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Conserved domains on  [gi|530409731|ref|XP_005256481|]
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kinesin-like protein KIF1C isoform X1 [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 ...
4-355 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: 646.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    4 ASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQS-------KDAPKSFTFDYSYWSHTStEDPQFASQQQVYRD 76
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQAdknnkatREVPKSFSFDYSYWSHDS-EDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   77 IGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEpgQQGIVPQLCEDLFSRVSENQSAQLSYSVEVSYMEIYCERVRD 156
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  157 LLNPKS---RGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQL 233
Cdd:cd01365   158 LLNPKPkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  234 TGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMQSKK--RKSDFIPYRDSVLTWLLKE 311
Cdd:cd01365   238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKskKKSSFIPYRDSVLTWLLKE 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 530409731  312 NLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAIIN 355
Cdd:cd01365   318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
Kinesin_assoc super family cl24686
Kinesin-associated;
352-522 4.05e-74

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 242.83  E-value: 4.05e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   352 AIINEDPNARLIRELQEEVARLRELLMAQGLSasalEGLKTEEGSVRGALPAVSSPPAPVSPSSPTTHNGELEPSFSPNT 431
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLG----DIIDTIAHPTKKRANTPAANASAATAAMAGASPSPSLSALSSRA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   432 ESQI----------GPEEAMERLQETEKIIAELNETWEEKLRKTEALRMEREALLAEMGVAVREDGGTVGVFSPKKTPHL 501
Cdd:pfam16183   77 ASVSslherimftpGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHL 156
                          170       180
                   ....*....|....*....|.
gi 530409731   502 VNLNEDPLMSECLLYHIKDGV 522
Cdd:pfam16183  157 VNLNEDPLMSECLLYYIKDGI 177
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
498-599 3.08e-71

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: 231.68  E-value: 3.08e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  498 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDMDIKLTGQFIREQHCLFRSIPQPDGEVVVTLEPCEGAETYVNGKLVTE 577
Cdd:cd22728     1 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVDIKLSGQFIREQHCLFRSIPNPSGEVVVTLEPCEGAETYVNGKQVTE 80
                          90       100
                  ....*....|....*....|..
gi 530409731  578 PLVLKSGNRIVMGKNHVFRFNH 599
Cdd:cd22728    81 PLVLKSGNRIVMGKNHVFRFNH 102
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
4-355 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: 646.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    4 ASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQS-------KDAPKSFTFDYSYWSHTStEDPQFASQQQVYRD 76
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQAdknnkatREVPKSFSFDYSYWSHDS-EDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   77 IGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEpgQQGIVPQLCEDLFSRVSENQSAQLSYSVEVSYMEIYCERVRD 156
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  157 LLNPKS---RGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQL 233
Cdd:cd01365   158 LLNPKPkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  234 TGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMQSKK--RKSDFIPYRDSVLTWLLKE 311
Cdd:cd01365   238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKskKKSSFIPYRDSVLTWLLKE 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 530409731  312 NLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAIIN 355
Cdd:cd01365   318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
5-355 3.30e-157

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: 469.75  E-value: 3.30e-157
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731      5 SVKVAVRVRPFNARETSQDAKCVVSMQGN---TTSIINPKQSKDApKSFTFDYSYwshtstedPQFASQQQVYRDIGEEM 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKvgkTLTVRSPKNRQGE-KKFTFDKVF--------DATASQEDVFEETAAPL 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731     82 LLHAFEGYNVCIFAYGQTGAGKSYTMMGrqEPGQQGIVPQLCEDLFSRVsENQSAQLSYSVEVSYMEIYCERVRDLLNPk 161
Cdd:smart00129   72 VDSVLEGYNATIFAYGQTGSGKTYTMIG--TPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP- 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    162 SRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDqlTGLDSEKV 241
Cdd:smart00129  148 SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN--SSSGSGKA 225
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    242 SKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMQskkrKSDFIPYRDSVLTWLLKENLGGNSRTAM 321
Cdd:smart00129  226 SKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTLM 301
                           330       340       350
                    ....*....|....*....|....*....|....
gi 530409731    322 IAALSPADINYEETLSTLRYADRTKQIRCNAIIN 355
Cdd:smart00129  302 IANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-348 1.69e-152

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 457.03  E-value: 1.69e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    11 RVRPFNARETSQDAKCVVSM--QGNTTSIINPKQSKDAPKSFTFDYSYWSHtstedpqfASQQQVYRDIGEEMLLHAFEG 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVesVDSETVESSHLTNKNRTKTFTFDKVFDPE--------ATQEDVYEETAKPLVESVLEG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    89 YNVCIFAYGQTGAGKSYTMMGRQEpgQQGIVPQLCEDLFSRVSENQSaQLSYSVEVSYMEIYCERVRDLLNP--KSRGSL 166
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDE--QPGIIPRALEDLFDRIQKTKE-RSEFSVKVSYLEIYNEKIRDLLSPsnKNKRKL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   167 RVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQlTGLDSEKVSKISL 246
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRST-GGEESVKTGKLNL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   247 VDLAGSERADSSG-ARGMRLKEGANINKSLTTLGKVISALADMQSKkrksdFIPYRDSVLTWLLKENLGGNSRTAMIAAL 325
Cdd:pfam00225  229 VDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSK-----HIPYRDSKLTRLLQDSLGGNSKTLMIANI 303
                          330       340
                   ....*....|....*....|...
gi 530409731   326 SPADINYEETLSTLRYADRTKQI 348
Cdd:pfam00225  304 SPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
68-399 5.56e-82

