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Conserved domains on  [gi|1907080140|ref|XP_036012245|]
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kinesin-like protein KIF1C isoform X1 [Mus musculus]

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: 649.41  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    4 ASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQS-------KDAPKSFTFDYSYWSHTSvEDPQFASQQQVYRD 76
Cdd:cd01365      1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQAdknnkatREVPKSFSFDYSYWSHDS-EDPNYASQEQVYED 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   77 IGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEpgQQGIVPQLCEDLFSRVNVNQSAQLSYSVEVSYMEIYCERVRD 156
Cdd:cd01365     80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  157 LLNPKS---RGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHDQL 233
Cdd:cd01365    158 LLNPKPkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  234 TGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADLQSKK--RKSDFIPYRDSVLTWLLKE 311
Cdd:cd01365    238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKskKKSSFIPYRDSVLTWLLKE 317
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1907080140  312 NLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAVIN 355
Cdd:cd01365    318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
Kinesin_assoc pfam16183
Kinesin-associated;
352-522 6.28e-76

Kinesin-associated;


:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 247.83  E-value: 6.28e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  352 AVINEDPNARLIRELQEEVARLRDLLMAQGLSA---SALGGLKVEEGSPGGVLPPASSPPAPASPSSPPPHNGELEPSFS 428
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLGDiidTIAHPTKKRANTPAANASAATAAMAGASPSPSLSALSSRAASVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  429 PSAEPQI---GPEEAMERLQETEKIIAELNETWEEKLRKTEALRMEREALLAEMGVAVREDGGTVGVFSPKKTPHLVNLN 505
Cdd:pfam16183   81 SLHERIMftpGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLN 160
                          170
                   ....*....|....*..
gi 1907080140  506 EDPLMSECLLYHIKDGV 522
Cdd:pfam16183  161 EDPLMSECLLYYIKDGI 177
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
498-599 6.94e-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: 230.91  E-value: 6.94e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  498 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVDIKLTGQFIREQHCLFRSIPQPDGEVMVTLEPCEGAETYVNGKLVTE 577
Cdd:cd22728      1 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVDIKLSGQFIREQHCLFRSIPNPSGEVVVTLEPCEGAETYVNGKQVTE 80
                           90       100
                   ....*....|....*....|..
gi 1907080140  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: 649.41  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    4 ASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQS-------KDAPKSFTFDYSYWSHTSvEDPQFASQQQVYRD 76
Cdd:cd01365      1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQAdknnkatREVPKSFSFDYSYWSHDS-EDPNYASQEQVYED 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   77 IGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEpgQQGIVPQLCEDLFSRVNVNQSAQLSYSVEVSYMEIYCERVRD 156
Cdd:cd01365     80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  157 LLNPKS---RGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHDQL 233
Cdd:cd01365    158 LLNPKPkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  234 TGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADLQSKK--RKSDFIPYRDSVLTWLLKE 311
Cdd:cd01365    238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKskKKSSFIPYRDSVLTWLLKE 317
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1907080140  312 NLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAVIN 355
Cdd:cd01365    318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
5-355 6.21e-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: 469.36  E-value: 6.21e-157
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140     5 SVKVAVRVRPFNARETSQDAKCVVSMQGN---TTSIINPKQSKDApKSFTFDYSYwshtsvedPQFASQQQVYRDIGEEM 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKvgkTLTVRSPKNRQGE-KKFTFDKVF--------DATASQEDVFEETAAPL 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    82 LLHAFEGYNVCIFAYGQTGAGKSYTMMGrqEPGQQGIVPQLCEDLFSRVNvNQSAQLSYSVEVSYMEIYCERVRDLLNPk 161
Cdd:smart00129   72 VDSVLEGYNATIFAYGQTGSGKTYTMIG--TPDSPGIIPRALKDLFEKID-KREEGWQFSVKVSYLEIYNEKIRDLLNP- 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   162 SRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHDqlTGLDSEKV 241
Cdd:smart00129  148 SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN--SSSGSGKA 225
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   242 SKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADLQskkrKSDFIPYRDSVLTWLLKENLGGNSRTAM 321
Cdd:smart00129  226 SKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTLM 301
                           330       340       350
                    ....*....|....*....|....*....|....
gi 1907080140   322 IAALSPADINYEETLSTLRYADRTKQIRCNAVIN 355
Cdd:smart00129  302 IANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-348 3.13e-152

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 456.65  E-value: 3.13e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   11 RVRPFNARETSQDAKCVVSM--QGNTTSIINPKQSKDAPKSFTFDYSYWSHtsvedpqfASQQQVYRDIGEEMLLHAFEG 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVesVDSETVESSHLTNKNRTKTFTFDKVFDPE--------ATQEDVYEETAKPLVESVLEG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   89 YNVCIFAYGQTGAGKSYTMMGRQEpgQQGIVPQLCEDLFSRVNvNQSAQLSYSVEVSYMEIYCERVRDLLNP--KSRGSL 166
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDE--QPGIIPRALEDLFDRIQ-KTKERSEFSVKVSYLEIYNEKIRDLLSPsnKNKRKL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  167 RVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHDQlTGLDSEKVSKISL 246
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRST-GGEESVKTGKLNL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  247 VDLAGSERADSSG-ARGMRLKEGANINKSLTTLGKVISALADlqskkRKSDFIPYRDSVLTWLLKENLGGNSRTAMIAAL 325
Cdd:pfam00225  229 VDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANI 303
                          330       340
                   ....*....|....*....|...
gi 1907080140  326 SPADINYEETLSTLRYADRTKQI 348
Cdd:pfam00225  304 SPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
68-355 3.69e-81

