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Conserved domains on  [gi|568930680|ref|XP_006538659|]
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kinesin-like protein KIF1B isoform X14 [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 ...
4-361 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: 651.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    4 ASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKN-------PKEAPKSFSFDYSYWSHTsPEDPCFASQNRVYND 76
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkaTREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   77 IGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEesQAGIIPQLCEELFEKINDNCNEEMSYSVEVSYMEIYCERVRD 156
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  157 LLNPK---NKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPE 233
Cdd:cd01365   158 LLNPKpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  234 TNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskSKKKKKTDFIPYRDSVLTW 313
Cdd:cd01365   238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSS----GKSKKKSSFIPYRDSVLTW 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 568930680  314 LLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVIN 361
Cdd:cd01365   314 LLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
Kinesin_assoc pfam16183
Kinesin-associated;
358-555 2.95e-91

Kinesin-associated;


:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 290.59  E-value: 2.95e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   358 AVINEDPNAKLVRELKEEVTRLKDLLRAQGLGdiididpliddysgsggkylkDFQNNKHRYLLASENQRPGNFSTASMG 437
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLG---------------------DIIDTIAHPTKKRANTPAANASAATAA 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   438 SLTSSPSSCSLNSQVGLTSVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIR 517
Cdd:pfam16183   60 MAGASPSPSLSALSSRAASVSSLHERIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIR 139
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568930680   518 EDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGI 555
Cdd:pfam16183  140 EDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGI 177
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
530-639 2.46e-78

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: 252.26  E-value: 2.46e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  530 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCLFRSERSNTGEVIVTLEPCERSETYVNG 609
Cdd:cd22727     1 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNNNGEVIVTLEPCERSETYVNG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 568930680  610 KRVAHPVQLRSGNRIIMGKNHVFRFNHPEQ 639
Cdd:cd22727    81 KRVVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
4-361 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: 651.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    4 ASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKN-------PKEAPKSFSFDYSYWSHTsPEDPCFASQNRVYND 76
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkaTREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   77 IGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEesQAGIIPQLCEELFEKINDNCNEEMSYSVEVSYMEIYCERVRD 156
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  157 LLNPK---NKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPE 233
Cdd:cd01365   158 LLNPKpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  234 TNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskSKKKKKTDFIPYRDSVLTW 313
Cdd:cd01365   238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSS----GKSKKKSSFIPYRDSVLTW 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 568930680  314 LLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVIN 361
Cdd:cd01365   314 LLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
5-361 1.42e-153

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: 462.81  E-value: 1.42e-153
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680      5 SVKVAVRVRPFNSRETSKESKCIIQMQGNS--TSIINPKNPKEAPKSFSFDYSYwshtspeDPcFASQNRVYNDIGKEML 82
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVgkTLTVRSPKNRQGEKKFTFDKVF-------DA-TASQEDVFEETAAPLV 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680     83 LHAFEGYNVCIFAYGQTGAGKSYTMMGkqEESQAGIIPQLCEELFEKInDNCNEEMSYSVEVSYMEIYCERVRDLLNPkN 162
Cdd:smart00129   73 DSVLEGYNATIFAYGQTGSGKTYTMIG--TPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP-S 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    163 KGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETnlSTEKVS 242
Cdd:smart00129  149 SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS--GSGKAS 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    243 KISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkkTDFIPYRDSVLTWLLRENLGGN 322
Cdd:smart00129  227 KLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK----------SRHIPYRDSKLTRLLQDSLGGN 296
                           330       340       350
                    ....*....|....*....|....*....|....*....
gi 568930680    323 SRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVIN 361
Cdd:smart00129  297 SKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-354 9.02e-150

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 452.41  E-value: 9.02e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    11 RVRPFNSRETSKESKCIIQM--QGNSTSIINPKNPKEAPKSFSFDYSYWSHtspedpcfASQNRVYNDIGKEMLLHAFEG 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVesVDSETVESSHLTNKNRTKTFTFDKVFDPE--------ATQEDVYEETAKPLVESVLEG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    89 YNVCIFAYGQTGAGKSYTMMGKQEesQAGIIPQLCEELFEKINDnCNEEMSYSVEVSYMEIYCERVRDLLNP--KNKGNL 166
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDE--QPGIIPRALEDLFDRIQK-TKERSEFSVKVSYLEIYNEKIRDLLSPsnKNKRKL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   167 RVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETNLSTeKVSKISL 246
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKLNL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   247 VDLAGSERADSTG-AKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkktDFIPYRDSVLTWLLRENLGGNSRT 325
Cdd:pfam00225  229 VDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS-----------KHIPYRDSKLTRLLQDSLGGNSKT 297
                          330       340
                   ....*....|....*....|....*....
gi 568930680   326 AMVAALSPADINYDETLSTLRYADRAKQI 354
Cdd:pfam00225  298 LMIANISPSSSNYEETLSTLRFASRAKNI 326
Kinesin_assoc pfam16183
Kinesin-associated;
358-555 2.95e-91

