e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 530387683   756 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 802
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1422-1660 5.10e-11

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.43  E-value: 5.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1422 GIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFV-PQMPKLLKSLFPVRDEKRGKRPSPLAHQAQPEmGPDVLVQTm 1500
Cdd:PHA03247 2493 GAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVhPRMLTWIRGLEELASDDAGDPPPPLPPAAPPA-APDRSVPP- 2570
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1501 gapalkicDKPAKVPSPPpviAVTAVTPAPEAqdgPPSPLSEASsgyfshsvstatlsdalgPGLDAAAPPGSMPTAPeA 1580
Cdd:PHA03247 2571 --------PRPAPRPSEP---AVTSRARRPDA---PPQSARPRA------------------PVDDRGDPRGPAPPSP-L 2617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1581 EPEAPISHPPPPTAVP-AEEPPGPQQLVSPGRERPDlEAPAPGSPFRVRRVRA--------SELRSFSRMLAGDPGCSPG 1651
Cdd:PHA03247 2618 PPDTHAPDPPPPSPSPaANEPDPHPPPTVPPPERPR-DDPAPGRVSRPRRARRlgraaqasSPPQRPRRRAARPTVGSLT 2696

                  ....*....
gi 530387683 1652 AEGNAPAPG 1660
Cdd:PHA03247 2697 SLADPPPPP 2705
DUF3694 super family cl13857
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
1221-1278 7.36e-07

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


The actual alignment was detected with superfamily member pfam12473:

Pssm-ID: 463599  Cd Length: 149  Bit Score: 50.66  E-value: 7.36e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530387683  1221 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1278
Cdd:pfam12473   91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
bMERB_dom super family cl48129
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
1099-1143 1.26e-04

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


The actual alignment was detected with superfamily member pfam12130:

Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 43.66  E-value: 1.26e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 530387683  1099 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1143
Cdd:pfam12130   66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
611-760 7.30e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  611 LNSLEQQHE--EEKRSALERQRlmyeHELEQLRRRLSPEKQNCRSMDRFSFHS---PSAQQRLRQWAEEREATLNNS--L 683
Cdd:COG4913   612 LAALEAELAelEEELAEAEERL----EALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSddL 687
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683  684 MRLREQIVKANLLVREANYIAEELDKRteykvtlqipASSLDANRKR-GSLLSEPAIQVRRKGKGKQIWSLEKLDNRL 760
Cdd:COG4913   688 AALEEQLEELEAELEELEEELDELKGE----------IGRLEKELEQaEEELDELQDRLEAAEDLARLELRALLEERF 755
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
4-360 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 602.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNLSKGDARGQPKVFAYDHCFWSMDeSVKEKYAGQDIVFKC 82
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLkNPKQADKNNKATREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  163 DPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSG 240
Cdd:cd01365   160 NPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  241 TSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01365   240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSFIPYRDSVLTWLLKENL 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 530387683  319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:cd01365   320 GGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
6-360 1.71e-156

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 482.07  E-value: 1.71e-156
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683      6 VKVAVRIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGE 85
Cdd:smart00129    2 IRVVVRVRPLNKREKSRKSPSVVPFPDKV----GKTLTVRSPKNRQGEKKFTFDKVF---DAT-----ASQEDVFEETAA 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683     86 NILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTqKEENEEQSFKVEVSYMEIYNEKVRDLLDPk 165
Cdd:smart00129   70 PLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP- 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    166 gSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSgeK 245
Cdd:smart00129  148 -SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSG--K 224
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    246 VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSagknKNKFVPYRDSVLTWLLKDSLGGNSKTA 325
Cdd:smart00129  225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTL 300
                           330       340       350
                    ....*....|....*....|....*....|....*
gi 530387683    326 MVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:smart00129  301 MIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-353 6.53e-149

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 461.27  E-value: 6.53e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    11 RIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFWSmdesvkekYAGQDIVFKCLGENILQN 90
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVD----SETVESSHLTNKNRTKTFTFDKVFDP--------EATQEDVYEETAKPLVES 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    91 AFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQ- 169
Cdd:pfam00225   69 VLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKr 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   170 TLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGeKVGKL 249
Cdd:pfam00225  148 KLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   250 SLVDLAGSERATKTGAA-GDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVA 328
Cdd:pfam00225  227 NLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIA 301
                          330       340
                   ....*....|....*....|....*
gi 530387683   329 TVSPAADNYDETLSTLRYADRAKHI 353
Cdd:pfam00225  302 NISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
50-439 8.55e-95

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 318.99  E-value: 8.55e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   50 RGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSG 129
Cdd:COG5059    52 KSKEGTYAFDKVF---GPS-----ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKE 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  130 LFERTQKEeNEEQSFKVEVSYMEIYNEKVRDLLDPKgsRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRT 209
Cdd:COG5059   124 LFSKLEDL-SMTKDFAVSISYLEIYNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  210 VAATNMNEESSRSHAVFKITLTHtlYDVKSGTSGEkvGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISA 289
Cdd:COG5059   201 TASTEINDESSRSHSIFQIELAS--KNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINA 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  290 LADqsagKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE-----DPN 364
Cdd:COG5059   277 LGD----KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdssREI 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  365 ARIIRDL---REEVEKLREQLTKAEAMKSPELKDR--LEESEKLIQEMTVT---WEEKLRKTEEIAQERQKQLESLGISL 436
Cdd:COG5059   353 EEIKFDLsedRSEIEILVFREQSQLSQSSLSGIFAymQSLKKETETLKSRIdliMKSIISGTFERKKLLKEEGWKYKSTL 432

                  ...
gi 530387683  437 QSS 439
Cdd:COG5059   433 QFL 435
PLN03188 PLN03188
kinesin-12 family protein; Provisional
3-379 3.32e-77

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 282.59  E-value: 3.32e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    3 DSKVKVAVRIRPMNRRETDlhtkcvvDVDANKVILNPVNTNlskgdarGQpkVFAYDhcfwsmdeSVKEKYAGQDIVFKC 82
Cdd:PLN03188   97 DSGVKVIVRMKPLNKGEEG-------EMIVQKMSNDSLTIN-------GQ--TFTFD--------SIADPESTQEDIFQL 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA----------DQPGLIPRLCSGLFERTQKEE----NEEQSFKVEV 148
Cdd:PLN03188  153 VGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRC 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  149 SYMEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKI 228
Cdd:PLN03188  233 SFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  229 TLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgKNKNKFVPYRDS 308
Cdd:PLN03188  311 VVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQ-TGKQRHIPYRDS 389
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683  309 VLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE----DPN--ARIIRDLREEVEKLR 379
Cdd:PLN03188  390 RLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
447-545 4.13e-68

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 224.02  E-value: 4.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22730     1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80
                          90
                  ....*....|....*....
gi 530387683  527 HHGDRILWGNNHFFRLNLP 545
Cdd:cd22730    81 HHGDRILWGNNHFFRINLP 99
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
1683-1746 3.22e-30

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 114.42  E-value: 3.22e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530387683  1683 GEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRV 1746
Cdd:pfam01302    2 GDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
1683-1747 5.85e-26

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 102.28  E-value: 5.85e-26
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683   1683 GEFVTVGAH-KTGVVRYVGPADFQEGTWVGVELDLP-SGKNDGSIGGKQYFRCNPGYGLLVRPSRVR 1747
Cdd:smart01052    2 GDRVEVGGGgRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
Kinesin_assoc pfam16183
Kinesin-associated;
357-469 5.41e-25

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 103.77  E-value: 5.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   357 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 391
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   392 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 454
Cdd:pfam16183   81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160
                          170
                   ....*....|....*
gi 530387683   455 ADPALNELLVYYLKE 469
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
756-802 1.85e-13

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


Pssm-ID: 463574  Cd Length: 43  Bit Score: 66.09  E-value: 1.85e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 530387683   756 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 802
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
1683-1752 4.58e-13

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 74.34  E-value: 4.58e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1683 GEFVTVGAHKtGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGP 1752
Cdd:COG5244     7 NDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGN 75
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
471-534 3.66e-11

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 60.28  E-value: 3.66e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530387683   471 TLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNT-RTFVNGSSVSS-PIQLHHGDRILW 534
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTnGTFVNGQRLGPePVRLKDGDVIRL 66
PHA03247 PHA03247
large tegument protein UL36; Provisional
1422-1660 5.10e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.43  E-value: 5.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1422 GIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFV-PQMPKLLKSLFPVRDEKRGKRPSPLAHQAQPEmGPDVLVQTm 1500
Cdd:PHA03247 2493 GAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVhPRMLTWIRGLEELASDDAGDPPPPLPPAAPPA-APDRSVPP- 2570
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1501 gapalkicDKPAKVPSPPpviAVTAVTPAPEAqdgPPSPLSEASsgyfshsvstatlsdalgPGLDAAAPPGSMPTAPeA 1580
Cdd:PHA03247 2571 --------PRPAPRPSEP---AVTSRARRPDA---PPQSARPRA------------------PVDDRGDPRGPAPPSP-L 2617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1581 EPEAPISHPPPPTAVP-AEEPPGPQQLVSPGRERPDlEAPAPGSPFRVRRVRA--------SELRSFSRMLAGDPGCSPG 1651
Cdd:PHA03247 2618 PPDTHAPDPPPPSPSPaANEPDPHPPPTVPPPERPR-DDPAPGRVSRPRRARRlgraaqasSPPQRPRRRAARPTVGSLT 2696

                  ....*....
gi 530387683 1652 AEGNAPAPG 1660
Cdd:PHA03247 2697 SLADPPPPP 2705
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1396-1621 2.62e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.93  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1396 IPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPqnnhSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEk 1475
Cdd:pfam03154  148 IPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPS----PPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ- 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1476 rgkrpSPLAHQAQPEMGPDVLVQTMGAPALKIcdKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLS-EASSGYFSHSVST 1554
Cdd:pfam03154  223 -----STAAPHTLIQQTPTLHPQRLPSPHPPL--QPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSlQTGPSHMQHPVPP 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1555 ATLSDA---------LGPGLDAAAPPGSMPTAPEAEPEAPISHPP-------PPTAVPAEEPPGPQ---QLVSPGRER-- 1613
Cdd:pfam03154  296 QPFPLTpqssqsqvpPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPreqplppAPLSMPHIKPPPTTpipQLPNPQSHKhp 375

                   ....*...
gi 530387683  1614 PDLEAPAP 1621
Cdd:pfam03154  376 PHLSGPSP 383
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
1221-1278 7.36e-07

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 463599  Cd Length: 149  Bit Score: 50.66  E-value: 7.36e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530387683  1221 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1278
Cdd:pfam12473   91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
1479-1732 1.60e-06

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 52.76  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1479 RPSPLAHQAQPEMGPDVLVQTMGAPAlkICDKPAKvpsPPPVIAVTAVTPAPEAqDGPPSPLSEASSGYFSHSVSTATLS 1558
Cdd:COG5180   243 RSRPATVDAQPEMRPPADAKERRRAA--IGDTPAA---EPPGLPVLEAGSEPQS-DAPEAETARPIDVKGVASAPPATRP 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1559 DALGPG-LDAAAPPGSMPT-APEAEPEAPISHPPPPTAVPAEEP-----PGPQQLVSPGRE-------RPDLEAPAPGSP 1624
Cdd:COG5180   317 VRPPGGaRDPGTPRPGQPTeRPAGVPEAASDAGQPPSAYPPAEEavpgkPLEQGAPRPGSSggdgapfQPPNGAPQPGLG 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1625 FR---VRRVRASELRSFSRMLAGDPGCSPGAEGNAP--APGAGGQALASDSEEADEVPEwlregefVTVGAHKTGVVRYV 1699
Cdd:COG5180   397 RRgapGPPMGAGDLVQAALDGGGRETASLGGAAGGAgqGPKADFVPGDAESVSGPAGLA-------DQAGAAASTAMADF 469
                         250       260       270
                  ....*....|....*....|....*....|...
gi 530387683 1700 GPADFQEGTWVGVELDLPSGKNDGSIGGKQYFR 1732
Cdd:COG5180   470 VAPVTDATPVDVADVLGVRPDAILGGNVAPASG 502
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
1512-1633 7.26e-06