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 276.23  E-value: 3.69e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   68 ASQQQVYRDIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGrqEPGQQGIVPQLCEDLFSRvNVNQSAQLSYSVEVSYM 147
Cdd:COG5059     68 ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG--TEEEPGIIPLSLKELFSK-LEDLSMTKDFAVSISYL 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  148 EIYCERVRDLLNPKSRgSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQ 227
Cdd:COG5059    145 EIYNEKIYDLLSPNEE-SLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELAS 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  228 RshDQLTGLDSEkvSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALadlqSKKRKSDFIPYRDSVLTW 307
Cdd:COG5059    224 K--NKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINAL----GDKKKSGHIPYRESKLTR 295
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1907080140  308 LLKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAVIN 355
Cdd:COG5059    296 LLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
Kinesin_assoc pfam16183
Kinesin-associated;
352-522 6.28e-76

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 247.83  E-value: 6.28e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  352 AVINEDPNARLIRELQEEVARLRDLLMAQGLSA---SALGGLKVEEGSPGGVLPPASSPPAPASPSSPPPHNGELEPSFS 428
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLGDiidTIAHPTKKRANTPAANASAATAAMAGASPSPSLSALSSRAASVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  429 PSAEPQI---GPEEAMERLQETEKIIAELNETWEEKLRKTEALRMEREALLAEMGVAVREDGGTVGVFSPKKTPHLVNLN 505
Cdd:pfam16183   81 SLHERIMftpGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLN 160
                          170
                   ....*....|....*..
gi 1907080140  506 EDPLMSECLLYHIKDGV 522
Cdd:pfam16183  161 EDPLMSECLLYYIKDGI 177
PLN03188 PLN03188
kinesin-12 family protein; Provisional
1-375 7.30e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 268.34  E-value: 7.30e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    1 MAGASVKVAVRVRPFNAREtsQDAKCVVSMQGNTTSIINpkqskdapKSFTFDysywshtSVEDPQfASQQQVYRDIGEE 80
Cdd:PLN03188    95 VSDSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTING--------QTFTFD-------SIADPE-STQEDIFQLVGAP 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   81 MLLHAFEGYNVCIFAYGQTGAGKSYTMMG--------RQEPGQQGIVPQLCEDLFSRVNVNQ----SAQLSYSVEVSYME 148
Cdd:PLN03188   157 LVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglleeHLSGDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRCSFLE 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  149 IYCERVRDLLNPKSRgSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQR 228
Cdd:PLN03188   237 IYNEQITDLLDPSQK-NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESR 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  229 SHDQLTGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADLqSKKRKSDFIPYRDSVLTWL 308
Cdd:PLN03188   316 CKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEI-SQTGKQRHIPYRDSRLTFL 394
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907080140  309 LKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAVINE----DPN--ARLIRELQEEVARLRD 375
Cdd:PLN03188   395 LQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVKA 467
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
498-599 6.94e-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: 230.91  E-value: 6.94e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  498 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVDIKLTGQFIREQHCLFRSIPQPDGEVMVTLEPCEGAETYVNGKLVTE 577
Cdd:cd22728      1 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVDIKLSGQFIREQHCLFRSIPNPSGEVVVTLEPCEGAETYVNGKQVTE 80
                           90       100
                   ....*....|....*....|..
gi 1907080140  578 PLVLKSGNRIVMGKNHVFRFNH 599
Cdd:cd22728     81 PLVLKSGNRIVMGKNHVFRFNH 102
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
523-589 6.13e-06

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 44.87  E-value: 6.13e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  523 TRVGQ-VDVDIKLTGQFIREQHCLFRSipqpDGEVMVTLEPC-EGAETYVNGKLVT-EPLVLKSGNRIVM 589
Cdd:pfam00498    1 VTIGRsPDCDIVLDDPSVSRRHAEIRY----DGGGRFYLEDLgSTNGTFVNGQRLGpEPVRLKDGDVIRL 66
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
516-597 1.26e-05

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 44.95  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  516 YHIKDGVTRVG-QVDVDIKLTGQFIREQHCLFRsiPQPDGevmVTLEPCEGA-ETYVNGKLVTEPLVLKSGNRIVMGKnH 593
Cdd:COG1716     16 FPLDGGPLTIGrAPDNDIVLDDPTVSRRHARIR--RDGGG---WVLEDLGSTnGTFVNGQRVTEPAPLRDGDVIRLGK-T 89

                   ....
gi 1907080140  594 VFRF 597
Cdd:COG1716     90 ELRF 93
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
529-575 1.17e-03

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 37.93  E-value: 1.17e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1907080140   529 DVDIKLTGQFIREQHCLFRSipqpDGEVMVTLEPC-EGAETYVNGKLV 575
Cdd:smart00240    9 DCDIQLDGPSISRRHAVIVY----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: 649.41  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    4 ASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQS-------KDAPKSFTFDYSYWSHTSvEDPQFASQQQVYRD 76
Cdd:cd01365      1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQAdknnkatREVPKSFSFDYSYWSHDS-EDPNYASQEQVYED 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   77 IGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEpgQQGIVPQLCEDLFSRVNVNQSAQLSYSVEVSYMEIYCERVRD 156
Cdd:cd01365     80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  157 LLNPKS---RGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHDQL 233
Cdd:cd01365    158 LLNPKPkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  234 TGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADLQSKK--RKSDFIPYRDSVLTWLLKE 311
Cdd:cd01365    238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKskKKSSFIPYRDSVLTWLLKE 317
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 1907080140  312 NLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAVIN 355
Cdd:cd01365    318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
5-355 6.21e-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: 469.36  E-value: 6.21e-157
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140     5 SVKVAVRVRPFNARETSQDAKCVVSMQGN---TTSIINPKQSKDApKSFTFDYSYwshtsvedPQFASQQQVYRDIGEEM 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKvgkTLTVRSPKNRQGE-KKFTFDKVF--------DATASQEDVFEETAAPL 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    82 LLHAFEGYNVCIFAYGQTGAGKSYTMMGrqEPGQQGIVPQLCEDLFSRVNvNQSAQLSYSVEVSYMEIYCERVRDLLNPk 161
Cdd:smart00129   72 VDSVLEGYNATIFAYGQTGSGKTYTMIG--TPDSPGIIPRALKDLFEKID-KREEGWQFSVKVSYLEIYNEKIRDLLNP- 147
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   162 SRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHDqlTGLDSEKV 241
Cdd:smart00129  148 SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN--SSSGSGKA 225
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   242 SKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADLQskkrKSDFIPYRDSVLTWLLKENLGGNSRTAM 321
Cdd:smart00129  226 SKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTLM 301
                           330       340       350
                    ....*....|....*....|....*....|....
gi 1907080140   322 IAALSPADINYEETLSTLRYADRTKQIRCNAVIN 355
Cdd:smart00129  302 IANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-348 3.13e-152