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 290.59  E-value: 2.95e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   358 AVINEDPNAKLVRELKEEVTRLKDLLRAQGLGdiididpliddysgsggkylkDFQNNKHRYLLASENQRPGNFSTASMG 437
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLG---------------------DIIDTIAHPTKKRANTPAANASAATAA 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   438 SLTSSPSSCSLNSQVGLTSVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIR 517
Cdd:pfam16183   60 MAGASPSPSLSALSSRAASVSSLHERIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIR 139
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568930680   518 EDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGI 555
Cdd:pfam16183  140 EDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGI 177
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
1-374 1.10e-78

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 270.46  E-value: 1.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    1 MSGASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINpknpKEAPKSFSFDYSYWSHtspedpcfASQNRVYNDIGKE 80
Cdd:COG5059    13 LSSRNEKSVSDIKSTIRIIPGELGERLINTSKKSHVSLE----KSKEGTYAFDKVFGPS--------ATQEDVYEETIKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   81 MLLHAFEGYNVCIFAYGQTGAGKSYTMMGkqEESQAGIIPQLCEELFEKInDNCNEEMSYSVEVSYMEIYCERVRDLLNP 160
Cdd:COG5059    81 LIDSLLLGYNCTVFAYGQTGSGKTYTMSG--TEEEPGIIPLSLKELFSKL-EDLSMTKDFAVSISYLEIYNEKIYDLLSP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  161 KNKGnLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETNLStek 240
Cdd:COG5059   158 NEES-LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET--- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  241 vSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkkTDFIPYRDSVLTWLLRENLG 320
Cdd:COG5059   234 -SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKK----------SGHIPYRESKLTRLLQDSLG 302
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568930680  321 GNSRTAMVAALSPADINYDETLSTLRYADRAKQIK-----CNAVINEDPNAKLVRELKE 374
Cdd:COG5059   303 GNCNTRVICTISPSSNSFEETINTLKFASRAKSIKnkiqvNSSSDSSREIEEIKFDLSE 361
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
530-639 2.46e-78

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: 252.26  E-value: 2.46e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  530 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCLFRSERSNTGEVIVTLEPCERSETYVNG 609
Cdd:cd22727     1 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNNNGEVIVTLEPCERSETYVNG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 568930680  610 KRVAHPVQLRSGNRIIMGKNHVFRFNHPEQ 639
Cdd:cd22727    81 KRVVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
PLN03188 PLN03188
kinesin-12 family protein; Provisional
1-381 3.37e-72

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 264.10  E-value: 3.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    1 MSGASVKVAVRVRPFNSREtskESKCIIQMQGNSTSIINPKnpkeapkSFSFDysywSHTSPEdpcfASQNRVYNDIGKE 80
Cdd:PLN03188   95 VSDSGVKVIVRMKPLNKGE---EGEMIVQKMSNDSLTINGQ-------TFTFD----SIADPE----STQEDIFQLVGAP 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   81 MLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQ----EES----QAGIIPQLCEELFEKIND----NCNEEMSYSVEVSYME 148
Cdd:PLN03188  157 LVENCLAGFNSSVFAYGQTGSGKTYTMWGPAngllEEHlsgdQQGLTPRVFERLFARINEeqikHADRQLKYQCRCSFLE 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  149 IYCERVRDLLNPKNKgNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQK 228
Cdd:PLN03188  237 IYNEQITDLLDPSQK-NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESR 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  229 KQDPETNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKkkkktdfIPYRD 308
Cdd:PLN03188  316 CKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRH-------IPYRD 388
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930680  309 SVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVINE----DPN--AKLVRELKEEVTRLKD 381
Cdd:PLN03188  389 SRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVKA 467
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
556-624 1.36e-06