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 50.15  E-value: 7.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1512 AKVPSPPPVIAVT---AVTPAPEAQDGPPSPLSEASSG-----YFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPE 1583
Cdd:NF040712  200 ATVPRLAREPADArpeEVEPAPAAEGAPATDSDPAEAGtpddlASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530387683 1584 APIS---HPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRAS 1633
Cdd:NF040712  280 PPAPgaaETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRAS 332
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
468-542 1.13e-05

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 45.72  E-value: 1.13e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683  468 KEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNTR-TFVNGSSVSSPIQLHHGDRILWGNNHF-FRL 542
Cdd:COG1716    20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRD-GGGWVLEDLGSTNgTFVNGQRVTEPAPLRDGDVIRLGKTELrFRL 95
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
1099-1143 1.26e-04

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 43.66  E-value: 1.26e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 530387683  1099 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1143
Cdd:pfam12130   66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
1501-1620 5.54e-04

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 42.37  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1501 GAPALKICDKPAKVPSPPpviAVTAVTPAPEAQDgPPSPLSEASS-----------GYFSHSVSTATLSDALGPGLDAAA 1569
Cdd:cd21975    29 GLAAGLDVRATREVAKGP---GPPGPAWKPDGAD-SPGLVTAAPHllaanvlaplrGPSVEGSSLESGDADMGSDSDVAP 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530387683 1570 PPGSM-PTAPEAE---PEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPA 1620
Cdd:cd21975   105 ASGAAaSTSPESSsdaASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTPAA 159
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
1558-1642 7.17e-04

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 44.22  E-value: 7.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1558 SDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGR--ERPDLEAPAPGSPFRVRRVRA-SE 1634
Cdd:NF041121   22 PSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPppPGPAGAAPGAALPVRVPAPPAlPN 101

                  ....*...
gi 530387683 1635 LRSFSRML 1642
Cdd:NF041121  102 PLELARAL 109
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
1518-1624 1.51e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 42.83  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1518 PPVIAVTAV-TPAPEAQDGPPSPLSEASSGYF---SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPT 1593
Cdd:NF040712  194 RPLRPLATVpRLAREPADARPEEVEPAPAAEGapaTDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEA 273
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530387683 1594 AVPAEEPPGPQQLVSPGRERPDLEAPAPGSP 1624
Cdd:NF040712  274 TRDAGEPPAPGAAETPEAAEPPAPAPAAPAA 304
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
1511-1678 1.74e-03

poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.


Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 43.14  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1511 PAKVPSPPPVIAV-----TAVTPAPEAQDGPPSP-LSEASSGYFSHSVSTATLSDAL-GPGLDAAAPPGSMP-TAPEAEP 1582
Cdd:TIGR01645  291 PATVSAIPAAAAVaaaaaTAKIMAAEAVAGAAVLgPRAQSPATPSSSLPTDIGNKAVvSSAKKEAEEVPPLPqAAPAVVK 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1583 ----EAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEApAPGSPFRVRRVRASELRSFSRMLAGDP--GCSPGAEGNA 1656
Cdd:TIGR01645  371 pgpmEIPTPVPPPGLAIPSLVA--PPGLVAPTEINPSFLA-SPRKKMKREKLPVTFGALDDTLAWKEPskEDQTSEDGKM 447
                          170       180
                   ....*....|....*....|...
gi 530387683  1657 PA-PGAGGQALASDSEEADEVPE 1678
Cdd:TIGR01645  448 LAiMGEAAAALALEPKKKKKEKE 470
COG5493 COG5493
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ...
368-444 2.01e-03

Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only];


Pssm-ID: 444244 [Multi-domain]  Cd Length: 239  Bit Score: 41.89  E-value: 2.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530387683  368 IRDLREEVEKLREQLTKAE--AMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG 444
Cdd:COG5493    36 LEELLERLEKLEEQMRKWEeqLRKLEEEIKKLREQVRKLEEDVKRLEEQERKLEEAMAEHSELREELMKLIKRLERSIG 114
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
368-432 2.49e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683  368 IRDLREEVEKLREQLTKAEAMKS--PELKDRLEESEKLIQEMtvtwEEKLRKTEEIAQERQKQLESL 432
Cdd:PRK03918  216 LPELREELEKLEKEVKELEELKEeiEELEKELESLEGSKRKL----EEKIRELEERIEELKKEIEEL 278
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
611-760 7.30e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  611 LNSLEQQHE--EEKRSALERQRlmyeHELEQLRRRLSPEKQNCRSMDRFSFHS---PSAQQRLRQWAEEREATLNNS--L 683
Cdd:COG4913   612 LAALEAELAelEEELAEAEERL----EALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSddL 687
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683  684 MRLREQIVKANLLVREANYIAEELDKRteykvtlqipASSLDANRKR-GSLLSEPAIQVRRKGKGKQIWSLEKLDNRL 760
Cdd:COG4913   688 AALEEQLEELEAELEELEEELDELKGE----------IGRLEKELEQaEEELDELQDRLEAAEDLARLELRALLEERF 755
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
4-360 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 602.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNLSKGDARGQPKVFAYDHCFWSMDeSVKEKYAGQDIVFKC 82
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLkNPKQADKNNKATREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  163 DPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSG 240
Cdd:cd01365   160 NPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  241 TSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01365   240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSFIPYRDSVLTWLLKENL 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 530387683  319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:cd01365   320 GGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
6-360 1.71e-156

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 482.07  E-value: 1.71e-156
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683      6 VKVAVRIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGE 85
Cdd:smart00129    2 IRVVVRVRPLNKREKSRKSPSVVPFPDKV----GKTLTVRSPKNRQGEKKFTFDKVF---DAT-----ASQEDVFEETAA 69
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683     86 NILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTqKEENEEQSFKVEVSYMEIYNEKVRDLLDPk 165
Cdd:smart00129   70 PLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP- 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    166 gSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSgeK 245
Cdd:smart00129  148 -SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSG--K 224
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    246 VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSagknKNKFVPYRDSVLTWLLKDSLGGNSKTA 325
Cdd:smart00129  225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTL 300
                           330       340       350
                    ....*....|....*....|....*....|....*
gi 530387683    326 MVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:smart00129  301 MIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-353 6.53e-149

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 461.27  E-value: 6.53e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    11 RIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFWSmdesvkekYAGQDIVFKCLGENILQN 90
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVD----SETVESSHLTNKNRTKTFTFDKVFDP--------EATQEDVYEETAKPLVES 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    91 AFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQ- 169
Cdd:pfam00225   69 VLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKr 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   170 TLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGeKVGKL 249
Cdd:pfam00225  148 KLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   250 SLVDLAGSERATKTGAA-GDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVA 328
Cdd:pfam00225  227 NLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIA 301
                          330       340
                   ....*....|....*....|....*
gi 530387683   329 TVSPAADNYDETLSTLRYADRAKHI 353
Cdd:pfam00225  302 NISPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
5-351 2.69e-142

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 443.24  E-value: 2.69e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    5 KVKVAVRIRPMNRRETDLhTKCVVDVDANK-VILNPvntnlsKGDARGQPKVFAYDHCFWSMdesvkekyAGQDIVFKCL 83
Cdd:cd00106     1 NVRVAVRVRPLNGREARS-AKSVISVDGGKsVVLDP------PKNRVAPPKTFAFDAVFDST--------STQEEVYEGT 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   84 GENILQNAFDGYNACIFAYGQTGSGKSYTMMGTAD-QPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd00106    66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPeQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  163 DPKgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHtlYDVKSGTS 242
Cdd:cd00106   146 SPV-PKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQ--RNREKSGE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd00106   223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----GQNKHIPYRDSKLTRLLQDSLGGNS 297
                         330       340
                  ....*....|....*....|....*....
gi 530387683  323 KTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd00106   298 KTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
6-353 1.40e-119

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 380.65  E-value: 1.40e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    6 VKVAVRIRPMNRRETDLHTKCVVDVDankVILNPVNTNLSKGDARGQPKVFAYDHCFwsmDESVKEkYAGQDIVFKCLGE 85
Cdd:cd01371     3 VKVVVRCRPLNGKEKAAGALQIVDVD---EKRGQVSVRNPKATANEPPKTFTFDAVF---DPNSKQ-LDVYDETARPLVD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   86 NILQnafdGYNACIFAYGQTGSGKSYTMMGTADQP---GLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01371    76 SVLE----GYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQ-FLVRVSYLEIYNEEIRDLL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  163 DpKGSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTlYDVKSGTS 242
Cdd:cd01371   151 G-KDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECS-EKGEDGEN 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd01371   229 HIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----GKSTHIPYRDSKLTRLLQDSLGGNS 303
                         330       340       350
                  ....*....|....*....|....*....|.
gi 530387683  323 KTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01371   304 KTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
5-355 5.00e-112

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 359.22  E-value: 5.00e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVILNpvntnLSKGDARgqPKVFAYDHCFwSMDESvkekyagQDIVFKCLg 84
Cdd:cd01366     3 NIRVFCRVRPLLPSEENEDTSHITFPDEDGQTIE-----LTSIGAK--QKEFSFDKVF-DPEAS-------QEDVFEEV- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLLDP 164
Cdd:cd01366    67 SPLVQSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLLAP 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  165 KGSRQT-LKVREHSVLGP-YVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLthtlydvkSGT- 241
Cdd:cd01366   147 GNAPQKkLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--------SGRn 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  242 --SGEK-VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAdqsagkNKNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01366   219 lqTGEIsVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------QKQSHIPYRNSKLTYLLQDSL 292
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 530387683  319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVN 355
Cdd:cd01366   293 GGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
6-353 6.76e-111

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 356.65  E-value: 6.76e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    6 VKVAVRIRPMNRRETDLHTKCVVDV-DANKVILNP----------VNTNLSKGDARGQPKVFAYDHCFwsmDEsvkekYA 74
Cdd:cd01370     2 LTVAVRVRPFSEKEKNEGFRRIVKVmDNHMLVFDPkdeedgffhgGSNNRDRRKRRNKELKYVFDRVF---DE-----TS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   75 GQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIY 154
Cdd:cd01370    74 TQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK-DEKEFEVSMSYLEIY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  155 NEKVRDLLDPKGSRqtLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTl 234
Cdd:cd01370   153 NETIRDLLNPSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQ- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  235 YDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsaGKNKNKFVPYRDSVLTWLL 314
Cdd:cd01370   230 DKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD---PGKKNKHIPYRDSKLTRLL 306
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 530387683  315 KDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01370   307 KDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
3-353 2.23e-110

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 354.33  E-value: 2.23e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    3 DSKVKVAVRIRPMNRRETDLHTKCVVDVDankvilnPVNTNLSKGDARGqpKVFAYDHCFwSMDesvkekyAGQDIVFKC 82
Cdd:cd01369     1 ECNIKVVCRFRPLNELEVLQGSKSIVKFD-------PEDTVVIATSETG--KTFSFDRVF-DPN-------TTQEDVYNF 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQP---GLIPRLCSGLFERTQKEeNEEQSFKVEVSYMEIYNEKVR 159
Cdd:cd01369    64 AAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSM-DENLEFHVKVSYFEIYMEKIR 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  160 DLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTlyDVKS 239
Cdd:cd01369   143 DLLDV--SKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE--NVET 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  240 GTSgeKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLG 319
Cdd:cd01369   219 EKK--KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----GKKTHIPYRDSKLTRILQDSLG 291
                         330       340       350
                  ....*....|....*....|....*....|....
gi 530387683  320 GNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01369   292 GNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
4-353 6.00e-110