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 456.65  E-value: 3.13e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   11 RVRPFNARETSQDAKCVVSM--QGNTTSIINPKQSKDAPKSFTFDYSYWSHtsvedpqfASQQQVYRDIGEEMLLHAFEG 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVesVDSETVESSHLTNKNRTKTFTFDKVFDPE--------ATQEDVYEETAKPLVESVLEG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   89 YNVCIFAYGQTGAGKSYTMMGRQEpgQQGIVPQLCEDLFSRVNvNQSAQLSYSVEVSYMEIYCERVRDLLNP--KSRGSL 166
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDE--QPGIIPRALEDLFDRIQ-KTKERSEFSVKVSYLEIYNEKIRDLLSPsnKNKRKL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  167 RVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHDQlTGLDSEKVSKISL 246
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRST-GGEESVKTGKLNL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  247 VDLAGSERADSSG-ARGMRLKEGANINKSLTTLGKVISALADlqskkRKSDFIPYRDSVLTWLLKENLGGNSRTAMIAAL 325
Cdd:pfam00225  229 VDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANI 303
                          330       340
                   ....*....|....*....|...
gi 1907080140  326 SPADINYEETLSTLRYADRTKQI 348
Cdd:pfam00225  304 SPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
5-346 7.80e-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: 455.56  E-value: 7.80e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    5 SVKVAVRVRPFNAREtSQDAKCVVSMQG-NTTSIINPKQSKDAPKSFTFDYSYWSHtsvedpqfASQQQVYRDIGEEMLL 83
Cdd:cd00106      1 NVRVAVRVRPLNGRE-ARSAKSVISVDGgKSVVLDPPKNRVAPPKTFAFDAVFDST--------STQEEVYEGTAKPLVD 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   84 HAFEGYNVCIFAYGQTGAGKSYTMMGRQePGQQGIVPQLCEDLFSRVNVNQSAQLSYSVEVSYMEIYCERVRDLLNPKSR 163
Cdd:cd00106     72 SALEGYNGTIFAYGQTGSGKTYTMLGPD-PEQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLLSPVPK 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  164 GSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHDQltGLDSEKVSK 243
Cdd:cd00106    151 KPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREK--SGESVTSSK 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  244 ISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADlqskkRKSDFIPYRDSVLTWLLKENLGGNSRTAMIA 323
Cdd:cd00106    229 LNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----GQNKHIPYRDSKLTRLLQDSLGGNSKTIMIA 303
                          330       340
                   ....*....|....*....|...
gi 1907080140  324 ALSPADINYEETLSTLRYADRTK 346
Cdd:cd00106    304 CISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
5-348 1.67e-119

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


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 371.41  E-value: 1.67e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    5 SVKVAVRVRPFNARETSQDAKCVVSM--QGNTTSIINPKQ-SKDAPKSFTFDYSYwshtsvedPQFASQQQVYRDIGEEM 81
Cdd:cd01371      2 NVKVVVRCRPLNGKEKAAGALQIVDVdeKRGQVSVRNPKAtANEPPKTFTFDAVF--------DPNSKQLDVYDETARPL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   82 LLHAFEGYNVCIFAYGQTGAGKSYTMMG-RQEPGQQGIVPQLCEDLFSRVNVNQSAQlSYSVEVSYMEIYCERVRDLLNP 160
Cdd:cd01371     74 VDSVLEGYNGTIFAYGQTGTGKTYTMEGkREDPELRGIIPNSFAHIFGHIARSQNNQ-QFLVRVSYLEIYNEEIRDLLGK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  161 KSRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFtQRSHDQLTGLDSEK 240
Cdd:cd01371    153 DQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI-ECSEKGEDGENHIR 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  241 VSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADlqskkRKSDFIPYRDSVLTWLLKENLGGNSRTA 320
Cdd:cd01371    232 VGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----GKSTHIPYRDSKLTRLLQDSLGGNSKTV 306
                          330       340
                   ....*....|....*....|....*...
gi 1907080140  321 MIAALSPADINYEETLSTLRYADRTKQI 348
Cdd:cd01371    307 MCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
5-349 1.24e-109