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 278.55  E-value: 5.56e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   68 ASQQQVYRDIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGrqEPGQQGIVPQLCEDLFSRVsENQSAQLSYSVEVSYM 147
Cdd:COG5059    68 ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG--TEEEPGIIPLSLKELFSKL-EDLSMTKDFAVSISYL 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  148 EIYCERVRDLLNPKSRgSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQ 227
Cdd:COG5059   145 EIYNEKIYDLLSPNEE-SLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELAS 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  228 RChdqlTGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALadmqSKKRKSDFIPYRDSVLTW 307
Cdd:COG5059   224 KN----KVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINAL----GDKKKSGHIPYRESKLTR 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  308 LLKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIR-----CNAIINEDPNARL---IRELQEEVARLRELLmA 379
Cdd:COG5059   296 LLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKnkiqvNSSSDSSREIEEIkfdLSEDRSEIEILVFRE-Q 374
                         330       340
                  ....*....|....*....|
gi 530409731  380 QGLSASALEGLKTEEGSVRG 399
Cdd:COG5059   375 SQLSQSSLSGIFAYMQSLKK 394
PLN03188 PLN03188
kinesin-12 family protein; Provisional
1-374 1.49e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 270.27  E-value: 1.49e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    1 MAGASVKVAVRVRPFNAREtsQDAKCVVSMQGNTTSIINpkqskdapKSFTFDysywshtSTEDPQfASQQQVYRDIGEE 80
Cdd:PLN03188   95 VSDSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTING--------QTFTFD-------SIADPE-STQEDIFQLVGAP 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   81 MLLHAFEGYNVCIFAYGQTGAGKSYTMMG--------RQEPGQQGIVPQLCEDLFSRVSENQ----SAQLSYSVEVSYME 148
Cdd:PLN03188  157 LVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglleeHLSGDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRCSFLE 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  149 IYCERVRDLLNPKSRgSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQR 228
Cdd:PLN03188  237 IYNEQITDLLDPSQK-NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESR 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  229 CHDQLTGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMqSKKRKSDFIPYRDSVLTWL 308
Cdd:PLN03188  316 CKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEI-SQTGKQRHIPYRDSRLTFL 394
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530409731  309 LKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAIINE----DPN--ARLIRELQEEVARLR 374
Cdd:PLN03188  395 LQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
Kinesin_assoc pfam16183
Kinesin-associated;
352-522 4.05e-74

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 242.83  E-value: 4.05e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   352 AIINEDPNARLIRELQEEVARLRELLMAQGLSasalEGLKTEEGSVRGALPAVSSPPAPVSPSSPTTHNGELEPSFSPNT 431
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLG----DIIDTIAHPTKKRANTPAANASAATAAMAGASPSPSLSALSSRA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   432 ESQI----------GPEEAMERLQETEKIIAELNETWEEKLRKTEALRMEREALLAEMGVAVREDGGTVGVFSPKKTPHL 501
Cdd:pfam16183   77 ASVSslherimftpGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHL 156
                          170       180
                   ....*....|....*....|.
gi 530409731   502 VNLNEDPLMSECLLYHIKDGV 522
Cdd:pfam16183  157 VNLNEDPLMSECLLYYIKDGI 177
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
498-599 3.08e-71

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: 231.68  E-value: 3.08e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  498 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDMDIKLTGQFIREQHCLFRSIPQPDGEVVVTLEPCEGAETYVNGKLVTE 577
Cdd:cd22728     1 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVDIKLSGQFIREQHCLFRSIPNPSGEVVVTLEPCEGAETYVNGKQVTE 80
                          90       100
                  ....*....|....*....|..
gi 530409731  578 PLVLKSGNRIVMGKNHVFRFNH 599
Cdd:cd22728    81 PLVLKSGNRIVMGKNHVFRFNH 102
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
516-597 1.60e-05

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 44.56  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  516 YHIKDGVTRVG-QVDMDIKLTGQFIREQHCLFRsipqPDGEVVVtLEPCEGA-ETYVNGKLVTEPLVLKSGNRIVMGKnH 593
Cdd:COG1716    16 FPLDGGPLTIGrAPDNDIVLDDPTVSRRHARIR----RDGGGWV-LEDLGSTnGTFVNGQRVTEPAPLRDGDVIRLGK-T 89

                  ....
gi 530409731  594 VFRF 597
Cdd:COG1716    90 ELRF 93
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
531-575 5.34e-03

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 36.00  E-value: 5.34e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 530409731    531 DIKLTGQFIREQHCLFRSipqpDGEVVVTLEPC-EGAETYVNGKLV 575
Cdd:smart00240   11 DIQLDGPSISRRHAVIVY----DGGGRFYLIDLgSTNGTFVNGKRI 52
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
4-355 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: 646.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    4 ASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQS-------KDAPKSFTFDYSYWSHTStEDPQFASQQQVYRD 76
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQAdknnkatREVPKSFSFDYSYWSHDS-EDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   77 IGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEpgQQGIVPQLCEDLFSRVSENQSAQLSYSVEVSYMEIYCERVRD 156
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  157 LLNPKS---RGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQL 233
Cdd:cd01365   158 LLNPKPkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  234 TGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMQSKK--RKSDFIPYRDSVLTWLLKE 311
Cdd:cd01365   238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKskKKSSFIPYRDSVLTWLLKE 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 530409731  312 NLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAIIN 355
Cdd:cd01365   318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
5-355 3.30e-157

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: 469.75  E-value: 3.30e-157
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731      5 SVKVAVRVRPFNARETSQDAKCVVSMQGN---TTSIINPKQSKDApKSFTFDYSYwshtstedPQFASQQQVYRDIGEEM 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKvgkTLTVRSPKNRQGE-KKFTFDKVF--------DATASQEDVFEETAAPL 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731     82 LLHAFEGYNVCIFAYGQTGAGKSYTMMGrqEPGQQGIVPQLCEDLFSRVsENQSAQLSYSVEVSYMEIYCERVRDLLNPk 161
Cdd:smart00129   72 VDSVLEGYNATIFAYGQTGSGKTYTMIG--TPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP- 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    162 SRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDqlTGLDSEKV 241
Cdd:smart00129  148 SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN--SSSGSGKA 225
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    242 SKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMQskkrKSDFIPYRDSVLTWLLKENLGGNSRTAM 321
Cdd:smart00129  226 SKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTLM 301
                           330       340       350
                    ....*....|....*....|....*....|....
gi 530409731    322 IAALSPADINYEETLSTLRYADRTKQIRCNAIIN 355
Cdd:smart00129  302 IANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
5-346 1.24e-152