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 353.56  E-value: 6.00e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANK--VILnpvntnlskgdarGQPKVFAYDHCFWSMDEsvkekyagQDIVFK 81
Cdd:cd01372     1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEpqVTV-------------GTDKSFTFDYVFDPSTE--------QEEVYN 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   82 CLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA------DQPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYN 155
Cdd:cd01372    60 TCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYtaeedeEQVGIIPRAIQHIFKKIEKKKDTFE-FQLKVSFLEIYN 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  156 EKVRDLLDPKG-SRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTL 234
Cdd:cd01372   139 EEIRDLLDPETdKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTK 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  235 YDVKSGTSGEK------VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgknKNKFVPYRDS 308
Cdd:cd01372   219 KNGPIAPMSADdknstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESK---KGAHVPYRDS 295
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 530387683  309 VLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01372   296 KLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
5-353 9.98e-109

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 349.32  E-value: 9.98e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNlskgdargqpkvFAYDHCFwSMDESVKEkyagqdiVFKCL 83
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIYLvEPPSTS------------FTFDHVF-GGDSTNRE-------VYELI 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   84 GENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQkeENEEQSFKVEVSYMEIYNEKVRDLLD 163
Cdd:cd01374    61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQ--DTPDREFLLRVSYLEIYNEKINDLLS 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  164 PKGsrQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGtSG 243
Cdd:cd01374   139 PTS--QNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEE-GT 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  244 EKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALadqSAGKnKNKFVPYRDSVLTWLLKDSLGGNSK 323
Cdd:cd01374   216 VRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKL---SEGK-VGGHIPYRDSKLTRILQPSLGGNSR 291
                         330       340       350
                  ....*....|....*....|....*....|
gi 530387683  324 TAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01374   292 TAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
6-362 1.35e-100

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 327.54  E-value: 1.35e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    6 VKVAVRIRPMNRRETDL-HTKCVVDVDANKVILNPVntnlskgdargQPKVFAYDHcfwsmdesVKEKYAGQDIVFKCLG 84
Cdd:cd01373     3 VKVFVRIRPPAEREGDGeYGQCLKKLSSDTLVLHSK-----------PPKTFTFDH--------VADSNTNQESVFQSVG 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQP--------GLIPRLCSGLFERTQKEEN---EEQSFKVEVSYMEI 153
Cdd:cd01373    64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQREKEkagEGKSFLCKCSFLEI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  154 YNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHt 233
Cdd:cd01373   144 YNEQIYDLLDP--ASRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  234 lYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKNKNkfVPYRDSVLTWL 313
Cdd:cd01373   221 -WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRH--VCYRDSKLTFL 297
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 530387683  314 LKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNED 362
Cdd:cd01373   298 LRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
3-362 4.93e-95

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 311.57  E-value: 4.93e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    3 DSKVKVAVRIRPMNRRETDLHTKCVVDV-DANKVILNPVNTNLSKGDArgqpKVFAYDHCFWSmdesvkekYAGQDIVFK 81
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVdPVRKEVSVRTGGLADKSST----KTYTFDMVFGP--------EAKQIDVYR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   82 CLGENILQNAFDGYNACIFAYGQTGSGKSYTMMG-----------TADQPGLIPRLCSGLFERTqkeENEEQSFKVEVSY 150
Cdd:cd01364    69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKL---EDNGTEYSVKVSY 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  151 MEIYNEKVRDLLDPKGS-RQTLKVREHS--VLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFK 227
Cdd:cd01364   146 LEIYNEELFDLLSPSSDvSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  228 ITLthtlYDVKSGTSGE---KVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagknKNKFVP 304
Cdd:cd01364   226 ITI----HIKETTIDGEelvKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------RAPHVP 295
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683  305 YRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNED 362
Cdd:cd01364   296 YRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
50-439 8.55e-95

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 318.99  E-value: 8.55e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   50 RGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSG 129
Cdd:COG5059    52 KSKEGTYAFDKVF---GPS-----ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKE 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  130 LFERTQKEeNEEQSFKVEVSYMEIYNEKVRDLLDPKgsRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRT 209
Cdd:COG5059   124 LFSKLEDL-SMTKDFAVSISYLEIYNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  210 VAATNMNEESSRSHAVFKITLTHtlYDVKSGTSGEkvGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISA 289
Cdd:COG5059   201 TASTEINDESSRSHSIFQIELAS--KNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINA 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  290 LADqsagKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE-----DPN 364
Cdd:COG5059   277 LGD----KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdssREI 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  365 ARIIRDL---REEVEKLREQLTKAEAMKSPELKDR--LEESEKLIQEMTVT---WEEKLRKTEEIAQERQKQLESLGISL 436
Cdd:COG5059   353 EEIKFDLsedRSEIEILVFREQSQLSQSSLSGIFAymQSLKKETETLKSRIdliMKSIISGTFERKKLLKEEGWKYKSTL 432

                  ...
gi 530387683  437 QSS 439
Cdd:COG5059   433 QFL 435
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
5-351 4.83e-79

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 265.41  E-value: 4.83e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    5 KVKVAVRIRPMNRRETDLHTK-CVVDVDANKVILNPVNTNLSKGDARG---QPKVFAYDHCFwSMDESVKEKYAGqdiVF 80
Cdd:cd01368     2 PVKVYLRVRPLSKDELESEDEgCIEVINSTTVVLHPPKGSAANKSERNggqKETKFSFSKVF-GPNTTQKEFFQG---TA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   81 KCLGENILQnafdGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFertqkeeNEEQSFKVEVSYMEIYNEKVRD 160
Cdd:cd01368    78 LPLVQDLLH----GKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIF-------NSIGGYSVFVSYIEIYNEYIYD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  161 LLDPKGS-----RQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITL----T 231
Cdd:cd01368   147 LLEPSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLvqapG 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  232 HTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAdQSAGKNKNKFVPYRDSVLT 311
Cdd:cd01368   227 DSDGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLR-ENQLQGTNKMVPFRDSKLT 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 530387683  312 WLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01368   306 HLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
PLN03188 PLN03188
kinesin-12 family protein; Provisional
3-379 3.32e-77

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 282.59  E-value: 3.32e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    3 DSKVKVAVRIRPMNRRETDlhtkcvvDVDANKVILNPVNTNlskgdarGQpkVFAYDhcfwsmdeSVKEKYAGQDIVFKC 82
Cdd:PLN03188   97 DSGVKVIVRMKPLNKGEEG-------EMIVQKMSNDSLTIN-------GQ--TFTFD--------SIADPESTQEDIFQL 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA----------DQPGLIPRLCSGLFERTQKEE----NEEQSFKVEV 148
Cdd:PLN03188  153 VGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRC 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  149 SYMEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKI 228
Cdd:PLN03188  233 SFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  229 TLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgKNKNKFVPYRDS 308
Cdd:PLN03188  311 VVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQ-TGKQRHIPYRDS 389
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683  309 VLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE----DPN--ARIIRDLREEVEKLR 379
Cdd:PLN03188  390 RLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
5-351 8.14e-75

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 252.89  E-value: 8.14e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    5 KVKVAVRIRPMNRREtdlHTKCVVDVDaNKVILNPVNTNLSKGDARGQPKVFAYdhcfwSMDESVKEkyAGQDIVFKCLG 84
Cdd:cd01375     1 KVQAFVRVRPTDDFA---HEMIKYGED-GKSISIHLKKDLRRGVVNNQQEDWSF-----KFDGVLHN--ASQELVYETVA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTAD---QPGLIPRLCSGLFErtQKEENEEQSFKVEVSYMEIYNEKVRDL 161
Cdd:cd01375    70 KDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTEnykHRGIIPRALQQVFR--MIEERPTKAYTVHVSYLEIYNEQLYDL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  162 LDPK----GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITL---THTL 234
Cdd:cd01375   148 LSTLpyvgPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeahSRTL 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  235 YDVKSGTSgekvgKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQsagknKNKFVPYRDSVLTWLL 314
Cdd:cd01375   228 SSEKYITS-----KLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDK-----DRTHVPFRQSKLTHVL 297
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 530387683  315 KDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01375   298 RDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
5-351 2.28e-74

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 251.06  E-value: 2.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVIlnPVNTNLSKGDARGQPKV--FAYDHCFwsmDESVKekyagQDIVFKC 82
Cdd:cd01367     1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTL--IVHEPKLKVDLTKYIENhtFRFDYVF---DESSS-----NETVYRS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMG----TADQPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKV 158
Cdd:cd01367    71 TVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDN-LGVTVSFFEIYGGKV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  159 RDLLDPKgsrQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLthtlydvK 238
Cdd:cd01367   150 FDLLNRK---KRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-------R 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  239 SGTSGEKVGKLSLVDLAGSERATKTGAAG-DRLKEGSNINKSLTTLGLVISALADQSAgknknkFVPYRDSVLTWLLKDS 317
Cdd:cd01367   220 DRGTNKLHGKLSFVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKA------HIPFRGSKLTQVLKDS 293
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 530387683  318 L-GGNSKTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01367   294 FiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
6-351 6.34e-69

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 235.09  E-value: 6.34e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683    6 VKVAVRIRPMNRRETDLHTKCVVDvdankvILNPVNTNLSKGDARGQPKVFAYDHcFWSMDESVKEKYAGQdivFKClge 85
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVS------GIDSCSVELADPRNHGETLKYQFDA-FYGEESTQEDIYARE---VQP--- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   86 nILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEneeQSFKVEVSYMEIYNEKVRDLLDPK 165
Cdd:cd01376    69 -IVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA---WALSFTMSYLEIYQEKILDLLEPA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  166 GSRqtLKVRE---HSVLGPyvdGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVksgTS 242
Cdd:cd01376   145 SKE--LVIREdkdGNILIP---GLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLA---PF 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALadqsagKNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd01376   217 RQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------NKNLPRIPYRDSKLTRLLQDSLGGGS 290
                         330       340
                  ....*....|....*....|....*....
gi 530387683  323 KTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01376   291 RCIMVANIAPERTFYQDTLSTLNFAARSR 319
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
447-545 4.13e-68

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 224.02  E-value: 4.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22730     1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80
                          90
                  ....*....|....*....
gi 530387683  527 HHGDRILWGNNHFFRLNLP 545
Cdd:cd22730    81 HHGDRILWGNNHFFRINLP 99
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
447-545 2.40e-59

forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438758 [Multi-domain]  Cd Length: 101  Bit Score: 199.06  E-value: 2.40e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANS---QDIQLCGMGILPEHCIIDItSEGQVMLTPQKNTRTFVNGSSVSSP 523
Cdd:cd22706     1 KYYLVNLNADPSLNELLVYYLKEHTLIGRSDAptqQDIQLSGLGIQPEHCIITI-ENEDVYLTPLEGARTCVNGSIVTEK 79
                          90       100
                  ....*....|....*....|..
gi 530387683  524 IQLHHGDRILWGNNHFFRLNLP 545
Cdd:cd22706    80 TQLRHGDRILWGNNHFFRLNCP 101
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
447-550 1.41e-55