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 46.80  E-value: 1.36e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568930680   556 TRVGQADaerRQDIVLSGAHIKEEHCLFRSERSNTgeviVTLEPC-ERSETYVNGKRVAH-PVQLRSGNRI 624
Cdd:pfam00498    1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYDGGGR----FYLEDLgSTNGTFVNGQRLGPePVRLKDGDVI 64
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
551-634 5.29e-06

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 46.10  E-value: 5.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  551 IKDGITRVGQADaerRQDIVLSGAHIKEEHCLFRseRSNTGEVIVTLEpcERSETYVNGKRVAHPVQLRSGNRIIMGKnH 630
Cdd:COG1716    18 LDGGPLTIGRAP---DNDIVLDDPTVSRRHARIR--RDGGGWVLEDLG--STNGTFVNGQRVTEPAPLRDGDVIRLGK-T 89

                  ....
gi 568930680  631 VFRF 634
Cdd:COG1716    90 ELRF 93
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
4-361 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: 651.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    4 ASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKN-------PKEAPKSFSFDYSYWSHTsPEDPCFASQNRVYND 76
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkaTREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   77 IGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEesQAGIIPQLCEELFEKINDNCNEEMSYSVEVSYMEIYCERVRD 156
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  157 LLNPK---NKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPE 233
Cdd:cd01365   158 LLNPKpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  234 TNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskSKKKKKTDFIPYRDSVLTW 313
Cdd:cd01365   238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSS----GKSKKKSSFIPYRDSVLTW 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 568930680  314 LLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVIN 361
Cdd:cd01365   314 LLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
5-361 1.42e-153

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: 462.81  E-value: 1.42e-153
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680      5 SVKVAVRVRPFNSRETSKESKCIIQMQGNS--TSIINPKNPKEAPKSFSFDYSYwshtspeDPcFASQNRVYNDIGKEML 82
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVgkTLTVRSPKNRQGEKKFTFDKVF-------DA-TASQEDVFEETAAPLV 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680     83 LHAFEGYNVCIFAYGQTGAGKSYTMMGkqEESQAGIIPQLCEELFEKInDNCNEEMSYSVEVSYMEIYCERVRDLLNPkN 162
Cdd:smart00129   73 DSVLEGYNATIFAYGQTGSGKTYTMIG--TPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP-S 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    163 KGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETnlSTEKVS 242
Cdd:smart00129  149 SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSS--GSGKAS 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    243 KISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkkTDFIPYRDSVLTWLLRENLGGN 322
Cdd:smart00129  227 KLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK----------SRHIPYRDSKLTRLLQDSLGGN 296
                           330       340       350
                    ....*....|....*....|....*....|....*....
gi 568930680    323 SRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVIN 361
Cdd:smart00129  297 SKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
5-352 2.23e-153

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: 461.72  E-value: 2.23e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    5 SVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNPKEAPKSFSFDYSYWSHtspedpcfASQNRVYNDIGKEMLLH 84
Cdd:cd00106     1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPPKTFAFDAVFDST--------STQEEVYEGTAKPLVDS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   85 AFEGYNVCIFAYGQTGAGKSYTMMGKQEEsQAGIIPQLCEELFEKINDNCNEEMSYSVEVSYMEIYCERVRDLLNPKNKG 164
Cdd:cd00106    73 ALEGYNGTIFAYGQTGSGKTYTMLGPDPE-QRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLLSPVPKK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  165 NLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKqdPETNLSTEKVSKI 244
Cdd:cd00106   152 PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRN--REKSGESVTSSKL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  245 SLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkktDFIPYRDSVLTWLLRENLGGNSR 324
Cdd:cd00106   230 NLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN-----------KHIPYRDSKLTRLLQDSLGGNSK 298
                         330       340
                  ....*....|....*....|....*...
gi 568930680  325 TAMVAALSPADINYDETLSTLRYADRAK 352
Cdd:cd00106   299 TIMIACISPSSENFEETLSTLRFASRAK 326
Kinesin pfam00225
Kinesin motor domain;
11-354 9.02e-150