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: 457.49  E-value: 1.24e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    5 SVKVAVRVRPFNAREtSQDAKCVVSMQG-NTTSIINPKQSKDAPKSFTFDYSYWSHtstedpqfASQQQVYRDIGEEMLL 83
Cdd:cd00106     1 NVRVAVRVRPLNGRE-ARSAKSVISVDGgKSVVLDPPKNRVAPPKTFAFDAVFDST--------STQEEVYEGTAKPLVD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   84 HAFEGYNVCIFAYGQTGAGKSYTMMGRQePGQQGIVPQLCEDLFSRVSENQSAQLSYSVEVSYMEIYCERVRDLLNPKSR 163
Cdd:cd00106    72 SALEGYNGTIFAYGQTGSGKTYTMLGPD-PEQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLLSPVPK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  164 GSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQltGLDSEKVSK 243
Cdd:cd00106   151 KPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREK--SGESVTSSK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  244 ISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMQSKkrksdFIPYRDSVLTWLLKENLGGNSRTAMIA 323
Cdd:cd00106   229 LNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK-----HIPYRDSKLTRLLQDSLGGNSKTIMIA 303
                         330       340
                  ....*....|....*....|...
gi 530409731  324 ALSPADINYEETLSTLRYADRTK 346
Cdd:cd00106   304 CISPSSENFEETLSTLRFASRAK 326
Kinesin pfam00225
Kinesin motor domain;
11-348 1.69e-152

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 457.03  E-value: 1.69e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    11 RVRPFNARETSQDAKCVVSM--QGNTTSIINPKQSKDAPKSFTFDYSYWSHtstedpqfASQQQVYRDIGEEMLLHAFEG 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVesVDSETVESSHLTNKNRTKTFTFDKVFDPE--------ATQEDVYEETAKPLVESVLEG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    89 YNVCIFAYGQTGAGKSYTMMGRQEpgQQGIVPQLCEDLFSRVSENQSaQLSYSVEVSYMEIYCERVRDLLNP--KSRGSL 166
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDE--QPGIIPRALEDLFDRIQKTKE-RSEFSVKVSYLEIYNEKIRDLLSPsnKNKRKL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   167 RVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQlTGLDSEKVSKISL 246
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRST-GGEESVKTGKLNL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   247 VDLAGSERADSSG-ARGMRLKEGANINKSLTTLGKVISALADMQSKkrksdFIPYRDSVLTWLLKENLGGNSRTAMIAAL 325
Cdd:pfam00225  229 VDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSK-----HIPYRDSKLTRLLQDSLGGNSKTLMIANI 303
                          330       340
                   ....*....|....*....|...
gi 530409731   326 SPADINYEETLSTLRYADRTKQI 348
Cdd:pfam00225  304 SPSSSNYEETLSTLRFASRAKNI 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
5-348 6.77e-120

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: 372.18  E-value: 6.77e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    5 SVKVAVRVRPFNARETSQDAKCVVSM--QGNTTSIINPKQ-SKDAPKSFTFDYSYwshtstedPQFASQQQVYRDIGEEM 81
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVdeKRGQVSVRNPKAtANEPPKTFTFDAVF--------DPNSKQLDVYDETARPL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   82 LLHAFEGYNVCIFAYGQTGAGKSYTMMG-RQEPGQQGIVPQLCEDLFSRVSENQSAQlSYSVEVSYMEIYCERVRDLLNP 160
Cdd:cd01371    74 VDSVLEGYNGTIFAYGQTGTGKTYTMEGkREDPELRGIIPNSFAHIFGHIARSQNNQ-QFLVRVSYLEIYNEEIRDLLGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  161 KSRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIvfTQRCHDQltGLDSE- 239
Cdd:cd01371   153 DQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTI--TIECSEK--GEDGEn 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  240 --KVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADmqskkRKSDFIPYRDSVLTWLLKENLGGNS 317
Cdd:cd01371   229 hiRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----GKSTHIPYRDSKLTRLLQDSLGGNS 303
                         330       340       350
                  ....*....|....*....|....*....|.
gi 530409731  318 RTAMIAALSPADINYEETLSTLRYADRTKQI 348
Cdd:cd01371   304 KTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
5-349 3.05e-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: 347.01  E-value: 3.05e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    5 SVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIInpkqsKDAPKSFTFDYSYwshtsteDPQfASQQQVYRDIGEEMLLH 84
Cdd:cd01372     2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT-----VGTDKSFTFDYVF-------DPS-TEQEEVYNTCVAPLVDG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   85 AFEGYNVCIFAYGQTGAGKSYTMMG----RQEPGQQGIVPQLCEDLFSRVSENQSaQLSYSVEVSYMEIYCERVRDLLNP 160
Cdd:cd01372    69 LFEGYNATVLAYGQTGSGKTYTMGTaytaEEDEEQVGIIPRAIQHIFKKIEKKKD-TFEFQLKVSFLEIYNEEIRDLLDP 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  161 --KSRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQLTGLDS 238
Cdd:cd01372   148 etDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  239 EK------VSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADmqsKKRKSDFIPYRDSVLTWLLKEN 312
Cdd:cd01372   228 ADdknstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGD---ESKKGAHVPYRDSKLTRLLQDS 304
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 530409731  313 LGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIR 349
Cdd:cd01372   305 LGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
5-348 7.43e-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: 345.08  E-value: 7.43e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    5 SVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIInpkQSKDAPKSFTFDYSYwshtstedPQFASQQQVYRDIGEEMLLH 84
Cdd:cd01369     3 NIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVI---ATSETGKTFSFDRVF--------DPNTTQEDVYNFAAKPIVDD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   85 AFEGYNVCIFAYGQTGAGKSYTMMG-RQEPGQQGIVPQLCEDLFSRVSENqSAQLSYSVEVSYMEIYCERVRDLLNPkSR 163
Cdd:cd01369    72 VLNGYNGTIFAYGQTSSGKTYTMEGkLGDPESMGIIPRIVQDIFETIYSM-DENLEFHVKVSYFEIYMEKIRDLLDV-SK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  164 GSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRchDQLTGldSEKVSK 243
Cdd:cd01369   150 TNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE--NVETE--KKKSGK 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  244 ISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADmqskkRKSDFIPYRDSVLTWLLKENLGGNSRTAMIA 323
Cdd:cd01369   226 LYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----GKKTHIPYRDSKLTRILQDSLGGNSRTTLII 300
                         330       340
                  ....*....|....*....|....*
gi 530409731  324 ALSPADINYEETLSTLRYADRTKQI 348
Cdd:cd01369   301 CCSPSSYNESETLSTLRFGQRAKTI 325
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
5-348 1.81e-105