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: 345.47  E-value: 1.24e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    5 SVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIInpkqsKDAPKSFTFDYsywshtsVEDPQfASQQQVYRDIGEEMLLH 84
Cdd:cd01372      2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT-----VGTDKSFTFDY-------VFDPS-TEQEEVYNTCVAPLVDG 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   85 AFEGYNVCIFAYGQTGAGKSYTMMG----RQEPGQQGIVPQLCEDLFSRVNVNQSaQLSYSVEVSYMEIYCERVRDLLNP 160
Cdd:cd01372     69 LFEGYNATVLAYGQTGSGKTYTMGTaytaEEDEEQVGIIPRAIQHIFKKIEKKKD-TFEFQLKVSFLEIYNEEIRDLLDP 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  161 --KSRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHDQLTGLDS 238
Cdd:cd01372    148 etDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  239 EK------VSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADlqsKKRKSDFIPYRDSVLTWLLKEN 312
Cdd:cd01372    228 ADdknstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGD---ESKKGAHVPYRDSKLTRLLQDS 304
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1907080140  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 2.55e-109

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: 343.93  E-value: 2.55e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    5 SVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIInpkQSKDAPKSFTFDYsywshtsVEDPQfASQQQVYRDIGEEMLLH 84
Cdd:cd01369      3 NIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVI---ATSETGKTFSFDR-------VFDPN-TTQEDVYNFAAKPIVDD 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   85 AFEGYNVCIFAYGQTGAGKSYTMMG-RQEPGQQGIVPQLCEDLFSRVNvNQSAQLSYSVEVSYMEIYCERVRDLLNPkSR 163
Cdd:cd01369     72 VLNGYNGTIFAYGQTSSGKTYTMEGkLGDPESMGIIPRIVQDIFETIY-SMDENLEFHVKVSYFEIYMEKIRDLLDV-SK 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  164 GSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRshDQLTGldSEKVSK 243
Cdd:cd01369    150 TNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE--NVETE--KKKSGK 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  244 ISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADlqskkRKSDFIPYRDSVLTWLLKENLGGNSRTAMIA 323
Cdd:cd01369    226 LYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----GKKTHIPYRDSKLTRILQDSLGGNSRTTLII 300
                          330       340
                   ....*....|....*....|....*
gi 1907080140  324 ALSPADINYEETLSTLRYADRTKQI 348
Cdd:cd01369    301 CCSPSSYNESETLSTLRFGQRAKTI 325
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
11-350 1.09e-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: 1.09e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   11 RVRPFNARETSQDAKCVVSMQGNTTSIINPKQSkDAPKSFTFDYsywshtsVEDPQfASQQQVYRDIgeEMLLH-AFEGY 89
Cdd:cd01366      9 RVRPLLPSEENEDTSHITFPDEDGQTIELTSIG-AKQKEFSFDK-------VFDPE-ASQEDVFEEV--SPLVQsALDGY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   90 NVCIFAYGQTGAGKSYTMMGRQEpgQQGIVPQLCEDLFSRVNVNQSAQLSYSVEVSYMEIYCERVRDLLNPKSRGSLR-- 167
Cdd:cd01366     78 NVCIFAYGQTGSGKTYTMEGPPE--SPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLLAPGNAPQKKle 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  168 VREHPILGP-YVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFtqRSHDQLTGLDSekVSKISL 246
Cdd:cd01366    156 IRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--SGRNLQTGEIS--VGKLNL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  247 VDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALAdlqskkRKSDFIPYRDSVLTWLLKENLGGNSRTAMIAALS 326
Cdd:cd01366    232 VDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNIS 305
                          330       340
                   ....*....|....*....|....
gi 1907080140  327 PADINYEETLSTLRYADRTKQIRC 350
Cdd:cd01366    306 PAESNLNETLNSLRFASKVNSCEL 329
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
5-348 1.35e-104

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: 332.39  E-value: 1.35e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    5 SVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQSKDA-----------------PKSFTFDYsywshtsVEDPQf 67
Cdd:cd01370      1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGffhggsnnrdrrkrrnkELKYVFDR-------VFDET- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   68 ASQQQVYRDIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMG-RQEPGqqgIVPQLCEDLFSRVNvNQSAQLSYSVEVSY 146
Cdd:cd01370     73 STQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGtPQEPG---LMVLTMKELFKRIE-SLKDEKEFEVSMSY 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  147 MEIYCERVRDLLNPKSrGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFT 226
Cdd:cd01370    149 LEIYNETIRDLLNPSS-GPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVR 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  227 QRshDQLTGLDSE-KVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADlqsKKRKSDFIPYRDSVL 305
Cdd:cd01370    228 QQ--DKTASINQQvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD---PGKKNKHIPYRDSKL 302
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1907080140  306 TWLLKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQI 348
Cdd:cd01370    303 TRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
5-348 3.30e-102

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: 325.06  E-value: 3.30e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    5 SVKVAVRVRPFNARETSQDAKCVVSMQGNTTSiinpkQSKDAPKSFTFDYSYWSHTSVEdpqfasqqQVYRDIGEEMLLH 84
Cdd:cd01374      1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIY-----LVEPPSTSFTFDHVFGGDSTNR--------EVYELIAKPVVKS 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   85 AFEGYNVCIFAYGQTGAGKSYTMMG-RQEPGqqgIVPQLCEDLFSRVNvnQSAQLSYSVEVSYMEIYCERVRDLLNPKSR 163
Cdd:cd01374     68 ALEGYNGTIFAYGQTSSGKTFTMSGdEDEPG---IIPLAIRDIFSKIQ--DTPDREFLLRVSYLEIYNEKINDLLSPTSQ 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  164 gSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHDQLTGlDSEKVSK 243
Cdd:cd01374    143 -NLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEE-GTVRVST 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  244 ISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALadlqSKKRKSDFIPYRDSVLTWLLKENLGGNSRTAMIA 323
Cdd:cd01374    221 LNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKL----SEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIIC 296
                          330       340
                   ....*....|....*....|....*
gi 1907080140  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 1.37e-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: 316.37  E-value: 1.37e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    6 VKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQskdaPKSFTFDYSYWSHTSvedpqfasQQQVYRDIGEEMLLHA 85
Cdd:cd01373      3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKP----PKTFTFDHVADSNTN--------QESVFQSVGKPIVESC 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   86 FEGYNVCIFAYGQTGAGKSYTMMGRQEP------GQQGIVPQLCEDLFSRVN---VNQSAQLSYSVEVSYMEIYCERVRD 156
Cdd:cd01373     71 LSGYNGTIFAYGQTGSGKTYTMWGPSESdnesphGLRGVIPRIFEYLFSLIQrekEKAGEGKSFLCKCSFLEIYNEQIYD 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  157 LLNPKSRGsLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTivFTQRSHDQLTGL 236
Cdd:cd01373    151 LLDPASRN-LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFT--CTIESWEKKACF 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  237 DSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADLQSKKrkSDFIPYRDSVLTWLLKENLGGN 316
Cdd:cd01373    228 VNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGK--QRHVCYRDSKLTFLLRDSLGGN 305
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1907080140  317 SRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAVINED 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 3.87e-94