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438781 [Multi-domain]  Cd Length: 109  Bit Score: 188.56  E-value: 1.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22729     1 KCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCVIDIAADGDVTLTPKENARTCVNGTLVCSVTQL 80
                          90       100
                  ....*....|....*....|....
gi 530387683  527 HHGDRILWGNNHFFRLNLPKKKKK 550
Cdd:cd22729    81 WHGDRILWGNNHFFRINLPKRKRR 104
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
450-543 7.81e-34

forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438757 [Multi-domain]  Cd Length: 101  Bit Score: 126.19  E-value: 7.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  450 LVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22705     4 LVNLNEDPLMSECLLYYIKPgITRVGRADAdvpQDIQLSGTHILEEHCTFE-NEDGVVTLEPCEGALTYVNGKRVTEPTR 82
                          90
                  ....*....|....*...
gi 530387683  526 LHHGDRILWGNNHFFRLN 543
Cdd:cd22705    83 LKTGSRVILGKNHVFRFN 100
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
450-545 3.90e-31

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 118.52  E-value: 3.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  450 LVNLNADPALNELLVYYLKE-HTLIGS--ANSQ-DIQLCGMGILPEHCIIdITSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22707    10 LVNLNEDPQLSEMLLYMLKEgQTRVGRskASSShDIQLSGALIADDHCTI-ENNGGKVTIIPVGDAETYVNGELISEPTV 88
                          90       100
                  ....*....|....*....|
gi 530387683  526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22707    89 LHHGDRVILGGDHYFRFNHP 108
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
1683-1746 3.22e-30

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 114.42  E-value: 3.22e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530387683  1683 GEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRV 1746
Cdd:pfam01302    2 GDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
448-545 1.55e-28

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 110.77  E-value: 1.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  448 CFLVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIdITSEGQVMLTPQKNT-RTFVNGSSVSS 522
Cdd:cd22709     1 PHLLNLNEDPQLSGVIVHFLQEgETTIGRADAepePDIVLSGLSIQKQHAVI-TNTDGKVTIEPVSPGaKVIVNGVPVTG 79
                          90       100
                  ....*....|....*....|...
gi 530387683  523 PIQLHHGDRILWGNNHFFRLNLP 545
Cdd:cd22709    80 ETELHHLDRVILGSNHLYVFVGP 102
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
58-289 3.76e-28

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 112.44  E-value: 3.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   58 YDHCFWSMDeSVKEKYAGQDIVFKcLGENILQNAFDGYN-ACIFAYGQTGSGKSYTMMGtadqpgLIPRLCSGLFERTQK 136
Cdd:cd01363    15 RDSKIIVFY-RGFRRSESQPHVFA-IADPAYQSMLDGYNnQSIFAYGESGAGKTETMKG------VIPYLASVAFNGINK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  137 EENEEQsfkvevsymeiynekvrdlldpkgsrqtlkvrehsvlgpyvDGLSKLAVTSYKDIESLMSEGNKSRTvAATNMN 216
Cdd:cd01363    87 GETEGW-----------------------------------------VYLTEITVTLEDQILQANPILEAFGN-AKTTRN 124
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530387683  217 EESSRSHAVFKItlthtlydvksgtsgekvgklsLVDLAGSERatktgaagdrlkegsnINKSLTTLGLVISA 289
Cdd:cd01363   125 ENSSRFGKFIEI----------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
1683-1747 5.85e-26

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 102.28  E-value: 5.85e-26
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683   1683 GEFVTVGAH-KTGVVRYVGPADFQEGTWVGVELDLP-SGKNDGSIGGKQYFRCNPGYGLLVRPSRVR 1747
Cdd:smart01052    2 GDRVEVGGGgRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
Kinesin_assoc pfam16183
Kinesin-associated;
357-469 5.41e-25

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 103.77  E-value: 5.41e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   357 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 391
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   392 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 454
Cdd:pfam16183   81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160
                          170
                   ....*....|....*
gi 530387683   455 ADPALNELLVYYLKE 469
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
450-547 1.62e-23

forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438779 [Multi-domain]  Cd Length: 110  Bit Score: 97.03  E-value: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  450 LVNLNADPALNELLVYYLKEH-TLIGSANS---QDIQLCGMGILPEHCII--DITSEGQVMLT--PQKNTRTFVNGSSVS 521
Cdd:cd22727     5 LVNLNEDPLMSECLLYYIKDGiTRVGQADAerrQDIVLSGAHIKEEHCIFrsERNNNGEVIVTlePCERSETYVNGKRVV 84
                          90       100
                  ....*....|....*....|....*.
gi 530387683  522 SPIQLHHGDRILWGNNHFFRLNLPKK 547
Cdd:cd22727    85 QPVQLRSGNRIIMGKNHVFRFNHPEQ 110
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
450-554 4.25e-20

forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438778 [Multi-domain]  Cd Length: 115  Bit Score: 87.29  E-value: 4.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  450 LVNLNADPALNELLVYYLKEH-TLIGSANS---QDIQLCGMGILPEHCII--DITSEGQ--VMLTPQKNTRTFVNGSSVS 521
Cdd:cd22726     4 LVNLNEDPLMSECLLYYIKDGiTRVGREDAerrQDIVLSGHFIKEEHCIFrsDTRSGGEavVTLEPCEGADTYVNGKKVT 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 530387683  522 SPIQLHHGDRILWGNNHFFRLNLPKKKKKaERE 554
Cdd:cd22726    84 EPSILRSGNRIIMGKSHVFRFNHPEQARQ-ERE 115
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
5-162 3.68e-19

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 85.73  E-value: 3.68e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683     5 KVKVAVRIRPMNRREtdlhtkcvvdvdankVILNPVNTNLSKGDARGQPKVFAYDHCFwsmdesvkEKYAGQDIVFKCLg 84
Cdd:pfam16796   21 NIRVFARVRPELLSE---------------AQIDYPDETSSDGKIGSKNKSFSFDRVF--------PPESEQEDVFQEI- 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683    85 ENILQNAFDGYNACIFAYGQTGSGKSytmmgtadqPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKVRDLL 162
Cdd:pfam16796   77 SQLVQSCLDGYNVCIFAYGQTGSGSN---------DGMIPRAREQIFRFISSLKKGWK-YTIELQFVEIYNESSQDLL 144
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
450-543 1.65e-17

forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438780 [Multi-domain]  Cd Length: 102  Bit Score: 79.53  E-value: 1.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  450 LVNLNADPALNELLVYYLKEH-TLIGSANSqDIQLCGMGILPEHCII--DITSEGQVMLT--PQKNTRTFVNGSSVSSPI 524
Cdd:cd22728     4 LVNLNEDPLMSECLLYHIKDGvTRVGQVDV-DIKLSGQFIREQHCLFrsIPNPSGEVVVTlePCEGAETYVNGKQVTEPL 82
                          90
                  ....*....|....*....
gi 530387683  525 QLHHGDRILWGNNHFFRLN 543
Cdd:cd22728    83 VLKSGNRIVMGKNHVFRFN 101
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
450-545 3.82e-17

forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438760 [Multi-domain]  Cd Length: 109  Bit Score: 78.85  E-value: 3.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  450 LVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22708    11 LIGIDDDLLSTGVVLYHLKEgKTRIGREDApqeQDIVLDGEDIEAEHCIIE-NVGGVVTLHPLPGALCAVNGQVITQPTR 89
                          90       100
                  ....*....|....*....|
gi 530387683  526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22708    90 LTQGDVILLGKTNMFRFNHP 109
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
448-545 2.77e-15

forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438763 [Multi-domain]  Cd Length: 106  Bit Score: 73.51  E-value: 2.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  448 CFLVNLNADPALNellvYYLKEH------TLIGSANS-----QDIQLCGMGILPEHCIIDITsEGQVMLTP-QKNTRTFV 515
Cdd:cd22711     2 PYLLELSPDGSDR----DKPRRHrlqpnvTEVGSERSpansgQFIQLFGPDILPRHCVITHM-EGVVTVTPaSQDAETYV 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 530387683  516 NGSSVSSPIQLHHGDRILWGNNHFFRLNLP 545
Cdd:cd22711    77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
468-539 1.17e-13

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 68.39  E-value: 1.17e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530387683  468 KEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTP-QKNTRTFVNGSSVSSPIQLHHGDRILWGNNHF 539
Cdd:cd22673    20 KKSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGKAYLENlSTTNPTLVNGKAIEKSAELKDGDVITIGGRSF 92
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
756-802 1.85e-13

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


Pssm-ID: 463574  Cd Length: 43  Bit Score: 66.09  E-value: 1.85e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 530387683   756 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 802
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
438-549 2.34e-13

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438765  Cd Length: 120  Bit Score: 68.12  E-value: 2.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  438 SSGIKVGDDKCFLVNLNADPALNELLVYYLKE-HTLIGSANSQDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNtRTFVN 516
Cdd:cd22713     7 GKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEgKTTIGTAASDIISLQGPGVEPEHCYIE-NINGTVTLYPCGN-LCSVD 84
                          90       100       110
                  ....*....|....*....|....*....|...
gi 530387683  517 GSSVSSPIQLHHGDRILWGNNHFFRLNLPKKKK 549
Cdd:cd22713    85 GLPITEPTRLTQGCMICLGRSNYFRFNHPAEAK 117
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
1683-1752 4.58e-13

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 74.34  E-value: 4.58e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1683 GEFVTVGAHKtGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGP 1752
Cdd:COG5244     7 NDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGN 75
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
450-550 1.70e-12

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 65.73  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  450 LVNLNADPALNELLVYYLKE-HTLIG---SANSQDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22732    11 LIGIDDDLLSTGIILYHLKEgRTYVGrddATTEQDIVLHGLDLESEHCIFE-NLNGTVTLIPLNGAQCSVNGVQITEATQ 89
                          90       100
                  ....*....|....*....|....*
gi 530387683  526 LHHGDRILWGNNHFFRLNLPKKKKK 550
Cdd:cd22732    90 LNQGAVILLGRTNMFRFNHPKEAAK 114
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
471-534 3.66e-11

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 60.28  E-value: 3.66e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530387683   471 TLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNT-RTFVNGSSVSS-PIQLHHGDRILW 534
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTnGTFVNGQRLGPePVRLKDGDVIRL 66
PHA03247 PHA03247
large tegument protein UL36; Provisional
1422-1660 5.10e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.43  E-value: 5.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1422 GIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFV-PQMPKLLKSLFPVRDEKRGKRPSPLAHQAQPEmGPDVLVQTm 1500
Cdd:PHA03247 2493 GAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVhPRMLTWIRGLEELASDDAGDPPPPLPPAAPPA-APDRSVPP- 2570
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1501 gapalkicDKPAKVPSPPpviAVTAVTPAPEAqdgPPSPLSEASsgyfshsvstatlsdalgPGLDAAAPPGSMPTAPeA 1580
Cdd:PHA03247 2571 --------PRPAPRPSEP---AVTSRARRPDA---PPQSARPRA------------------PVDDRGDPRGPAPPSP-L 2617
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1581 EPEAPISHPPPPTAVP-AEEPPGPQQLVSPGRERPDlEAPAPGSPFRVRRVRA--------SELRSFSRMLAGDPGCSPG 1651
Cdd:PHA03247 2618 PPDTHAPDPPPPSPSPaANEPDPHPPPTVPPPERPR-DDPAPGRVSRPRRARRlgraaqasSPPQRPRRRAARPTVGSLT 2696

                  ....*....
gi 530387683 1652 AEGNAPAPG 1660
Cdd:PHA03247 2697 SLADPPPPP 2705
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
449-539 5.12e-11