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: 334.31  E-value: 1.81e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    5 SVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQSKDAPKSFTFDYSYWSHTSTEDPQF---------ASQQQVYR 75
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGFFHGGSNNRDRRKRRNKELKYvfdrvfdetSTQEEVYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   76 DIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMG-RQEPGqqgIVPQLCEDLFSRVsENQSAQLSYSVEVSYMEIYCERV 154
Cdd:cd01370    81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGtPQEPG---LMVLTMKELFKRI-ESLKDEKEFEVSMSYLEIYNETI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  155 RDLLNPKSrGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRchDQLT 234
Cdd:cd01370   157 RDLLNPSS-GPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQ--DKTA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  235 GLDSE-KVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADmqsKKRKSDFIPYRDSVLTWLLKENL 313
Cdd:cd01370   234 SINQQvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD---PGKKNKHIPYRDSKLTRLLKDSL 310
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 530409731  314 GGNSRTAMIAALSPADINYEETLSTLRYADRTKQI 348
Cdd:cd01370   311 GGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
11-350 1.03e-104

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: 331.87  E-value: 1.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   11 RVRPFNARETSQDAKCVVSMQGNTTSIINPKQSkDAPKSFTFDYSYwshtsteDPQfASQQQVYRDIgeEMLLH-AFEGY 89
Cdd:cd01366     9 RVRPLLPSEENEDTSHITFPDEDGQTIELTSIG-AKQKEFSFDKVF-------DPE-ASQEDVFEEV--SPLVQsALDGY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   90 NVCIFAYGQTGAGKSYTMMGRQEpgQQGIVPQLCEDLFSRVSENQSAQLSYSVEVSYMEIYCERVRDLLNPKSRGSLR-- 167
Cdd:cd01366    78 NVCIFAYGQTGSGKTYTMEGPPE--SPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLLAPGNAPQKKle 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  168 VREHPILGP-YVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFtqRCHDQLTGLDSekVSKISL 246
Cdd:cd01366   156 IRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--SGRNLQTGEIS--VGKLNL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  247 VDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALAdmqskkRKSDFIPYRDSVLTWLLKENLGGNSRTAMIAALS 326
Cdd:cd01366   232 VDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNIS 305
                         330       340
                  ....*....|....*....|....
gi 530409731  327 PADINYEETLSTLRYADRTKQIRC 350
Cdd:cd01366   306 PAESNLNETLNSLRFASKVNSCEL 329
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
5-348 8.69e-104

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: 328.91  E-value: 8.69e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    5 SVKVAVRVRPFNARETSQDAKCVVSMQGNTTSiinpkQSKDAPKSFTFDYSYWSHTSTEdpqfasqqQVYRDIGEEMLLH 84
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIY-----LVEPPSTSFTFDHVFGGDSTNR--------EVYELIAKPVVKS 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   85 AFEGYNVCIFAYGQTGAGKSYTMMG-RQEPGqqgIVPQLCEDLFSRVSENQSAQlsYSVEVSYMEIYCERVRDLLNPKSR 163
Cdd:cd01374    68 ALEGYNGTIFAYGQTSSGKTFTMSGdEDEPG---IIPLAIRDIFSKIQDTPDRE--FLLRVSYLEIYNEKINDLLSPTSQ 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  164 gSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQLTGlDSEKVSK 243
Cdd:cd01374   143 -NLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEE-GTVRVST 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  244 ISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALadmqSKKRKSDFIPYRDSVLTWLLKENLGGNSRTAMIA 323
Cdd:cd01374   221 LNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKL----SEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIIC 296
                         330       340
                  ....*....|....*....|....*
gi 530409731  324 ALSPADINYEETLSTLRYADRTKQI 348
Cdd:cd01374   297 TITPAESHVEETLNTLKFASRAKKI 321
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
6-357 1.74e-98

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: 315.60  E-value: 1.74e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    6 VKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQskdaPKSFTFDYSYWSHTSTEDpqfasqqqVYRDIGEEMLLHA 85
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKP----PKTFTFDHVADSNTNQES--------VFQSVGKPIVESC 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   86 FEGYNVCIFAYGQTGAGKSYTMMGRQEP------GQQGIVPQLCEDLFSRVS---ENQSAQLSYSVEVSYMEIYCERVRD 156
Cdd:cd01373    71 LSGYNGTIFAYGQTGSGKTYTMWGPSESdnesphGLRGVIPRIFEYLFSLIQrekEKAGEGKSFLCKCSFLEIYNEQIYD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  157 LLNPKSRGsLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDqlTGL 236
Cdd:cd01373   151 LLDPASRN-LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKK--ACF 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  237 DSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMQSKKrkSDFIPYRDSVLTWLLKENLGGN 316
Cdd:cd01373   228 VNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGK--QRHVCYRDSKLTFLLRDSLGGN 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 530409731  317 SRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAIINED 357
Cdd:cd01373   306 AKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
3-357 9.73e-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: 305.79  E-value: 9.73e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    3 GASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSII---NPKQSKDAPKSFTFDYSYwshtsteDPQfASQQQVYRDIGE 79
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSvrtGGLADKSSTKTYTFDMVF-------GPE-AKQIDVYRSVVC 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   80 EMLLHAFEGYNVCIFAYGQTGAGKSYTMMGR---------QEPGQQGIVPQLCEDLFSRVSENQSaqlSYSVEVSYMEIY 150
Cdd:cd01364    73 PILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwELDPLAGIIPRTLHQLFEKLEDNGT---EYSVKVSYLEIY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  151 CERVRDLLNPKSRGSLRVREHPIL----GPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFt 226
Cdd:cd01364   150 NEELFDLLSPSSDVSERLRMFDDPrnkrGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITI- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  227 qrcHDQLTGLDSE---KVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADmqskkrKSDFIPYRDS 303
Cdd:cd01364   229 ---HIKETTIDGEelvKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------RAPHVPYRES 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530409731  304 VLTWLLKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAIINED 357
Cdd:cd01364   300 KLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
68-399 5.56e-82