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: 304.25  E-value: 3.87e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    3 GASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSII---NPKQSKDAPKSFTFDYSYwshtsveDPQfASQQQVYRDIGE 79
Cdd:cd01364      1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSvrtGGLADKSSTKTYTFDMVF-------GPE-AKQIDVYRSVVC 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   80 EMLLHAFEGYNVCIFAYGQTGAGKSYTMMG---------RQEPGQQGIVPQLCEDLFSRVNVNQSaqlSYSVEVSYMEIY 150
Cdd:cd01364     73 PILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrspneeytWELDPLAGIIPRTLHQLFEKLEDNGT---EYSVKVSYLEIY 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  151 CERVRDLLNPKSRGSLRVREHPIL----GPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFt 226
Cdd:cd01364    150 NEELFDLLSPSSDVSERLRMFDDPrnkrGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITI- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  227 qrsHDQLTGLDSE---KVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADlqskkrKSDFIPYRDS 303
Cdd:cd01364    229 ---HIKETTIDGEelvKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------RAPHVPYRES 299
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907080140  304 VLTWLLKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAVINED 357
Cdd:cd01364    300 KLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
68-355 3.69e-81

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 276.23  E-value: 3.69e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   68 ASQQQVYRDIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGrqEPGQQGIVPQLCEDLFSRvNVNQSAQLSYSVEVSYM 147
Cdd:COG5059     68 ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG--TEEEPGIIPLSLKELFSK-LEDLSMTKDFAVSISYL 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  148 EIYCERVRDLLNPKSRgSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQ 227
Cdd:COG5059    145 EIYNEKIYDLLSPNEE-SLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELAS 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  228 RshDQLTGLDSEkvSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALadlqSKKRKSDFIPYRDSVLTW 307
Cdd:COG5059    224 K--NKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINAL----GDKKKSGHIPYRESKLTR 295
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1907080140  308 LLKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAVIN 355
Cdd:COG5059    296 LLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
6-346 1.79e-77

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: 257.99  E-value: 1.79e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    6 VKVAVRVRPFNARETSQDAKCVVSMQGNTTSIIN-PKQSKDAPK-----SFTFDYSYwshtsVEDpqfASQQQVYRDIGE 79
Cdd:cd01367      2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHePKLKVDLTKyienhTFRFDYVF-----DES---SSNETVYRSTVK 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   80 EMLLHAFEGYNVCIFAYGQTGAGKSYTMMGR--QEPGQQGIVPQLCEDLFSRVNVNQSAqLSYSVEVSYMEIYCERVRDL 157
Cdd:cd01367     74 PLVPHIFEGGKATCFAYGQTGSGKTYTMGGDfsGQEESKGIYALAARDVFRLLNKLPYK-DNLGVTVSFFEIYGGKVFDL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  158 LNPKSRgsLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHDQLTGld 237
Cdd:cd01367    153 LNRKKR--VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNKLHG-- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  238 sekvsKISLVDLAGSER-ADSSGARGMRLKEGANINKSLTTLGKVISALAdlQSKKRksdfIPYRDSVLTWLLKENL-GG 315
Cdd:cd01367    229 -----KLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG--QNKAH----IPFRGSKLTQVLKDSFiGE 297
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1907080140  316 NSRTAMIAALSPADINYEETLSTLRYADRTK 346
Cdd:cd01367    298 NSKTCMIATISPGASSCEHTLNTLRYADRVK 328
Kinesin_assoc pfam16183
Kinesin-associated;
352-522 6.28e-76

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 247.83  E-value: 6.28e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  352 AVINEDPNARLIRELQEEVARLRDLLMAQGLSA---SALGGLKVEEGSPGGVLPPASSPPAPASPSSPPPHNGELEPSFS 428
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLGDiidTIAHPTKKRANTPAANASAATAAMAGASPSPSLSALSSRAASVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  429 PSAEPQI---GPEEAMERLQETEKIIAELNETWEEKLRKTEALRMEREALLAEMGVAVREDGGTVGVFSPKKTPHLVNLN 505
Cdd:pfam16183   81 SLHERIMftpGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLN 160
                          170
                   ....*....|....*..
gi 1907080140  506 EDPLMSECLLYHIKDGV 522
Cdd:pfam16183  161 EDPLMSECLLYYIKDGI 177
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
6-346 9.12e-76