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 60.75  E-value: 5.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  449 FLVNLNADPALNELLVYylKEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNT-RTFVNGSSVSSPIQLH 527
Cdd:cd00060     1 RLIVLDGDGGGREFPLT--KGVVTIGRSPDCDIVLDDPSVSRRHARIEVD-GGGVYLEDLGSTnGTFVNGKRITPPVPLQ 77
                          90
                  ....*....|..
gi 530387683  528 HGDRILWGNNHF 539
Cdd:cd00060    78 DGDVIRLGDTTF 89
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
450-545 3.56e-10

forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438783 [Multi-domain]  Cd Length: 119  Bit Score: 59.02  E-value: 3.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  450 LVNLNADPALNELLVYYLKEHTL-IGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22731    11 LIAMDDDILSTGVVLYHLREGTTkIGRSDSeqeQDIVLQGPWIERDHCMIH-NECGVVTLRPAQGAQCTVNGREVTESCR 89
                          90       100
                  ....*....|....*....|
gi 530387683  526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22731    90 LSQGAVIVLGKTHKFRFNHP 109
PHA03247 PHA03247
large tegument protein UL36; Provisional
1417-1662 4.54e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 65.34  E-value: 4.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1417 TTVSRGIAPAPALSVSPqnNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPlahqaqPEMGPDVL 1496
Cdd:PHA03247 2738 APAPPAVPAGPATPGGP--ARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSP------WDPADPPA 2809
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1497 VQTMGAPALKICDKPAKvPSPPPviavTAVTPAPEAQDGPPSPLSEASSGYF-----------SHSVSTATLSDALGPGL 1565
Cdd:PHA03247 2810 AVLAPAAALPPAASPAG-PLPPP----TSAQPTAPPPPPGPPPPSLPLGGSVapggdvrrrppSRSPAAKPAAPARPPVR 2884
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1566 DAAAPPGSMPTAPEAEPEAPISHPPPPtavPAEEPPGPQqlvsPGRERPDLEAPAPGSPFRVRRVRASElrsfsrmlaGD 1645
Cdd:PHA03247 2885 RLARPAVSRSTESFALPPDQPERPPQP---QAPPPPQPQ----PQPPPPPQPQPPPPPPPRPQPPLAPT---------TD 2948
                         250
                  ....*....|....*..
gi 530387683 1646 PGCSPGAEGNAPAPGAG 1662
Cdd:PHA03247 2949 PAGAGEPSGAVPQPWLG 2965
PHA03247 PHA03247
large tegument protein UL36; Provisional
1459-1678 8.59e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 64.19  E-value: 8.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1459 PQMPKLLKSLFPVRDEKRGKRPSPLAHQAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAV------TPAPEA 1532
Cdd:PHA03247 2683 PRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATpggparPARPPT 2762
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1533 QDGPPSPLSEAS-----------SGYFSHSVSTATLSDALGP--------GLDAAAPPGSMPTAPEAEPEAPISHPPPPT 1593
Cdd:PHA03247 2763 TAGPPAPAPPAApaagpprrltrPAVASLSESRESLPSPWDPadppaavlAPAAALPPAASPAGPLPPPTSAQPTAPPPP 2842
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1594 AVPAEEPPGPQQLVSPG---RERPDLEAPA--PGSPFR--VRRVRASELRSFSRMLAGDPgcsPGAEgNAPAPGAGGQAL 1666
Cdd:PHA03247 2843 PGPPPPSLPLGGSVAPGgdvRRRPPSRSPAakPAAPARppVRRLARPAVSRSTESFALPP---DQPE-RPPQPQAPPPPQ 2918
                         250
                  ....*....|..
gi 530387683 1667 ASDSEEADEVPE 1678
Cdd:PHA03247 2919 PQPQPPPPPQPQ 2930
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
446-540 9.89e-10

forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438764 [Multi-domain]  Cd Length: 120  Bit Score: 58.08  E-value: 9.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  446 DKCFLVNLNADPALNELLVYYLKEHT-LIGS----ANSQDIQLCGMGILPEHCII--------------DITSEGQVMLT 506
Cdd:cd22712     2 DYPYLLTLRGFSPKQDLLVYPLLEQViLVGSrtegARKVDISLRAPDILPQHCWIrrkpeplsddedsdKESADYRVVLS 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 530387683  507 PQKNTRTFVNGSSVSSPIQLHHGDRILWGNNHFF 540
Cdd:cd22712    82 PLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLF 115
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1515-1673 1.82e-09

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 62.88  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1515 PSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTA 1594
Cdd:PHA03307  114 PDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEP 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1595 V----PAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRmlagDPGCSPGAEGNAPAPGAGGQALASDS 1670
Cdd:PHA03307  194 PpstpPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE----SSGCGWGPENECPLPRPAPITLPTRI 269

                  ...
gi 530387683 1671 EEA 1673
Cdd:PHA03307  270 WEA 272
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1479-1629 1.99e-09

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 62.70  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1479 RPSPLAHQAQPEMGPDVLVQTMGAPALKICDKPAK---VPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTA 1555
Cdd:PRK07764  646 GVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAApppAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAA 725
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530387683 1556 TLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRR 1629
Cdd:PRK07764  726 QGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRR 799
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1479-1661 6.47e-09

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 61.05  E-value: 6.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1479 RPSPLAHQAQP---EMGPDVLVQTMGAPALKICDKPAKVPSPPPVIA-VTAVTPAPEAQDGPPSPLSEASSGYFSHSVST 1554
Cdd:PRK12323  364 RPGQSGGGAGPataAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPaAAAAARAVAAAPARRSPAPEALAAARQASARG 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1555 ATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDlEAPAPGSPFRVRRVRASE 1634
Cdd:PRK12323  444 PGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPP-EFASPAPAQPDAAPAGWV 522
                         170       180
                  ....*....|....*....|....*..
gi 530387683 1635 LRSFSRMLAGDPgcSPGAEGNAPAPGA 1661
Cdd:PRK12323  523 AESIPDPATADP--DDAFETLAPAPAA 547
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
1511-1634 1.63e-08

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 59.34  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGyfshsvstatlsdalgpglDAAAPPGSMPTAPEAEPEAPISHPP 1590
Cdd:PRK14951  389 PAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPA-------------------PVAAPAAAAPAAAPAAAPAAVALAP 449
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 530387683 1591 PPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASE 1634
Cdd:PRK14951  450 APPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1475-1678 3.22e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 58.84  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1475 KRGKRPSPLAHQAQPEMGPdvlvqtmgAPALKICDKPAKVPSPPpviAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVST 1554
Cdd:PRK07764  601 PAPASSGPPEEAARPAAPA--------APAAPAAPAPAGAAAAP---AEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1555 ATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAV------PAEEPPGPQQLVSPGRERPDLEAPAPGSPfrvr 1628
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPagqaddPAAQPPQAAQGASAPSPAADDPVPLPPEP---- 745
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 530387683 1629 rvraselrSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPE 1678
Cdd:PRK07764  746 --------DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAE 787
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1511-1778 3.51e-08

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 59.03  E-value: 3.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPVIAVTAVTPAPEAQ---DGPPSPLSEASSGYFSHSVS------TATLSDALGPGLDAAAPPGSMPTAPEAE 1581
Cdd:PHA03307   80 PANESRSTPTWSLSTLAPASPARegsPTPPGPSSPDPPPPTPPPASpppspaPDLSEMLRPVGSPGPPPAASPPAAGASP 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1582 PEAPISHPPPPTA------VPAEEPPGPqqlvSPGRERPDLEAPAPGSPfrvrrvRASELRSFSRMLAGDPGCSPGAEGN 1655
Cdd:PHA03307  160 AAVASDAASSRQAalplssPEETARAPS----SPPAEPPPSTPPAAASP------RPPRRSSPISASASSPAPAPGRSAA 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1656 APAPGAGGQALASDSEEADEVPEWLREGEFVTVGAHKTGVVRYVGpadfqegtWVGVELDLPSGKNDGSIGGK--QYFRC 1733
Cdd:PHA03307  230 DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASG--------WNGPSSRPGPASSSSSPRERspSPSPS 301
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 530387683 1734 NPGYGLLVRPSRVRRATGPVRRRSTGLRLGAPEARRSATLSGSAT 1778
Cdd:PHA03307  302 SPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPS 346
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
79-290 5.79e-08

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 57.83  E-value: 5.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683   79 VFKCLGENIlQNAFDGynacIFAYGQTGSGKSYTMMgtaDQPGLIPRLC-SGLFERTQKEENEEQSFKVEVSYMEIY-NE 156
Cdd:COG5059   370 VFREQSQLS-QSSLSG----IFAYMQSLKKETETLK---SRIDLIMKSIiSGTFERKKLLKEEGWKYKSTLQFLRIEiDR 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  157 KVRDLLDPKGSRQTLKVREHSVLGPYVDGLSKLA-VTSYKDIESLMSegnKSRTVAATNMNEESSRSHAVFKitlthtly 235
Cdd:COG5059   442 LLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPeETSDRVESEKAS---KLRSSASTKLNLRSSRSHSKFR-------- 510
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530387683  236 DVKSG-TSGEKVGKLSLVDLAGSERaTKTGAAGDRLKEGSNINKSLTTLGLVISAL 290
Cdd:COG5059   511 DHLNGsNSSTKELSLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
PHA03378 PHA03378
EBNA-3B; Provisional
1371-1665 1.61e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 56.61  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1371 GKGKLSRRSISSPNVNRLSGSrqdlIPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPQNNHSPDPGLSNLAASY 1450
Cdd:PHA03378  568 GLGPLQIQPLTSPTTSQLASS----APSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITF 643
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1451 LNPVKSFVPQMPKLLKSLFP---VRDEKRGKRPSPLAHQAQ------------PEMGPDVLVQTMGAPALKICDKPAKVP 1515
Cdd:PHA03378  644 NVLVFPTPHQPPQVEITPYKptwTQIGHIPYQPSPTGANTMlpiqwapgtmqpPPRAPTPMRPPAAPPGRAQRPAAATGR 723
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1516 SPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAV 1595
Cdd:PHA03378  724 ARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAG 803
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1596 PAEEPPGPQQLvsPGRERPDLEAPAPGSPFRVRRVRASeLRSFSRmlagdpGCSPGAEGNAPAPGAGGQA 1665
Cdd:PHA03378  804 PTSMQLMPRAA--PGQQGPTKQILRQLLTGGVKRGRPS-LKKPAA------LERQAAAGPTPSPGSGTSD 864
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1396-1621 2.62e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.93  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1396 IPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPqnnhSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEk 1475
Cdd:pfam03154  148 IPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPS----PPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ- 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1476 rgkrpSPLAHQAQPEMGPDVLVQTMGAPALKIcdKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLS-EASSGYFSHSVST 1554
Cdd:pfam03154  223 -----STAAPHTLIQQTPTLHPQRLPSPHPPL--QPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSlQTGPSHMQHPVPP 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1555 ATLSDA---------LGPGLDAAAPPGSMPTAPEAEPEAPISHPP-------PPTAVPAEEPPGPQ---QLVSPGRER-- 1613
Cdd:pfam03154  296 QPFPLTpqssqsqvpPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPreqplppAPLSMPHIKPPPTTpipQLPNPQSHKhp 375

                   ....*...
gi 530387683  1614 PDLEAPAP 1621
Cdd:pfam03154  376 PHLSGPSP 383
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
1221-1278 7.36e-07

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 463599  Cd Length: 149  Bit Score: 50.66  E-value: 7.36e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530387683  1221 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1278
Cdd:pfam12473   91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
1424-1621 8.11e-07