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 278.55  E-value: 5.56e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   68 ASQQQVYRDIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGrqEPGQQGIVPQLCEDLFSRVsENQSAQLSYSVEVSYM 147
Cdd:COG5059    68 ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG--TEEEPGIIPLSLKELFSKL-EDLSMTKDFAVSISYL 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  148 EIYCERVRDLLNPKSRgSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQ 227
Cdd:COG5059   145 EIYNEKIYDLLSPNEE-SLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELAS 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  228 RChdqlTGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALadmqSKKRKSDFIPYRDSVLTW 307
Cdd:COG5059   224 KN----KVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINAL----GDKKKSGHIPYRESKLTR 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  308 LLKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIR-----CNAIINEDPNARL---IRELQEEVARLRELLmA 379
Cdd:COG5059   296 LLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKnkiqvNSSSDSSREIEEIkfdLSEDRSEIEILVFRE-Q 374
                         330       340
                  ....*....|....*....|
gi 530409731  380 QGLSASALEGLKTEEGSVRG 399
Cdd:COG5059   375 SQLSQSSLSGIFAYMQSLKK 394
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
6-346 5.92e-78

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: 259.15  E-value: 5.92e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    6 VKVAVRVRPFNARETSQDAKCVVSMQGNTTSIIN-PKQSKDAPK-----SFTFDYSYwshtsTEDpqfASQQQVYRDIGE 79
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHePKLKVDLTKyienhTFRFDYVF-----DES---SSNETVYRSTVK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   80 EMLLHAFEGYNVCIFAYGQTGAGKSYTMMGR--QEPGQQGIVPQLCEDLFSRVSENQSAqLSYSVEVSYMEIYCERVRDL 157
Cdd:cd01367    74 PLVPHIFEGGKATCFAYGQTGSGKTYTMGGDfsGQEESKGIYALAARDVFRLLNKLPYK-DNLGVTVSFFEIYGGKVFDL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  158 LNPKSRgsLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQLTGld 237
Cdd:cd01367   153 LNRKKR--VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNKLHG-- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  238 sekvsKISLVDLAGSER-ADSSGARGMRLKEGANINKSLTTLGKVISALADMQSKkrksdfIPYRDSVLTWLLKENL-GG 315
Cdd:cd01367   229 -----KLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAH------IPFRGSKLTQVLKDSFiGE 297
                         330       340       350
                  ....*....|....*....|....*....|.
gi 530409731  316 NSRTAMIAALSPADINYEETLSTLRYADRTK 346
Cdd:cd01367   298 NSKTCMIATISPGASSCEHTLNTLRYADRVK 328
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
6-346 5.63e-75

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: 251.54  E-value: 5.63e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    6 VKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQSKDAPKS----------FTFDYSYWSHTStedpqfasQQQVYR 75
Cdd:cd01368     3 VKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSernggqketkFSFSKVFGPNTT--------QKEFFQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   76 DIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGrqEPGQQGIVPQLCEDLFSRVSEnqsaqlsYSVEVSYMEIYCERVR 155
Cdd:cd01368    75 GTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQG--SPGDGGILPRSLDVIFNSIGG-------YSVFVSYIEIYNEYIY 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  156 DLLNP------KSRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQrC 229
Cdd:cd01368   146 DLLEPspssptKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQ-A 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  230 HDQLTGL-----DSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMQsKKRKSDFIPYRDSV 304
Cdd:cd01368   225 PGDSDGDvdqdkDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQ-LQGTNKMVPFRDSK 303
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 530409731  305 LTWLLKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTK 346
Cdd:cd01368   304 LTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
PLN03188 PLN03188
kinesin-12 family protein; Provisional
1-374 1.49e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 270.27  E-value: 1.49e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    1 MAGASVKVAVRVRPFNAREtsQDAKCVVSMQGNTTSIINpkqskdapKSFTFDysywshtSTEDPQfASQQQVYRDIGEE 80
Cdd:PLN03188   95 VSDSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTING--------QTFTFD-------SIADPE-STQEDIFQLVGAP 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   81 MLLHAFEGYNVCIFAYGQTGAGKSYTMMG--------RQEPGQQGIVPQLCEDLFSRVSENQ----SAQLSYSVEVSYME 148
Cdd:PLN03188  157 LVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglleeHLSGDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRCSFLE 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  149 IYCERVRDLLNPKSRgSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQR 228
Cdd:PLN03188  237 IYNEQITDLLDPSQK-NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESR 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  229 CHDQLTGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMqSKKRKSDFIPYRDSVLTWL 308
Cdd:PLN03188  316 CKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEI-SQTGKQRHIPYRDSRLTFL 394
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530409731  309 LKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAIINE----DPN--ARLIRELQEEVARLR 374
Cdd:PLN03188  395 LQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
Kinesin_assoc pfam16183
Kinesin-associated;
352-522 4.05e-74