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: 253.86  E-value: 9.12e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    6 VKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQSKDAPKSFT---FDYSYWSHTSVEDPQfASQQQVYRDIGEEML 82
Cdd:cd01368      3 VKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERnggQKETKFSFSKVFGPN-TTQKEFFQGTALPLV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   83 LHAFEGYNVCIFAYGQTGAGKSYTMMGrqEPGQQGIVPQLCEDLFSRVNvnqsaqlSYSVEVSYMEIYCERVRDLLNP-- 160
Cdd:cd01368     82 QDLLHGKNGLLFTYGVTNSGKTYTMQG--SPGDGGILPRSLDVIFNSIG-------GYSVFVSYIEIYNEYIYDLLEPsp 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  161 ----KSRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQrSHDQLTGL 236
Cdd:cd01368    153 ssptKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQ-APGDSDGD 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  237 -----DSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADLQsKKRKSDFIPYRDSVLTWLLKE 311
Cdd:cd01368    232 vdqdkDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQ-LQGTNKMVPFRDSKLTHLFQN 310
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1907080140  312 NLGGNSRTAMIAALSPADINYEETLSTLRYADRTK 346
Cdd:cd01368    311 YFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
PLN03188 PLN03188
kinesin-12 family protein; Provisional
1-375 7.30e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 268.34  E-value: 7.30e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    1 MAGASVKVAVRVRPFNAREtsQDAKCVVSMQGNTTSIINpkqskdapKSFTFDysywshtSVEDPQfASQQQVYRDIGEE 80
Cdd:PLN03188    95 VSDSGVKVIVRMKPLNKGE--EGEMIVQKMSNDSLTING--------QTFTFD-------SIADPE-STQEDIFQLVGAP 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   81 MLLHAFEGYNVCIFAYGQTGAGKSYTMMG--------RQEPGQQGIVPQLCEDLFSRVNVNQ----SAQLSYSVEVSYME 148
Cdd:PLN03188   157 LVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglleeHLSGDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRCSFLE 236
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  149 IYCERVRDLLNPKSRgSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQR 228
Cdd:PLN03188   237 IYNEQITDLLDPSQK-NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESR 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  229 SHDQLTGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADLqSKKRKSDFIPYRDSVLTWL 308
Cdd:PLN03188   316 CKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEI-SQTGKQRHIPYRDSRLTFL 394
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907080140  309 LKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAVINE----DPN--ARLIRELQEEVARLRD 375
Cdd:PLN03188   395 LQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVKA 467
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
498-599 6.94e-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: 230.91  E-value: 6.94e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  498 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVDIKLTGQFIREQHCLFRSIPQPDGEVMVTLEPCEGAETYVNGKLVTE 577
Cdd:cd22728      1 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVDIKLSGQFIREQHCLFRSIPNPSGEVVVTLEPCEGAETYVNGKQVTE 80
                           90       100
                   ....*....|....*....|..
gi 1907080140  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 8.25e-71

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: 238.94  E-value: 8.25e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    6 VKVAVRVRPFNARETSQDAK-CVVSMQGNTTSIINPKQSKDaPKSFTFDYSYWSHtsvedpqfASQQQVYRDIGEEMLLH 84
Cdd:cd01376      2 VRVAVRVRPFVDGTAGASDPsCVSGIDSCSVELADPRNHGE-TLKYQFDAFYGEE--------STQEDIYAREVQPIVPH 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   85 AFEGYNVCIFAYGQTGAGKSYTMMGrqEPGQQGIVPQLCEDLFSrvnVNQSAQLSYSVEVSYMEIYCERVRDLLNPKSrG 164
Cdd:cd01376     73 LLEGQNATVFAYGSTGAGKTFTMLG--SPEQPGLMPLTVMDLLQ---MTRKEAWALSFTMSYLEIYQEKILDLLEPAS-K 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  165 SLRVRE---HPILgpyVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRshdQLTGLDSEKV 241
Cdd:cd01376    147 ELVIREdkdGNIL---IPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQR---ERLAPFRQRT 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  242 SKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALadLQSKKRksdfIPYRDSVLTWLLKENLGGNSRTAM 321
Cdd:cd01376    221 GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL--NKNLPR----IPYRDSKLTRLLQDSLGGGSRCIM 294
                          330       340
                   ....*....|....*....|....*
gi 1907080140  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 4.86e-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: 226.31  E-value: 4.86e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    5 SVKVAVRVRPfnareTSQDAKCVVSM--QGNTTSIINPKQSKDAP-----KSFTFDYSYWSHTsvedpqfASQQQVYRDI 77
Cdd:cd01375      1 KVQAFVRVRP-----TDDFAHEMIKYgeDGKSISIHLKKDLRRGVvnnqqEDWSFKFDGVLHN-------ASQELVYETV 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   78 GEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEP-GQQGIVPQLCEDLFSRVNVNQSAqlSYSVEVSYMEIYCERVRD 156
Cdd:cd01375     69 AKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENyKHRGIIPRALQQVFRMIEERPTK--AYTVHVSYLEIYNEQLYD 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  157 LLNPK-----SRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRSHD 231
Cdd:cd01375    147 LLSTLpyvgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRT 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  232 qltgLDSEKV--SKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADlqskkRKSDFIPYRDSVLTWLL 309
Cdd:cd01375    227 ----LSSEKYitSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD-----KDRTHVPFRQSKLTHVL 297
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1907080140  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 1.47e-62

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: 207.86  E-value: 1.47e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  498 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLTGQFIREQHCLFRSIPQPDGEVMVTLEPCEGAETYVNGK 573
Cdd:cd22726      1 TPHLVNLNEDPLMSECLLYYIKDGITRVGREDAerrqDIVLSGHFIKEEHCIFRSDTRSGGEAVVTLEPCEGADTYVNGK 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907080140  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 8.60e-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: 199.88  E-value: 8.60e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  497 KTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLTGQFIREQHCLFRSIPQPDGEVMVTLEPCEGAETYVNG 572
Cdd:cd22727      1 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAerrqDIVLSGAHIKEEHCIFRSERNNNGEVIVTLEPCERSETYVNG 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1907080140  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 2.91e-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: 195.14  E-value: 2.91e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  498 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVD----VDIKLTGQFIREQHCLFRSIpqpDGEVmvTLEPCEGAETYVNGK 573
Cdd:cd22705      1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADadvpQDIQLSGTHILEEHCTFENE---DGVV--TLEPCEGALTYVNGK 75
                           90       100
                   ....*....|....*....|....*.
gi 1907080140  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 9.46e-36