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 52.30  E-value: 8.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1424 APAPALSVS-PQNNHSPD--PG---LSNLAASYLNPvkSFVPqmPKLLKSLFPVRDEKRGKRPSplahqaQPEMGPDVLV 1497
Cdd:pfam15822   11 SPAKTSAVSnPKPGQPPQgwPGsnpWNNPSAPPAVP--SGLP--PSTAPSTVPFGPAPTGMYPS------IPLTGPSPGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1498 QTMGAPALKICDKPAKvPSPPPVIAvtavTPAPEAQDGPPS-PLSEASSGYFSHS--VSTATL-------SDALGPGLDA 1567
Cdd:pfam15822   81 PAPFPPSGPSCPPPGG-PYPAPTVP----GPGPIGPYPTPNmPFPELPRPYGAPTdpAAAAPSgpwgsmsSGPWAPGMGG 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 530387683  1568 AAPPGSMPTAPeaepeaPISHP-PPPTAVPAEEPPGPQQLVSPGRERPDLEAPAP 1621
Cdd:pfam15822  156 QYPAPNMPYPS------PGPYPaVPPPQSPGAAPPVPWGTVPPGPWGPPAPYPDP 204
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1425-1709 1.13e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.02  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1425 PAPALSVSPQNNHSPDPGLSNL-------AASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQAQPEMGPDVLV 1497
Cdd:PHA03307  172 AALPLSSPEETARAPSSPPAEPppstppaAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGP 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1498 QTM------GAPALKICDKPAKVPSPPPVIAVTAVTPAPE-AQDGPPSPLSEASSGyfshSVSTATLSDALGP----GLD 1566
Cdd:PHA03307  252 ENEcplprpAPITLPTRIWEASGWNGPSSRPGPASSSSSPrERSPSPSPSSPGSGP----APSSPRASSSSSSsresSSS 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1567 AAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPfRVRRVRASELRSFSRMLAgdP 1646
Cdd:PHA03307  328 STSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRP-TRRRARAAVAGRARRRDA--T 404
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530387683 1647 GCSPGAEGNAPAPGAGGQALASDSEEADEVPewlrEGE-FVTVGAHKTGVVRYVGPADFQEGTW 1709
Cdd:PHA03307  405 GRFPAGRPRPSPLDAGAASGAFYARYPLLTP----SGEpWPGSPPPPPGRVRYGGLGDSRPGLW 464
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
1479-1732 1.60e-06

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 52.76  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1479 RPSPLAHQAQPEMGPDVLVQTMGAPAlkICDKPAKvpsPPPVIAVTAVTPAPEAqDGPPSPLSEASSGYFSHSVSTATLS 1558
Cdd:COG5180   243 RSRPATVDAQPEMRPPADAKERRRAA--IGDTPAA---EPPGLPVLEAGSEPQS-DAPEAETARPIDVKGVASAPPATRP 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1559 DALGPG-LDAAAPPGSMPT-APEAEPEAPISHPPPPTAVPAEEP-----PGPQQLVSPGRE-------RPDLEAPAPGSP 1624
Cdd:COG5180   317 VRPPGGaRDPGTPRPGQPTeRPAGVPEAASDAGQPPSAYPPAEEavpgkPLEQGAPRPGSSggdgapfQPPNGAPQPGLG 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1625 FR---VRRVRASELRSFSRMLAGDPGCSPGAEGNAP--APGAGGQALASDSEEADEVPEwlregefVTVGAHKTGVVRYV 1699
Cdd:COG5180   397 RRgapGPPMGAGDLVQAALDGGGRETASLGGAAGGAgqGPKADFVPGDAESVSGPAGLA-------DQAGAAASTAMADF 469
                         250       260       270
                  ....*....|....*....|....*....|...
gi 530387683 1700 GPADFQEGTWVGVELDLPSGKNDGSIGGKQYFR 1732
Cdd:COG5180   470 VAPVTDATPVDVADVLGVRPDAILGGNVAPASG 502
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1476-1669 3.13e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 52.16  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1476 RGKRPSPLAHQAQPEMGPdVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTA 1555
Cdd:PRK07003  384 GARAAAAVGASAVPAVTA-VTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSR 462
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1556 TLSDALGPGLDA---AAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQqlvspGRERPDleAPAPGSPfrvrrvra 1632
Cdd:PRK07003  463 CDERDAQPPADSgsaSAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA-----AASRED--APAAAAP-------- 527
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 530387683 1633 selrsfsrmlagdpgcsPGAEGNAPAPGA-------GGQALASD 1669
Cdd:PRK07003  528 -----------------PAPEARPPTPAAaapaaraGGAAAALD 554
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
1500-1634 4.87e-06

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 50.94  E-value: 4.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1500 MGAPALKICDKPAKVPSPPPVI-------AVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDAlgPGLDAAAPPG 1572
Cdd:pfam13254  209 MRSPAPGGHSKSPSVSGISADSsptkeepSEEADTLSTDKEQSPAPTSASEPPPKTKELPKDSEEPAA--PSKSAEASTE 286
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683  1573 SMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRErPDLEAPAPGSP---FRV---RRVRASE 1634
Cdd:pfam13254  287 KKEPDTESSPETSSEKSAPSLLSPVSKASIDKPLSSPDRD-PLSPKPKPQSPpkdFRAnlrSREVPKD 353
PHA03247 PHA03247
large tegument protein UL36; Provisional
1476-1677 5.31e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.86  E-value: 5.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1476 RGKRPSPLAHQAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPP----VIAVTAVTPAPEAQDGPPSPLSEASSGYFSHS 1551
Cdd:PHA03247 2585 RARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPpspsPAANEPDPHPPPTVPPPERPRDDPAPGRVSRP 2664
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1552 VSTATLSDALGPGLDA------AAPPGSMPTAPEAEPEAPISHP-PPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSP 1624
Cdd:PHA03247 2665 RRARRLGRAAQASSPPqrprrrAARPTVGSLTSLADPPPPPPTPePAPHALVSATPLPPGPAAARQASPALPAAPAPPAV 2744
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530387683 1625 FRVRRVRASELRSFSRMLAGDPGCS--PGAEGNAPAPGAGGQALASDSEEADEVP 1677
Cdd:PHA03247 2745 PAGPATPGGPARPARPPTTAGPPAPapPAAPAAGPPRRLTRPAVASLSESRESLP 2799
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
1512-1633 7.26e-06

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 50.15  E-value: 7.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1512 AKVPSPPPVIAVT---AVTPAPEAQDGPPSPLSEASSG-----YFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPE 1583
Cdd:NF040712  200 ATVPRLAREPADArpeEVEPAPAAEGAPATDSDPAEAGtpddlASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530387683 1584 APIS---HPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRAS 1633
Cdd:NF040712  280 PPAPgaaETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRAS 332
PHA03247 PHA03247
large tegument protein UL36; Provisional
1551-1659 8.57e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 8.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1551 SVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHP----------------------PPPTAVPAEEPPGPQQLVS 1608
Cdd:PHA03247 2490 FAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPvhprmltwirgleelasddagdPPPPLPPAAPPAAPDRSVP 2569
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530387683 1609 PGRERPDLEAPAPGSpfRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAP 1659
Cdd:PHA03247 2570 PPRPAPRPSEPAVTS--RARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLP 2618
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1552-1710 9.50e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.75  E-value: 9.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1552 VSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVR 1631
Cdd:PRK07764  393 APAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAA 472
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1632 ASEL--RSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREGEFVTVGAhktgVVRYVGPADFQEGTW 1709
Cdd:PRK07764  473 APEPtaAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPEILAAVPKRSRKTWAI----LLPEATVLGVRGDTL 548

                  .
gi 530387683 1710 V 1710
Cdd:PRK07764  549 V 549
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1423-1600 1.07e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 50.54  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1423 IAPAPALSVSPQNN---HSPDPGLSNLAASYLNpvkSFVPQMPKL--LKSLFPVRDEKRGKRPSPLAHQAQ----PEMGP 1493
Cdd:pfam03154  355 IKPPPTTPIPQLPNpqsHKHPPHLSGPSPFQMN---SNLPPPPALkpLSSLSTHHPPSAHPPPLQLMPQSQqlppPPAQP 431
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1494 DVLVQTMGAPALKICDKPA----KVPSPPPVIA---VTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLD 1566
Cdd:pfam03154  432 PVLTQSQSLPPPAASHPPTsglhQVPSQSPFPQhpfVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVS 511
                          170       180       190
                   ....*....|....*....|....*....|....
gi 530387683  1567 AAAPPGSMPTAPEAEPEAPIShPPPPTAVPAEEP 1600
Cdd:pfam03154  512 CPLPPVQIKEEALDEAEEPES-PPPPPRSPSPEP 544
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
1499-1600 1.09e-05

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 49.54  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1499 TMGAPALKICDkPAKVPSPPPVIAVTAVTPAPEAQDGPPSPlseassgyfshsvsTATLSDALGPGldaAAPPGSMPTAP 1578
Cdd:pfam07174   30 AVALPAVAHAD-PEPAPPPPSTATAPPAPPPPPPAPAAPAP--------------PPPPAAPNAPN---APPPPADPNAP 91
                           90       100
                   ....*....|....*....|..
gi 530387683  1579 EAEPEAPISHPPPPTAVPAEEP 1600
Cdd:pfam07174   92 PPPPADPNAPPPPAVDPNAPEP 113
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
468-542 1.13e-05

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 45.72  E-value: 1.13e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683  468 KEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNTR-TFVNGSSVSSPIQLHHGDRILWGNNHF-FRL 542
Cdd:COG1716    20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRD-GGGWVLEDLGSTNgTFVNGQRVTEPAPLRDGDVIRLGKTELrFRL 95
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
1511-1624 2.22e-05

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 46.40  E-value: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1511 PAKVPSPPPVIAVTAVTPAP----EAQDGPPSPLseassgyfshsvstatlsdalgPGLDAAAPPGSMPTAPEAEPEAPI 1586
Cdd:pfam06346   18 GACIPTPPPLPGGGGPPPPPplpgSAAIPPPPPL----------------------PGGTSIPPPPPLPGAASIPPPPPL 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 530387683  1587 SH----PPPP-----TAVPAEEPPGPQqlvSPGRERPdlEAPAPGSP 1624
Cdd:pfam06346   76 PGstgiPPPPplpggAGIPPPPPPLPG---GAGVPPP--PPPLPGGP 117
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1424-1621 3.19e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 48.72  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1424 APAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQAQPEMGPDVLVQTMGAP 1503
Cdd:PRK12323  389 AAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAG 468
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1504 ALKicdkPAKVPSPPPVIAVTAVTPAPEAQDGPP---------SPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSM 1574
Cdd:PRK12323  469 PRP----VAAAAAAAPARAAPAAAPAPADDDPPPweelppefaSPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPA 544
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 530387683 1575 PTAPEAEPEAPISHPPPPTAVPAEEPPGPQQlVSPGrERPDLEAPAP 1621
Cdd:PRK12323  545 PAAAPAPRAAAATEPVVAPRPPRASASGLPD-MFDG-DWPALAARLP 589
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1520-1677 5.00e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1520 VIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEE 1599
Cdd:PRK07764  584 VEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683 1600 PPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPgcSPGAEGNAPAPGAGGQALASDSEEADEVP 1677
Cdd:PRK07764  664 DGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP--AGQADDPAAQPPQAAQGASAPSPAADDPV 739
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1511-1611 5.17e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 5.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPVIAVTAVTPAPEAQDGP---PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPE-API 1586
Cdd:PRK07764  406 PAAAPAPAAAAPAAAAAPAPAAAPQPapaPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPApAPP 485
                          90       100
                  ....*....|....*....|....*
gi 530387683 1587 SHPPPPTAVPAEEPPGPQQLVSPGR 1611
Cdd:PRK07764  486 AAPAPAAAPAAPAAPAAPAGADDAA 510
PHA03247 PHA03247
large tegument protein UL36; Provisional
1514-1677 6.44e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1514 VPSPPPVI----------AVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDalgpgldaAAPPGSMPTAPEAEPE 1583
Cdd:PHA03247  254 APAPPPVVgegadrapetARGATGPPPPPEAAAPNGAAAPPDGVWGAALAGAPLAL--------PAPPDPPPPAPAGDAE 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1584 A------------PISHPP-------PPTAVPAEEPPGPQQLVSPGRERPDLEAPapgsPFRVRRVRASELRSFSRMLAG 1644
Cdd:PHA03247  326 EeddedgamevvsPLPRPRqhyplgfPKRRRPTWTPPSSLEDLSAGRHHPKRASL----PTRKRRSARHAATPFARGPGG 401
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 530387683 1645 D--PGCSPGAEGNAPAPGAGGQALASDSEEADEVP 1677
Cdd:PHA03247  402 DdqTRPAAPVPASVPTPAPTPVPASAPPPPATPLP 436
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
1510-1674 7.68e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 47.40  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1510 KP-AKVPSPPPVIAVTAVTPAPEAQDgpPSPLSEASSgyfshsvstatlsdalgPGLDAAAPPGSMPTAPEAEPEAPish 1588
Cdd:PRK14951  365 KPaAAAEAAAPAEKKTPARPEAAAPA--AAPVAQAAA-----------------APAPAAAPAAAASAPAAPPAAAP--- 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1589 pPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPfrvrrvrasELRSFSRMLAGDPGCSPGAEGNAPAPGAggqALAS 1668
Cdd:PRK14951  423 -PAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAP---------ETVAIPVRVAPEPAVASAAPAPAAAPAA---ARLT 489