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 242.83  E-value: 4.05e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   352 AIINEDPNARLIRELQEEVARLRELLMAQGLSasalEGLKTEEGSVRGALPAVSSPPAPVSPSSPTTHNGELEPSFSPNT 431
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLG----DIIDTIAHPTKKRANTPAANASAATAAMAGASPSPSLSALSSRA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   432 ESQI----------GPEEAMERLQETEKIIAELNETWEEKLRKTEALRMEREALLAEMGVAVREDGGTVGVFSPKKTPHL 501
Cdd:pfam16183   77 ASVSslherimftpGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHL 156
                          170       180
                   ....*....|....*....|.
gi 530409731   502 VNLNEDPLMSECLLYHIKDGV 522
Cdd:pfam16183  157 VNLNEDPLMSECLLYYIKDGI 177
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
498-599 3.08e-71

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: 231.68  E-value: 3.08e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  498 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDMDIKLTGQFIREQHCLFRSIPQPDGEVVVTLEPCEGAETYVNGKLVTE 577
Cdd:cd22728     1 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVDIKLSGQFIREQHCLFRSIPNPSGEVVVTLEPCEGAETYVNGKQVTE 80
                          90       100
                  ....*....|....*....|..
gi 530409731  578 PLVLKSGNRIVMGKNHVFRFNH 599
Cdd:cd22728    81 PLVLKSGNRIVMGKNHVFRFNH 102
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
6-346 1.35e-70

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: 238.56  E-value: 1.35e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    6 VKVAVRVRPFNARETSQDAK-CVVSMQGNTTSIINPKQSKDaPKSFTFDYSYwshtSTEDpqfaSQQQVYRDIGEEMLLH 84
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPsCVSGIDSCSVELADPRNHGE-TLKYQFDAFY----GEES----TQEDIYAREVQPIVPH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   85 AFEGYNVCIFAYGQTGAGKSYTMMGrqEPGQQGIVPQLCEDLfsrVSENQSAQLSYSVEVSYMEIYCERVRDLLNPKSrG 164
Cdd:cd01376    73 LLEGQNATVFAYGSTGAGKTFTMLG--SPEQPGLMPLTVMDL---LQMTRKEAWALSFTMSYLEIYQEKILDLLEPAS-K 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  165 SLRVRE---HPILgpyVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRchdQLTGLDSEKV 241
Cdd:cd01376   147 ELVIREdkdGNIL---IPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQR---ERLAPFRQRT 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  242 SKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALadmqsKKRKSDfIPYRDSVLTWLLKENLGGNSRTAM 321
Cdd:cd01376   221 GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL-----NKNLPR-IPYRDSKLTRLLQDSLGGGSRCIM 294
                         330       340
                  ....*....|....*....|....*
gi 530409731  322 IAALSPADINYEETLSTLRYADRTK 346
Cdd:cd01376   295 VANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
5-346 3.91e-66

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: 226.69  E-value: 3.91e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    5 SVKVAVRVRPfnareTSQDAKCVVSM--QGNTTSIINPKQSKDAP-----KSFTFDYSYWSHTstedpqfASQQQVYRDI 77
Cdd:cd01375     1 KVQAFVRVRP-----TDDFAHEMIKYgeDGKSISIHLKKDLRRGVvnnqqEDWSFKFDGVLHN-------ASQELVYETV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   78 GEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEP-GQQGIVPQLCEDLFSRVSENQSAqlSYSVEVSYMEIYCERVRD 156
Cdd:cd01375    69 AKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENyKHRGIIPRALQQVFRMIEERPTK--AYTVHVSYLEIYNEQLYD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  157 LLNPK-----SRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHD 231
Cdd:cd01375   147 LLSTLpyvgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRT 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  232 qltgLDSEKV--SKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADmqskkRKSDFIPYRDSVLTWLL 309
Cdd:cd01375   227 ----LSSEKYitSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----KDRTHVPFRQSKLTHVL 297
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 530409731  310 KENLGGNSRTAMIAALSPADINYEETLSTLRYADRTK 346
Cdd:cd01375   298 RDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
498-608 7.20e-63

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: 208.63  E-value: 7.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  498 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVD----MDIKLTGQFIREQHCLFRSIPQPDGEVVVTLEPCEGAETYVNGK 573
Cdd:cd22726     1 TPHLVNLNEDPLMSECLLYYIKDGITRVGREDaerrQDIVLSGHFIKEEHCIFRSDTRSGGEAVVTLEPCEGADTYVNGK 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 530409731  574 LVTEPLVLKSGNRIVMGKNHVFRFNHPEQARLERE 608
Cdd:cd22726    81 KVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
497-602 5.48e-60

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: 200.26  E-value: 5.48e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  497 KTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVD----MDIKLTGQFIREQHCLFRSIPQPDGEVVVTLEPCEGAETYVNG 572
Cdd:cd22727     1 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADaerrQDIVLSGAHIKEEHCIFRSERNNNGEVIVTLEPCERSETYVNG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 530409731  573 KLVTEPLVLKSGNRIVMGKNHVFRFNHPEQ 602
Cdd:cd22727    81 KRVVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
498-599 1.84e-58

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: 195.53  E-value: 1.84e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  498 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDM----DIKLTGQFIREQHCLFRSIpqpdgEVVVTLEPCEGAETYVNGK 573
Cdd:cd22705     1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADAdvpqDIQLSGTHILEEHCTFENE-----DGVVTLEPCEGALTYVNGK 75
                          90       100
                  ....*....|....*....|....*.
gi 530409731  574 LVTEPLVLKSGNRIVMGKNHVFRFNH 599
Cdd:cd22705    76 RVTEPTRLKTGSRVILGKNHVFRFNH 101
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
497-600 1.02e-35

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: 131.23  E-value: 1.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  497 KTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDM----DIKLTGQFIREQHCLFRSIpqpdgEVVVTLEPCEGAETYVNG 572
Cdd:cd22707     6 KLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKAssshDIQLSGALIADDHCTIENN-----GGKVTIIPVGDAETYVNG 80
                          90       100
                  ....*....|....*....|....*...
gi 530409731  573 KLVTEPLVLKSGNRIVMGKNHVFRFNHP 600
Cdd:cd22707    81 ELISEPTVLHHGDRVILGGDHYFRFNHP 108
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
8-284 2.22e-32