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: 9.46e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  497 KTPHLVNLNEDPLMSECLLYHIKDGVTRVGQ----VDVDIKLTGQFIREQHCLFRSIpqpdgEVMVTLEPCEGAETYVNG 572
Cdd:cd22707      6 KLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRskasSSHDIQLSGALIADDHCTIENN-----GGKVTIIPVGDAETYVNG 80
                           90       100
                   ....*....|....*....|....*...
gi 1907080140  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 8.21e-33

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: 125.15  E-value: 8.21e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    8 VAVRVRPFNARETSQDAKCVVSMQGnttsiinpkqskdapksftfdysywshtsveDPQFASQQQVYRDIGeEMLLHAFE 87
Cdd:cd01363      1 VLVRVNPFKELPIYRDSKIIVFYRG-------------------------------FRRSESQPHVFAIAD-PAYQSMLD 48
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   88 GYNV-CIFAYGQTGAGKSYTMMgrqepgqqGIVPQLCEDLFSRVNVNQSAQLSYsvevsymeiycervrdllnpksrgsl 166
Cdd:cd01363     49 GYNNqSIFAYGESGAGKTETMK--------GVIPYLASVAFNGINKGETEGWVY-------------------------- 94
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  167 rvrehpilgpyvqdLSKLAVTSYADIADLMDCGNKARTvAATNMNETSSRSHAVFTIVftqrshdqltgldsekvskisl 246
Cdd:cd01363     95 --------------LTEITVTLEDQILQANPILEAFGN-AKTTRNENSSRFGKFIEIL---------------------- 137
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907080140  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 3.21e-31

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: 118.09  E-value: 3.21e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  499 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVD----VDIKLTGQFIREQHCLFRSIpqpDGEvmVTLEPC-EGAETYVNGK 573
Cdd:cd22709      1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADaepePDIVLSGLSIQKQHAVITNT---DGK--VTIEPVsPGAKVIVNGV 75
                           90       100
                   ....*....|....*....|....*..
gi 1907080140  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 1.95e-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: 116.22  E-value: 1.95e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  497 KTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLTGQFIREQHCLFRSIpqpDGevMVTLEPCEGAETYVNG 572
Cdd:cd22708      7 ELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDApqeqDIVLDGEDIEAEHCIIENV---GG--VVTLHPLPGALCAVNG 81
                           90       100
                   ....*....|....*....|....*...
gi 1907080140  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 7.80e-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: 109.09  E-value: 7.80e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  491 GVFSPKKTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLTGQFIREQHCLfrsIPQPDGevMVTLEPCEGA 566
Cdd:cd22731      1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSeqeqDIVLQGPWIERDHCM---IHNECG--VVTLRPAQGA 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907080140  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 2.03e-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: 104.30  E-value: 2.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  501 LVNLNEDPLMSECLLYHIKDgVTRVGQVDV----DIKLTGQFIREQHCLfrsIPQPDGEVMVTlePCEGAETYVNGKLVT 576
Cdd:cd22706      4 LVNLNADPSLNELLVYYLKE-HTLIGRSDAptqqDIQLSGLGIQPEHCI---ITIENEDVYLT--PLEGARTCVNGSIVT 77
                           90       100
                   ....*....|....*....|....
gi 1907080140  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 4.32e-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: 89.61  E-value: 4.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  491 GVFSPKKTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLTGQFIREQHCLFRSIPQpdgevMVTLEPCEGA 566
Cdd:cd22732      1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDAtteqDIVLHGLDLESEHCIFENLNG-----TVTLIPLNGA 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1907080140  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 1.01e-19

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: 85.33  E-value: 1.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  501 LVNLNEDPLMSECLLYHIKDGvTRVG-QVDVDIKLTGQFIREQHCLFRSipQPDGEVmvTLEPCEGAETYVNGKLVTEPL 579
Cdd:cd22729      4 LVNLNADPALNELLVYYLKDH-TRVGaDTSQDIQLFGIGIQPEHCVIDI--AADGDV--TLTPKENARTCVNGTLVCSVT 78
                           90       100
                   ....*....|....*....|....*...
gi 1907080140  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 1.13e-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: 84.97  E-value: 1.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  501 LVNLNEDPLMSECLLYHIKDGvTRVGQVDV-DIKLTGQFIREQHCLFRSipQPDGEVMVTlePCEGAETYVNGKLVTEPL 579
Cdd:cd22730      4 LVNLNADPALNELLVYYLKEH-TLIGSADSqDIQLCGMGILPEHCIIDI--TPEGQVMLT--PQKNTRTFVNGSAVTSPI 78
                           90       100
                   ....*....|....*....|.
gi 1907080140  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 7.08e-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: 71.97  E-value: 7.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  499 PHLVNLNEDPLMSECLLYHIKDGVTRVGQVDVD-IKLTGQFIREQHCLFRSIpqpDGEVmvTLEPCEGAETyVNGKLVTE 577
Cdd:cd22713     17 PHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASDiISLQGPGVEPEHCYIENI---NGTV--TLYPCGNLCS-VDGLPITE 90
                           90       100
                   ....*....|....*....|....*.
gi 1907080140  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 9.03e-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: 68.50  E-value: 9.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  499 PHLVNLNEDPLMSECL-LYHIKDGVTRVG------QVDVDIKLTGQFIREQHCLFRSIpqpDGEVMVTlePCEG-AETYV 570
Cdd:cd22711      2 PYLLELSPDGSDRDKPrRHRLQPNVTEVGserspaNSGQFIQLFGPDILPRHCVITHM---EGVVTVT--PASQdAETYV 76
                           90       100       110
                   ....*....|....*....|....*....|
gi 1907080140  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 1.16e-12