                  ....*.
gi 530387683 1669 DSEEAD 1674
Cdd:PRK14951  490 PTEEGD 495
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1428-1626 8.80e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.86  E-value: 8.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1428 ALSVSPQNNHSPD----PGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPlahqaqpEMGPDVLVQTMGAP 1503
Cdd:PHA03307  730 ARTVAPLVRYSPRraraRASAWDITDALFSNPSLVPAKLAEALALLEPAEPQRGAGSSP-------PVRAEAAFRRPGRL 802
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1504 ALKICDKPAKVP------SPPPVIAVTAVTPAPEAQDGP-PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPT 1576
Cdd:PHA03307  803 RRSGPAADAASRtaskrkSRSHTPDGGSESSGPARPPGAaARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRAR 882
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 530387683 1577 APEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPgreRPdLEAPAPGSPFR 1626
Cdd:PHA03307  883 PGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLGP---MP-PGGPDPRGGFR 928
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
1099-1143 1.26e-04

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 43.66  E-value: 1.26e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 530387683  1099 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1143
Cdd:pfam12130   66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1511-1633 2.20e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.13  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPVIAVTAVTPAPEAQDGPPSPlseASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPP 1590
Cdd:PRK07764  398 APSAAAAAPAAAPAPAAAAPAAAAAPAPA---AAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAP 474
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 530387683 1591 PPTAVPAEEPPGPQQlvSPGRERPDLEAPAPGSPFRVRRVRAS 1633
Cdd:PRK07764  475 EPTAAPAPAPPAAPA--PAAAPAAPAAPAAPAGADDAATLRER 515
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1479-1674 2.86e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 45.64  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1479 RPSPLAHQAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAvtAVTPAPEAQDGPPSPLSEASSgyfshsvSTATLS 1558
Cdd:PRK12323  416 ARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPA--AAARPAAAGPRPVAAAAAAAP-------ARAAPA 486
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1559 DALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQlvsPGRERPDLEAPAPGSPFRVRRVRASELRSF 1638
Cdd:PRK12323  487 AAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATAD---PDDAFETLAPAPAAAPAPRAAAATEPVVAP 563
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 530387683 1639 SRMLAGDPGCSPGAEGNAPAPGAG------GQALASDSEEAD 1674
Cdd:PRK12323  564 RPPRASASGLPDMFDGDWPALAARlpvrglAQQLARQSELAG 605
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
1512-1677 2.93e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 45.69  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1512 AKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSgyfshSVSTATLSDALGPgldaaaPPGSMPTAPEAEPEAP------ 1585
Cdd:PLN03209  336 ADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPR-----PLSPYTAYEDLKP------PTSPIPTPPSSSPASSksvdav 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1586 --------ISHPPPPTAVPAEEP-PGPQQL---VSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAE 1653
Cdd:PLN03209  405 akpaepdvVPSPGSASNVPEVEPaQVEAKKtrpLSPYARYEDLKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATAAT 484
                         170       180
                  ....*....|....*....|....
gi 530387683 1654 GNAPAPGAGGQALASDSEEADEVP 1677
Cdd:PLN03209  485 DAAAPPPANMRPLSPYAVYDDLKP 508
dnaA PRK14086
chromosomal replication initiator protein DnaA;
1511-1663 3.35e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 45.59  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPviavtavTPAPEAQDGP--PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAP----------PGSMP--- 1575
Cdd:PRK14086   90 PSAGEPAPP-------PPHARRTSEPelPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARPaypayqqrpePGAWPraa 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1576 ------------------TAPEAEPEAPISHPPPPTAVPAEEPPGPQQ-------LVSPGRERPDLEAPAPGSPFRVRRV 1630
Cdd:PRK14086  163 ddygwqqqrlgfpprapyASPASYAPEQERDREPYDAGRPEYDQRRRDydhprpdWDRPRRDRTDRPEPPPGAGHVHRGG 242
                         170       180       190
                  ....*....|....*....|....*....|....
gi 530387683 1631 R-ASELRSFSRMLAGDPGCSPGAEGNAPAPGAGG 1663
Cdd:PRK14086  243 PgPPERDDAPVVPIRPSAPGPLAAQPAPAPGPGE 276
PHA03247 PHA03247
large tegument protein UL36; Provisional
1414-1665 3.40e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1414 VSQTTVSRGIAPAP-ALSVSPQNNHSPDPGLSNLA--ASYLNPVKSFVPQMPKLLKSLFPVRDEKRG---------KRPS 1481
Cdd:PHA03247 2788 VASLSESRESLPSPwDPADPPAAVLAPAAALPPAAspAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPP 2867
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1482 PLAHQAQPEMGPDVLVQTMGAPALKIC--------DKPAKVPSP---------PPVIAVTAVTPAPEAQDGPPSPLS--- 1541
Cdd:PHA03247 2868 SRSPAAKPAAPARPPVRRLARPAVSRStesfalppDQPERPPQPqappppqpqPQPPPPPQPQPPPPPPPRPQPPLAptt 2947
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1542 -EASSGYFSHSVSTATLSdALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPA-----------EEP-PGP----Q 1604
Cdd:PHA03247 2948 dPAGAGEPSGAVPQPWLG-ALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRvsswasslalhEETdPPPvslkQ 3026
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530387683 1605 QLVSPGR--------------ERPDLEAPAPgspfrvrrvraselrsfsrmLAGDPGCSPGAEGNAPAPGAGGQA 1665
Cdd:PHA03247 3027 TLWPPDDtedsdadslfdsdsERSDLEALDP--------------------LPPEPHDPFAHEPDPATPEAGARE 3081
PHA03247 PHA03247
large tegument protein UL36; Provisional
1477-1678 3.63e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.70  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1477 GKRPSPLA-HQAQPEMGPDVL--VQTMGAPALKicdkPAKVPSPPPVIAVTA------------VTPAPEAQD------- 1534
Cdd:PHA03247  277 GPPPPPEAaAPNGAAAPPDGVwgAALAGAPLAL----PAPPDPPPPAPAGDAeeeddedgamevVSPLPRPRQhyplgfp 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1535 -------GPPSPLSEASSGyfSHSVSTATLSD-------------ALGPGLD-----AAAPPGSMPTaPEAEPeAPISHP 1589
Cdd:PHA03247  353 krrrptwTPPSSLEDLSAG--RHHPKRASLPTrkrrsarhaatpfARGPGGDdqtrpAAPVPASVPT-PAPTP-VPASAP 428
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1590 PPP-TAVPAEEPPGPQQLVSPGRERPDLEA--PAPGSPFRVRRVRASELRsfSRMLAGDPGCSPgAE--GNAPAPGAGGQ 1664
Cdd:PHA03247  429 PPPaTPLPSAEPGSDDGPAPPPERQPPAPAtePAPDDPDDATRKALDALR--ERRPPEPPGADL-AEllGRHPDTAGTVV 505
                         250
                  ....*....|....*
gi 530387683 1665 ALAS-DSEEADEVPE 1678
Cdd:PHA03247  506 RLAArEAAIAREVAE 520
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1480-1674 3.66e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1480 PSPLAHQAQPEMGPDVLVQTMGAPA-LKICDKPAKVPSPPPVIAVTAVTPA-----------------PEAQDGPPSPLS 1541
Cdd:PHA03307  131 APDLSEMLRPVGSPGPPPAASPPAAgASPAAVASDAASSRQAALPLSSPEEtarapssppaepppstpPAAASPRPPRRS 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1542 EASSGYFSHSVSTATLSDALGPG--LDAAAPPGSMPTAPEAEPEAPISHPPPPT-------AVPAEEP---PGPQQLVSP 1609
Cdd:PHA03307  211 SPISASASSPAPAPGRSAADDAGasSSDSSSSESSGCGWGPENECPLPRPAPITlptriweASGWNGPssrPGPASSSSS 290
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683 1610 GRER-PDLEAPAPGSPFRVRRVRASELRSFSR--MLAGDPGCSPGAEGNAPAPGAGGQALASDSEEAD 1674
Cdd:PHA03307  291 PRERsPSPSPSSPGSGPAPSSPRASSSSSSSResSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPP 358
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1502-1677 4.45e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 45.23  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1502 APALKICDKPAKVPSPPPVIAVtavtPAPEAQdgpPSPLSEASSGYFSHSVSTATLSdalgpgldAAAPPGSMPTAPeAE 1581
Cdd:PRK07003  359 EPAVTGGGAPGGGVPARVAGAV----PAPGAR---AAAAVGASAVPAVTAVTGAAGA--------ALAPKAAAAAAA-TR 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1582 PEAPISHPPPPTAVPAEEPPGPQQLVSPGrerpdlEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAPGA 1661
Cdd:PRK07003  423 AEAPPAAPAPPATADRGDDAADGDAPVPA------KANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRA 496
                         170
                  ....*....|....*.
gi 530387683 1662 GGQALASDSEEADEVP 1677
Cdd:PRK07003  497 AAPSAATPAAVPDARA 512
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
1501-1620 5.54e-04

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 42.37  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1501 GAPALKICDKPAKVPSPPpviAVTAVTPAPEAQDgPPSPLSEASS-----------GYFSHSVSTATLSDALGPGLDAAA 1569
Cdd:cd21975    29 GLAAGLDVRATREVAKGP---GPPGPAWKPDGAD-SPGLVTAAPHllaanvlaplrGPSVEGSSLESGDADMGSDSDVAP 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530387683 1570 PPGSM-PTAPEAE---PEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPA 1620
Cdd:cd21975   105 ASGAAaSTSPESSsdaASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTPAA 159
Tymo_45kd_70kd pfam03251
Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a ...
1421-1626 5.69e-04

Tymovirus 45/70Kd protein; Tymoviruses are single stranded RNA viruses. This family includes a protein of unknown function that has been named based on its molecular weight. Tymoviruses such as the ononis yellow mosaic tymovirus encode only three proteins. Of these two are overlapping this protein overlaps a larger ORF that is thought to be the polymerase.