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: 123.99  E-value: 2.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731    8 VAVRVRPFNARETSQDAKCVVSMQGnttsiinpkqskdapksftfdysywshtsteDPQFASQQQVYRDIGEeMLLHAFE 87
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKIIVFYRG-------------------------------FRRSESQPHVFAIADP-AYQSMLD 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   88 GYNV-CIFAYGQTGAGKSYTMMGrqepgqqgIVPQLCEDLFSRVSENQSAQLSYsvevsymeiycervrdllnpksrgsl 166
Cdd:cd01363    49 GYNNqSIFAYGESGAGKTETMKG--------VIPYLASVAFNGINKGETEGWVY-------------------------- 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  167 rvrehpilgpyvqdLSKLAVTSYADIADLMDCGNKARTvAATNMNETSSRSHAVFTIVftqrchdqltgldsekvskisl 246
Cdd:cd01363    95 --------------LTEITVTLEDQILQANPILEAFGN-AKTTRNENSSRFGKFIEIL---------------------- 137
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 530409731  247 VDLAGSERadssgargmrlkeganINKSLTTLGKVISA 284
Cdd:cd01363   138 LDIAGFEI----------------INESLNTLMNVLRA 159
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
499-600 1.22e-30

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: 116.16  E-value: 1.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  499 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDM----DIKLTGQFIREQHCLFRSIpqpDGEVvvTLEPC-EGAETYVNGK 573
Cdd:cd22709     1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAepepDIVLSGLSIQKQHAVITNT---DGKV--TIEPVsPGAKVIVNGV 75
                          90       100
                  ....*....|....*....|....*..
gi 530409731  574 LVTEPLVLKSGNRIVMGKNHVFRFNHP 600
Cdd:cd22709    76 PVTGETELHHLDRVILGSNHLYVFVGP 102
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
497-600 2.07e-30

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: 115.83  E-value: 2.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  497 KTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVD----MDIKLTGQFIREQHCLFRSIpqpDGevVVTLEPCEGAETYVNG 572
Cdd:cd22708     7 ELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDapqeQDIVLDGEDIEAEHCIIENV---GG--VVTLHPLPGALCAVNG 81
                          90       100
                  ....*....|....*....|....*...
gi 530409731  573 KLVTEPLVLKSGNRIVMGKNHVFRFNHP 600
Cdd:cd22708    82 QVITQPTRLTQGDVILLGKTNMFRFNHP 109
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
491-609 2.44e-28

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: 110.25  E-value: 2.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  491 GVFSPKKTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVD----MDIKLTGQFIREQHCLfrsIPQPDGevVVTLEPCEGA 566
Cdd:cd22731     1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDseqeQDIVLQGPWIERDHCM---IHNECG--VVTLRPAQGA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 530409731  567 ETYVNGKLVTEPLVLKSGNRIVMGKNHVFRFNHPEQARLERER 609
Cdd:cd22731    76 QCTVNGREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQR 118
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
501-600 6.53e-26

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: 102.76  E-value: 6.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  501 LVNLNEDPLMSECLLYHIKDgVTRVGQVD----MDIKLTGQFIREQHCLfrsIPQPDGEVVVTlePCEGAETYVNGKLVT 576
Cdd:cd22706     4 LVNLNADPSLNELLVYYLKE-HTLIGRSDaptqQDIQLSGLGIQPEHCI---ITIENEDVYLT--PLEGARTCVNGSIVT 77
                          90       100
                  ....*....|....*....|....
gi 530409731  577 EPLVLKSGNRIVMGKNHVFRFNHP 600
Cdd:cd22706    78 EKTQLRHGDRILWGNNHFFRLNCP 101
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
491-608 3.77e-21

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: 89.99  E-value: 3.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  491 GVFSPKKTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVD----MDIKLTGQFIREQHCLFRSIPQpdgevVVTLEPCEGA 566
Cdd:cd22732     1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDatteQDIVLHGLDLESEHCIFENLNG-----TVTLIPLNGA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 530409731  567 ETYVNGKLVTEPLVLKSGNRIVMGKNHVFRFNHPEQARLERE 608
Cdd:cd22732    76 QCSVNGVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
501-607 5.48e-20

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: 86.10  E-value: 5.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  501 LVNLNEDPLMSECLLYHIKDGvTRVG-QVDMDIKLTGQFIREQHCLFRSipQPDGEVVVTlePCEGAETYVNGKLVTEPL 579
Cdd:cd22729     4 LVNLNADPALNELLVYYLKDH-TRVGaDTSQDIQLFGIGIQPEHCVIDI--AADGDVTLT--PKENARTCVNGTLVCSVT 78
                          90       100
                  ....*....|....*....|....*...
gi 530409731  580 VLKSGNRIVMGKNHVFRFNHPEQARLER 607
Cdd:cd22729    79 QLWHGDRILWGNNHFFRINLPKRKRRDW 106
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
501-600 1.53e-19

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: 84.58  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  501 LVNLNEDPLMSECLLYHIKDGvTRVGQVD-MDIKLTGQFIREQHCLFRSipQPDGEVVVTlePCEGAETYVNGKLVTEPL 579
Cdd:cd22730     4 LVNLNADPALNELLVYYLKEH-TLIGSADsQDIQLCGMGILPEHCIIDI--TPEGQVMLT--PQKNTRTFVNGSAVTSPI 78
                          90       100
                  ....*....|....*....|.
gi 530409731  580 VLKSGNRIVMGKNHVFRFNHP 600
Cdd:cd22730    79 QLHHGDRILWGNNHFFRINLP 99
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
499-603 2.07e-15