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 66.47  E-value: 1.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140    5 SVKVAVRVRPFNAREtsqdakCVVSMQGNTTSIINPKQSKdapKSFTFDysywshtSVEDPQfASQQQVYRDIgeEMLLH 84
Cdd:pfam16796   21 NIRVFARVRPELLSE------AQIDYPDETSSDGKIGSKN---KSFSFD-------RVFPPE-SEQEDVFQEI--SQLVQ 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907080140   85 -AFEGYNVCIFAYGQTGAGKSYTMmgrqepgqqgiVPQLCEDLFSRVNvNQSAQLSYSVEVSYMEIYCERVRDLL 158
Cdd:pfam16796   82 sCLDGYNVCIFAYGQTGSGSNDGM-----------IPRAREQIFRFIS-SLKKGWKYTIELQFVEIYNESSQDLL 144
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
498-600 1.35e-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: 59.62  E-value: 1.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  498 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVD-----VDIKLTGQFIREQHCLFRSIPQPDGEV----------MVTLEP 562
Cdd:cd22712      3 YPYLLTLRGFSPKQDLLVYPLLEQVILVGSRTegarkVDISLRAPDILPQHCWIRRKPEPLSDDedsdkesadyRVVLSP 82
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907080140  563 CEGAETYVNGKLVTEPLVLKSGNRIVMGKNHVFRFNHP 600
Cdd:cd22712     83 LRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
500-597 2.76e-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: 54.97  E-value: 2.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  500 HLVNLNEDPLMSEcllYHIKDGVTRVG-QVDVDIKLTGQFIREQHCLFRSIpqpDGEVMVT-LEPCEGaeTYVNGKLVTE 577
Cdd:cd00060      1 RLIVLDGDGGGRE---FPLTKGVVTIGrSPDCDIVLDDPSVSRRHARIEVD---GGGVYLEdLGSTNG--TFVNGKRITP 72
                           90       100
                   ....*....|....*....|
gi 1907080140  578 PLVLKSGNRIVMGkNHVFRF 597
Cdd:cd00060     73 PVPLQDGDVIRLG-DTTFRF 91
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
523-589 6.13e-06

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 44.87  E-value: 6.13e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  523 TRVGQ-VDVDIKLTGQFIREQHCLFRSipqpDGEVMVTLEPC-EGAETYVNGKLVT-EPLVLKSGNRIVM 589
Cdd:pfam00498    1 VTIGRsPDCDIVLDDPSVSRRHAEIRY----DGGGRFYLEDLgSTNGTFVNGQRLGpEPVRLKDGDVIRL 66
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
516-597 1.26e-05

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 44.95  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  516 YHIKDGVTRVG-QVDVDIKLTGQFIREQHCLFRsiPQPDGevmVTLEPCEGA-ETYVNGKLVTEPLVLKSGNRIVMGKnH 593
Cdd:COG1716     16 FPLDGGPLTIGrAPDNDIVLDDPTVSRRHARIR--RDGGG---WVLEDLGSTnGTFVNGQRVTEPAPLRDGDVIRLGK-T 89

                   ....
gi 1907080140  594 VFRF 597
Cdd:COG1716     90 ELRF 93
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
93-288 4.35e-05

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 47.43  E-value: 4.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140   93 IFAYGQTGAGKSYTMMGRQEpgqqGIVPQLCEDLFSRVNVNQSAQLSYSVEVSYMEIYCERVRDLLNPKSRGSLRVREHp 172
Cdd:COG5059    385 IFAYMQSLKKETETLKSRID----LIMKSIISGTFERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHK- 459
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  173 ilgpyvqdLSKL---AVTSYADIAD-----LMDCGNKA-RTVAATNMNETSSRSHAVFTivftqrsHDQLTGLDSEKVSK 243
Cdd:COG5059    460 --------LNKLrhdLSSLLSSIPEetsdrVESEKASKlRSSASTKLNLRSSRSHSKFR-------DHLNGSNSSTKELS 524
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1907080140  244 ISLVDLAGSERaDSSGARGMRLKEGANINKSLTTLGKVISALADL 288
Cdd:COG5059    525 LNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHALGSK 568
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
497-600 7.54e-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: 43.25  E-value: 7.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907080140  497 KTPHLVNLNEDPLMSECLLYHIKDGVTRVGQ----VDVDIKLTGQFIREQHCLFRSIPQPDG--EVMVTLEPCEGAETYV 570
Cdd:cd22733      4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQetpsSKPNISLSAPDILPLHCTIRRVRLPKHrsEEKLVLEPIPGAHVSV 83
                           90       100       110
                   ....*....|....*....|....*....|
gi 1907080140  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 2.39e-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: 41.04  E-value: 2.39e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907080140  531 DIKLTGQFIREQHCLFRsipqPDGEVMVTLEP-CEGAETYVNGKLVTEPLVLKSGNRIVMGkNHVFRF 597
Cdd:cd22673     32 DIRIQLPGVSREHCRIE----VDENGKAYLENlSTTNPTLVNGKAIEKSAELKDGDVITIG-GRSFRF 94
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
529-575 1.17e-03

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 37.93  E-value: 1.17e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1907080140   529 DVDIKLTGQFIREQHCLFRSipqpDGEVMVTLEPC-EGAETYVNGKLV 575
Cdd:smart00240    9 DCDIQLDGPSISRRHAVIVY----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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