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 452.41  E-value: 9.02e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    11 RVRPFNSRETSKESKCIIQM--QGNSTSIINPKNPKEAPKSFSFDYSYWSHtspedpcfASQNRVYNDIGKEMLLHAFEG 88
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVesVDSETVESSHLTNKNRTKTFTFDKVFDPE--------ATQEDVYEETAKPLVESVLEG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    89 YNVCIFAYGQTGAGKSYTMMGKQEesQAGIIPQLCEELFEKINDnCNEEMSYSVEVSYMEIYCERVRDLLNP--KNKGNL 166
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDE--QPGIIPRALEDLFDRIQK-TKERSEFSVKVSYLEIYNEKIRDLLSPsnKNKRKL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   167 RVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETNLSTeKVSKISL 246
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKLNL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   247 VDLAGSERADSTG-AKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkktDFIPYRDSVLTWLLRENLGGNSRT 325
Cdd:pfam00225  229 VDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS-----------KHIPYRDSKLTRLLQDSLGGNSKT 297
                          330       340
                   ....*....|....*....|....*....
gi 568930680   326 AMVAALSPADINYDETLSTLRYADRAKQI 354
Cdd:pfam00225  298 LMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
5-354 1.60e-114

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: 359.85  E-value: 1.60e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    5 SVKVAVRVRPFNSRETSKESKCIIQM--QGNSTSIINPK-NPKEAPKSFSFDYSYwshtspeDPCfASQNRVYNDIGKEM 81
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVdeKRGQVSVRNPKaTANEPPKTFTFDAVF-------DPN-SKQLDVYDETARPL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   82 LLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEESQA-GIIPQLCEELFEKINDNcNEEMSYSVEVSYMEIYCERVRDLLNP 160
Cdd:cd01371    74 VDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPELrGIIPNSFAHIFGHIARS-QNNQQFLVRVSYLEIYNEEIRDLLGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  161 KNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVF--TQKKQDPETNLst 238
Cdd:cd01371   153 DQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecSEKGEDGENHI-- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  239 eKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALaeVDNctskskkkkKTDFIPYRDSVLTWLLREN 318
Cdd:cd01371   231 -RVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISAL--VDG---------KSTHIPYRDSKLTRLLQDS 298
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 568930680  319 LGGNSRTAMVAALSPADINYDETLSTLRYADRAKQI 354
Cdd:cd01371   299 LGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
5-354 4.31e-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: 345.08  E-value: 4.31e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    5 SVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKnpkEAPKSFSFDYSYwshtsPEDpcfASQNRVYNDIGKEMLLH 84
Cdd:cd01369     3 NIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATS---ETGKTFSFDRVF-----DPN---TTQEDVYNFAAKPIVDD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   85 AFEGYNVCIFAYGQTGAGKSYTMMGKQEESQA-GIIPQLCEELFEKINDNCnEEMSYSVEVSYMEIYCERVRDLLNPKNK 163
Cdd:cd01369    72 VLNGYNGTIFAYGQTSSGKTYTMEGKLGDPESmGIIPRIVQDIFETIYSMD-ENLEFHVKVSYFEIYMEKIRDLLDVSKT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  164 gNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKkqdpetNLSTE--KV 241
Cdd:cd01369   151 -NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE------NVETEkkKS 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  242 SKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEvdnctskskkkKKTDFIPYRDSVLTWLLRENLGG 321
Cdd:cd01369   224 GKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----------GKKTHIPYRDSKLTRILQDSLGG 292
                         330       340       350
                  ....*....|....*....|....*....|...
gi 568930680  322 NSRTAMVAALSPADINYDETLSTLRYADRAKQI 354
Cdd:cd01369   293 NSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
5-355 7.99e-106

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: 336.61  E-value: 7.99e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    5 SVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNpkeapKSFSFDYSYwshtSPEDPcfasQNRVYNDIGKEMLLH 84
Cdd:cd01372     2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTD-----KSFTFDYVF----DPSTE----QEEVYNTCVAPLVDG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   85 AFEGYNVCIFAYGQTGAGKSYTMMG----KQEESQAGIIPQLCEELFEKInDNCNEEMSYSVEVSYMEIYCERVRDLLNP 160
Cdd:cd01372    69 LFEGYNATVLAYGQTGSGKTYTMGTaytaEEDEEQVGIIPRAIQHIFKKI-EKKKDTFEFQLKVSFLEIYNEEIRDLLDP 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  161 KN--KGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETNLST 238
Cdd:cd01372   148 ETdkKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  239 EK------VSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEvdnctskskKKKKTDFIPYRDSVLT 312
Cdd:cd01372   228 ADdknstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGD---------ESKKGAHVPYRDSKLT 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 568930680  313 WLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIK 355
Cdd:cd01372   299 RLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
5-354 4.99e-105