Pssm-ID: 281269 [Multi-domain]  Cd Length: 468  Bit Score: 44.40  E-value: 5.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1421 RGIAPAPA-------LSV----SPQNNHSPDPGLSNLAASYLNPVKSFVPQMP--KLLKS--LFPVRDEKRGKRPSPLAH 1485
Cdd:pfam03251  257 RPITPGPSnthdlrpLSVlprtSPRRGLLPNPRRHRTSTGHIPPTTTSRPTGPpsRLQRPvhLYQSSPHTPNFRPSSIRK 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1486 QAQPEMGPDV-LVQTMGAPA-LKICDKpakvpSPPpviaVTAVTPAPEAQDGPPSPLSEAS-SGYFSHSVSTATLSDalg 1562
Cdd:pfam03251  337 DALLQTGPRLgHLERLGQPAnLRTSER-----SPP----TKRRLPRSSEPNRLPKPLPEATlAPSYRHRRPYPLLPN--- 404
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530387683  1563 pgldaaaPPGSMPTAPEAEPEAPISHPPPPTAVPAE-EPPGPQQLVSPgrerpdleAPAPGSPFR 1626
Cdd:pfam03251  405 -------PPAALPSIAYTSSRGKIHHSLPKGALPKEgAPPPPRRLPSP--------APRPQLPLR 454
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
1522-1621 6.32e-04

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 43.76  E-value: 6.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1522 AVTAVTPAPEAQDGPPSPLseassgyfshsvstatlsdalgPGLDAAAPPgsMPTAPEAEPEAPISHPPPPTAVPAEEPP 1601
Cdd:pfam07174   28 AVAVALPAVAHADPEPAPP----------------------PPSTATAPP--APPPPPPAPAAPAPPPPPAAPNAPNAPP 83
                           90       100
                   ....*....|....*....|
gi 530387683  1602 GPQQLVSPGRERPDLEAPAP 1621
Cdd:pfam07174   84 PPADPNAPPPPPADPNAPPP 103
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
1558-1642 7.17e-04

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 44.22  E-value: 7.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1558 SDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGR--ERPDLEAPAPGSPFRVRRVRA-SE 1634
Cdd:NF041121   22 PSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPppPGPAGAAPGAALPVRVPAPPAlPN 101

                  ....*...
gi 530387683 1635 LRSFSRML 1642
Cdd:NF041121  102 PLELARAL 109
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
460-540 8.84e-04

forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438785  Cd Length: 113  Bit Score: 40.94  E-value: 8.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  460 NELLVYYL-KEHTLIG---SANSQDIQLCGMGILPEHCII------DITSEGQVMLTPQKNTRTFVNGSSVSSPIQLHHG 529
Cdd:cd22733    18 HDCLVYLLnREQHTVGqetPSSKPNISLSAPDILPLHCTIrrvrlpKHRSEEKLVLEPIPGAHVSVNFSEVERTTLLRHG 97
                          90
                  ....*....|.
gi 530387683  530 DRILWGNNHFF 540
Cdd:cd22733    98 DLLSFGAYYLF 108
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
1482-1682 1.08e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 43.70  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1482 PLAHQAQPEMGPDVLVQTMGAPALKicDKPAKVPSPPPVIAVTAVTPAPEAQdgPPSPLSEAssgyfshsvsTATLSDAL 1561
Cdd:PRK07994  361 PAAPLPEPEVPPQSAAPAASAQATA--APTAAVAPPQAPAVPPPPASAPQQA--PAVPLPET----------TSQLLAAR 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1562 gPGLDAAAPPgsmPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPgrerpdlEAPAPGSPFRVRRVRASElrsfsrm 1641
Cdd:PRK07994  427 -QQLQRAQGA---TKAKKSEPAAASRARPVNSALERLASVRPAPSALE-------KAPAKKEAYRWKATNPVE------- 488
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 530387683 1642 LAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLRE 1682
Cdd:PRK07994  489 VKKEPVATPKALKKALEHEKTPELAAKLAAEAIERDPWAAL 529
PHA03369 PHA03369
capsid maturational protease; Provisional
1497-1622 1.11e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 43.83  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1497 VQTMGAPALKICDKPA-----KVPSPPPVIAVTAVTPAPEAQDGPPSPLseassgyFSHSVSTATLSDALGPGLDAAA-- 1569
Cdd:PHA03369  521 AKTAAANIEPNCSADAaapatKRARPETKTELEAVVRFPYQIRNMESPA-------FVHSFTSTTLAAAAGQGSDTAEal 593
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683 1570 --------------PPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPgpqqlvsPGRERPDLEAPAPG 1622
Cdd:PHA03369  594 agaietlltqasaqPAGLSLPAPAVPVNASTPASTPPPLAPQEPPQ-------PGTSAPSLETSLPQ 653
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
1518-1624 1.51e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 42.83  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1518 PPVIAVTAV-TPAPEAQDGPPSPLSEASSGYF---SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPT 1593
Cdd:NF040712  194 RPLRPLATVpRLAREPADARPEEVEPAPAAEGapaTDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEA 273
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530387683 1594 AVPAEEPPGPQQLVSPGRERPDLEAPAPGSP 1624
Cdd:NF040712  274 TRDAGEPPAPGAAETPEAAEPPAPAPAAPAA 304
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
1511-1678 1.74e-03

poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.


Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 43.14  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1511 PAKVPSPPPVIAV-----TAVTPAPEAQDGPPSP-LSEASSGYFSHSVSTATLSDAL-GPGLDAAAPPGSMP-TAPEAEP 1582
Cdd:TIGR01645  291 PATVSAIPAAAAVaaaaaTAKIMAAEAVAGAAVLgPRAQSPATPSSSLPTDIGNKAVvSSAKKEAEEVPPLPqAAPAVVK 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  1583 ----EAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEApAPGSPFRVRRVRASELRSFSRMLAGDP--GCSPGAEGNA 1656
Cdd:TIGR01645  371 pgpmEIPTPVPPPGLAIPSLVA--PPGLVAPTEINPSFLA-SPRKKMKREKLPVTFGALDDTLAWKEPskEDQTSEDGKM 447
                          170       180
                   ....*....|....*....|...
gi 530387683  1657 PA-PGAGGQALASDSEEADEVPE 1678
Cdd:TIGR01645  448 LAiMGEAAAALALEPKKKKKEKE 470
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
1524-1621 1.74e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 43.26  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1524 TAVTPAPEAQDGPPsplseassgyfshsvsTATLSDALGPGLDAAAPPGSMPTA--PEAEPEAPISHPPPPTAVPAEEPP 1601
Cdd:PRK14950  358 ALLVPVPAPQPAKP----------------TAAAPSPVRPTPAPSTRPKAAAAAniPPKEPVRETATPPPVPPRPVAPPV 421
                          90       100
                  ....*....|....*....|....*...
gi 530387683 1602 GPQQ--------LVSPGRERPDLEAPAP 1621
Cdd:PRK14950  422 PHTPesapkltrAAIPVDEKPKYTPPAP 449
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1561-1678 1.98e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1561 LGPGLDAAAPPGSMPTAPEAEPEApiSHPPPPTAVPAEEPPGPqqlvsPGRERPdLEAPAPGSPFRVRRVRASELRSFSR 1640
Cdd:PRK07764  385 LGVAGGAGAPAAAAPSAAAAAPAA--APAPAAAAPAAAAAPAP-----AAAPQP-APAPAPAPAPPSPAGNAPAGGAPSP 456
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 530387683 1641 MLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPE 1678
Cdd:PRK07764  457 PPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAP 494
COG5493 COG5493
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ...
368-444 2.01e-03

Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only];


Pssm-ID: 444244 [Multi-domain]  Cd Length: 239  Bit Score: 41.89  E-value: 2.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530387683  368 IRDLREEVEKLREQLTKAE--AMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG 444
Cdd:COG5493    36 LEELLERLEKLEEQMRKWEeqLRKLEEEIKKLREQVRKLEEDVKRLEEQERKLEEAMAEHSELREELMKLIKRLERSIG 114
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1511-1636 2.26e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1511 PAKVPSPPPVIAVTAvTPAPEAQDGPPSPLSEASSGyfshsvstatlsdALGPGLDAAAPPGSMPTAPEAEPEAPISHPP 1590
Cdd:PRK07764  415 AAPAAAAAPAPAAAP-QPAPAPAPAPAPPSPAGNAP-------------AGGAPSPPPAAAPSAQPAPAPAAAPEPTAAP 480
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 530387683 1591 PPTAVPAEEPPGPQQLVSPGrerpdlEAPAPGSPFRVRRVRASELR 1636
Cdd:PRK07764  481 APAPPAAPAPAAAPAAPAAP------AAPAGADDAATLRERWPEIL 520
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
368-432 2.49e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530387683  368 IRDLREEVEKLREQLTKAEAMKS--PELKDRLEESEKLIQEMtvtwEEKLRKTEEIAQERQKQLESL 432
Cdd:PRK03918  216 LPELREELEKLEKEVKELEELKEeiEELEKELESLEGSKRKL----EEKIRELEERIEELKKEIEEL 278
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1502-1667 2.93e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1502 APALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGP--PSPLSEASSGYFSHSVSTATLSDALGPGldAAAPPGSMPTAPE 1579
Cdd:PHA03307  776 EPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADaaSRTASKRKSRSHTPDGGSESSGPARPPG--AAARPPPARSSES 853
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1580 AEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPG-SPFRVRRVRASELRSFSRMLAGDP---GC---SPGA 1652
Cdd:PHA03307  854 SKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPpAGAPAPRPRPAPRVKLGPMPPGGPdprGGfrrVPPG 933
                         170
                  ....*....|....*
gi 530387683 1653 EGNAPAPGAggQALA 1667
Cdd:PHA03307  934 DLHTPAPSA--AALA 946
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1528-1803 5.12e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1528 PAPEAQDGPPSPLSeASSGYFShsVSTATLSDALGPGLDAAAPPGSMPTAPEAEPeapishpppptavPAEEPPGPQQLV 1607
Cdd:PHA03307   24 PPATPGDAADDLLS-GSQGQLV--SDSAELAAVTVVAGAAACDRFEPPTGPPPGP-------------GTEAPANESRST 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1608 SPGRERPDLEAPAPGSPFRVRRVRASelrsfsrmlagDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREGEFVT 1687
Cdd:PHA03307   88 PTWSLSTLAPASPAREGSPTPPGPSS-----------PDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1688 V--GAHKTGVVRYVGPADFqegtwvgveLDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRR---ATGPVRRRSTGLRL 1762
Cdd:PHA03307  157 AspAAVASDAASSRQAALP---------LSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSspiSASASSPAPAPGRS 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 530387683 1763 GAPEARRSATLSGSATNLASLTAALAKADRSHKNPENRKSW 1803
Cdd:PHA03307  228 AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTR 268
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
611-760 7.30e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683  611 LNSLEQQHE--EEKRSALERQRlmyeHELEQLRRRLSPEKQNCRSMDRFSFHS---PSAQQRLRQWAEEREATLNNS--L 683
Cdd:COG4913   612 LAALEAELAelEEELAEAEERL----EALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSddL 687
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530387683  684 MRLREQIVKANLLVREANYIAEELDKRteykvtlqipASSLDANRKR-GSLLSEPAIQVRRKGKGKQIWSLEKLDNRL 760
Cdd:COG4913   688 AALEEQLEELEAELEELEEELDELKGE----------IGRLEKELEQaEEELDELQDRLEAAEDLARLELRALLEERF 755
flhF PRK06995
flagellar biosynthesis protein FlhF;
1565-1659 8.61e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 40.72  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530387683 1565 LDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAG 1644
Cdd:PRK06995   48 LAALAPPAAAAPAAAQPPPAAAPAAVSRPAAPAAEP--APWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAA 125
                          90
                  ....*....|....*
gi 530387683 1645 DPGCSPGAEGNAPAP 1659
Cdd:PRK06995  126 ENAARRLARAAAAAP 140
 
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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