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: 73.51  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  499 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDMD-IKLTGQFIREQHCLFRSIpqpDGEVvvTLEPCEGAETyVNGKLVTE 577
Cdd:cd22713    17 PHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDiISLQGPGVEPEHCYIENI---NGTV--TLYPCGNLCS-VDGLPITE 90
                          90       100
                  ....*....|....*....|....*.
gi 530409731  578 PLVLKSGNRIVMGKNHVFRFNHPEQA 603
Cdd:cd22713    91 PTRLTQGCMICLGRSNYFRFNHPAEA 116
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
499-600 4.80e-14

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: 69.27  E-value: 4.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  499 PHLVNLNEDPLMSECL-LYHIKDGVTRVGQVDMD------IKLTGQFIREQHCLFRSIpqpDGEVVVTlePCEG-AETYV 570
Cdd:cd22711     2 PYLLELSPDGSDRDKPrRHRLQPNVTEVGSERSPansgqfIQLFGPDILPRHCVITHM---EGVVTVT--PASQdAETYV 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 530409731  571 NGKLVTEPLVLKSGNRIVMGKNHVFRFNHP 600
Cdd:cd22711    77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
5-158 6.61e-14

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 69.94  E-value: 6.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731     5 SVKVAVRVRPFNAREtsqdakCVVSMQGNTTSIINPKQSKdapKSFTFDYSYwshtstedPQFASQQQVYRDIgeEMLLH 84
Cdd:pfam16796   21 NIRVFARVRPELLSE------AQIDYPDETSSDGKIGSKN---KSFSFDRVF--------PPESEQEDVFQEI--SQLVQ 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530409731    85 -AFEGYNVCIFAYGQTGAGKSYTMmgrqepgqqgiVPQLCEDLFsRVSENQSAQLSYSVEVSYMEIYCERVRDLL 158
Cdd:pfam16796   82 sCLDGYNVCIFAYGQTGSGSNDGM-----------IPRAREQIF-RFISSLKKGWKYTIELQFVEIYNESSQDLL 144
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
498-600 6.90e-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: 57.70  E-value: 6.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  498 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDM-----DIKLTGQFIREQHCLFRSIPQPDGEV----------VVTLEP 562
Cdd:cd22712     3 YPYLLTLRGFSPKQDLLVYPLLEQVILVGSRTEgarkvDISLRAPDILPQHCWIRRKPEPLSDDedsdkesadyRVVLSP 82
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 530409731  563 CEGAETYVNGKLVTEPLVLKSGNRIVMGKNHVFRFNHP 600
Cdd:cd22712    83 LRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
500-597 1.52e-09

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: 55.74  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  500 HLVNLNEDPLMSEcllYHIKDGVTRVG-QVDMDIKLTGQFIREQHCLFRSIpqpDGEVVVT-LEPCEGaeTYVNGKLVTE 577
Cdd:cd00060     1 RLIVLDGDGGGRE---FPLTKGVVTIGrSPDCDIVLDDPSVSRRHARIEVD---GGGVYLEdLGSTNG--TFVNGKRITP 72
                          90       100
                  ....*....|....*....|
gi 530409731  578 PLVLKSGNRIVMGkNHVFRF 597
Cdd:cd00060    73 PVPLQDGDVIRLG-DTTFRF 91
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
516-597 1.60e-05

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 44.56  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  516 YHIKDGVTRVG-QVDMDIKLTGQFIREQHCLFRsipqPDGEVVVtLEPCEGA-ETYVNGKLVTEPLVLKSGNRIVMGKnH 593
Cdd:COG1716    16 FPLDGGPLTIGrAPDNDIVLDDPTVSRRHARIR----RDGGGWV-LEDLGSTnGTFVNGQRVTEPAPLRDGDVIRLGK-T 89

                  ....
gi 530409731  594 VFRF 597
Cdd:COG1716    90 ELRF 93
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
497-600 3.68e-05

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: 44.02  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  497 KTPHLVNLNEDPLMSECLLYHIKDGVTRVGQ----VDMDIKLTGQFIREQHCLFRSIPQPDG--EVVVTLEPCEGAETYV 570
Cdd:cd22733     4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQetpsSKPNISLSAPDILPLHCTIRRVRLPKHrsEEKLVLEPIPGAHVSV 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 530409731  571 NGKLVTEPLVLKSGNRIVMGKNHVFRFNHP 600
Cdd:cd22733    84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
531-597 1.29e-04

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: 41.81  E-value: 1.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530409731  531 DIKLTGQFIREQHCLFRsipqPDGEVVVTLEP-CEGAETYVNGKLVTEPLVLKSGNRIVMGkNHVFRF 597
Cdd:cd22673    32 DIRIQLPGVSREHCRIE----VDENGKAYLENlSTTNPTLVNGKAIEKSAELKDGDVITIG-GRSFRF 94
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
93-285 1.49e-04

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 45.89  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731   93 IFAYGQTGAGKSYTMMGRQEpgqqGIVPQLCEDLFSRVSENQSAQLSYSVEVSYMEIYCervrdllnpKSRGSLRVREHP 172
Cdd:COG5059   385 IFAYMQSLKKETETLKSRID----LIMKSIISGTFERKKLLKEEGWKYKSTLQFLRIEI---------DRLLLLREEELS 451
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530409731  173 ILGPYVQDLSKL---AVTSYADIAD-----LMDCGNKA-RTVAATNMNETSSRSHAVFtivftqrCHDQLTGLDSEKVSK 243
Cdd:COG5059   452 KKKTKIHKLNKLrhdLSSLLSSIPEetsdrVESEKASKlRSSASTKLNLRSSRSHSKF-------RDHLNGSNSSTKELS 524
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 530409731  244 ISLVDLAGSERaDSSGARGMRLKEGANINKSLTTLGKVISAL 285
Cdd:COG5059   525 LNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
531-575 5.34e-03

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 36.00  E-value: 5.34e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 530409731    531 DIKLTGQFIREQHCLFRSipqpDGEVVVTLEPC-EGAETYVNGKLV 575
Cdd:smart00240   11 DIQLDGPSISRRHAVIVY----DGGGRFYLIDLgSTNGTFVNGKRI 52
 
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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