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: 333.92  E-value: 4.99e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    5 SVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKnpkeaPKSFSFDYSYWSHtspedpcfaSQNR-VYNDIGKEMLL 83
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIYLVEPP-----STSFTFDHVFGGD---------STNReVYELIAKPVVK 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   84 HAFEGYNVCIFAYGQTGAGKSYTMMGKQEEsqAGIIPQLCEELFEKINDNCNEEmsYSVEVSYMEIYCERVRDLLNPKNK 163
Cdd:cd01374    67 SALEGYNGTIFAYGQTSSGKTFTMSGDEDE--PGIIPLAIRDIFSKIQDTPDRE--FLLRVSYLEIYNEKINDLLSPTSQ 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  164 gNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETNlSTEKVSK 243
Cdd:cd01374   143 -NLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEE-GTVRVST 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  244 ISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEvdnctskskkKKKTDFIPYRDSVLTWLLRENLGGNS 323
Cdd:cd01374   221 LNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQPSLGGNS 290
                         330       340       350
                  ....*....|....*....|....*....|.
gi 568930680  324 RTAMVAALSPADINYDETLSTLRYADRAKQI 354
Cdd:cd01374   291 RTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
11-356 3.09e-101

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: 323.78  E-value: 3.09e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   11 RVRPFNSRETSKESKCI-IQMQGNSTSIINPKNPKEapKSFSFDYSYwshtspeDPCfASQNRVYNDIgkEMLLH-AFEG 88
Cdd:cd01366     9 RVRPLLPSEENEDTSHItFPDEDGQTIELTSIGAKQ--KEFSFDKVF-------DPE-ASQEDVFEEV--SPLVQsALDG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   89 YNVCIFAYGQTGAGKSYTMMGKqeESQAGIIPQLCEELFEKINDNCNEEMSYSVEVSYMEIYCERVRDLLNPKNKGNLR- 167
Cdd:cd01366    77 YNVCIFAYGQTGSGKTYTMEGP--PESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLLAPGNAPQKKl 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  168 -VREHPLLGP-YVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQkkqdpeTNLSTEK--VSK 243
Cdd:cd01366   155 eIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISG------RNLQTGEisVGK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  244 ISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAevdnctskskkkKKTDFIPYRDSVLTWLLRENLGGNS 323
Cdd:cd01366   229 LNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYLLQDSLGGNS 296
                         330       340       350
                  ....*....|....*....|....*....|...
gi 568930680  324 RTAMVAALSPADINYDETLSTLRYADRAKQIKC 356
Cdd:cd01366   297 KTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
5-354 2.49e-98

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: 316.59  E-value: 2.49e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    5 SVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNPKEA-----------------PKSFSFDYSYwshtspeDPcF 67
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGffhggsnnrdrrkrrnkELKYVFDRVF-------DE-T 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   68 ASQNRVYNDIGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKqeESQAGIIPQLCEELFEKInDNCNEEMSYSVEVSYM 147
Cdd:cd01370    73 STQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGT--PQEPGLMVLTMKELFKRI-ESLKDEKEFEVSMSYL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  148 EIYCERVRDLLNPKNKGnLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQ 227
Cdd:cd01370   150 EIYNETIRDLLNPSSGP-LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQ 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  228 KKQDPETNLSTeKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEvdnctskskKKKKTDFIPYR 307
Cdd:cd01370   229 QDKTASINQQV-RQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD---------PGKKNKHIPYR 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 568930680  308 DSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQI 354
Cdd:cd01370   299 DSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
3-363 8.22e-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: 304.63  E-value: 8.22e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    3 GASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSII---NPKNPKEAPKSFSFDYSYWShtspedpcFASQNRVYNDIGK 79
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSvrtGGLADKSSTKTYTFDMVFGP--------EAKQIDVYRSVVC 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   80 EMLLHAFEGYNVCIFAYGQTGAGKSYTMMGK---------QEESQAGIIPQLCEELFEKINDNCNEemsYSVEVSYMEIY 150
Cdd:cd01364    73 PILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwELDPLAGIIPRTLHQLFEKLEDNGTE---YSVKVSYLEIY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  151 CERVRDLLNPKNKGNLRVREHPLL----GPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFT 226
Cdd:cd01364   150 NEELFDLLSPSSDVSERLRMFDDPrnkrGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIH 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  227 QKKQDPEtNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEvdnctskskkkkKTDFIPY 306
Cdd:cd01364   230 IKETTID-GEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------------RAPHVPY 296
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568930680  307 RDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVINED 363
Cdd:cd01364   297 RESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
6-363 9.72e-94

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: 304.43  E-value: 9.72e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    6 VKVAVRVRPFNSRETSKE-SKCIIQMqgNSTSIINPKNPkeaPKSFSFDYSYWSHTSPEDpcfasqnrVYNDIGKEMLLH 84
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEyGQCLKKL--SSDTLVLHSKP---PKTFTFDHVADSNTNQES--------VFQSVGKPIVES 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   85 AFEGYNVCIFAYGQTGAGKSYTMMGKQEESQA------GIIPQLCEELFEKIN---DNCNEEMSYSVEVSYMEIYCERVR 155
Cdd:cd01373    70 CLSGYNGTIFAYGQTGSGKTYTMWGPSESDNEsphglrGVIPRIFEYLFSLIQrekEKAGEGKSFLCKCSFLEIYNEQIY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  156 DLLNPKNKgNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQdpETN 235
Cdd:cd01373   150 DLLDPASR-NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEK--KAC 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  236 LSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkKKTDFIPYRDSVLTWLL 315
Cdd:cd01373   227 FVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAH--------GKQRHVCYRDSKLTFLL 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 568930680  316 RENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVINED 363
Cdd:cd01373   299 RDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
Kinesin_assoc pfam16183
Kinesin-associated;
358-555 2.95e-91

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 290.59  E-value: 2.95e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   358 AVINEDPNAKLVRELKEEVTRLKDLLRAQGLGdiididpliddysgsggkylkDFQNNKHRYLLASENQRPGNFSTASMG 437
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLG---------------------DIIDTIAHPTKKRANTPAANASAATAA 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   438 SLTSSPSSCSLNSQVGLTSVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIR 517
Cdd:pfam16183   60 MAGASPSPSLSALSSRAASVSSLHERIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIR 139
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 568930680   518 EDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGI 555
Cdd:pfam16183  140 EDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGI 177
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
1-374 1.10e-78

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 270.46  E-value: 1.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    1 MSGASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINpknpKEAPKSFSFDYSYWSHtspedpcfASQNRVYNDIGKE 80
Cdd:COG5059    13 LSSRNEKSVSDIKSTIRIIPGELGERLINTSKKSHVSLE----KSKEGTYAFDKVFGPS--------ATQEDVYEETIKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   81 MLLHAFEGYNVCIFAYGQTGAGKSYTMMGkqEESQAGIIPQLCEELFEKInDNCNEEMSYSVEVSYMEIYCERVRDLLNP 160
Cdd:COG5059    81 LIDSLLLGYNCTVFAYGQTGSGKTYTMSG--TEEEPGIIPLSLKELFSKL-EDLSMTKDFAVSISYLEIYNEKIYDLLSP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  161 KNKGnLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETNLStek 240
Cdd:COG5059   158 NEES-LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET--- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  241 vSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkkTDFIPYRDSVLTWLLRENLG 320
Cdd:COG5059   234 -SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKK----------SGHIPYRESKLTRLLQDSLG 302
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568930680  321 GNSRTAMVAALSPADINYDETLSTLRYADRAKQIK-----CNAVINEDPNAKLVRELKE 374
Cdd:COG5059   303 GNCNTRVICTISPSSNSFEETINTLKFASRAKSIKnkiqvNSSSDSSREIEEIKFDLSE 361
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
530-639 2.46e-78

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: 252.26  E-value: 2.46e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  530 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCLFRSERSNTGEVIVTLEPCERSETYVNG 609
Cdd:cd22727     1 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNNNGEVIVTLEPCERSETYVNG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 568930680  610 KRVAHPVQLRSGNRIIMGKNHVFRFNHPEQ 639
Cdd:cd22727    81 KRVVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
PLN03188 PLN03188
kinesin-12 family protein; Provisional
1-381 3.37e-72

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 264.10  E-value: 3.37e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    1 MSGASVKVAVRVRPFNSREtskESKCIIQMQGNSTSIINPKnpkeapkSFSFDysywSHTSPEdpcfASQNRVYNDIGKE 80
Cdd:PLN03188   95 VSDSGVKVIVRMKPLNKGE---EGEMIVQKMSNDSLTINGQ-------TFTFD----SIADPE----STQEDIFQLVGAP 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   81 MLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQ----EES----QAGIIPQLCEELFEKIND----NCNEEMSYSVEVSYME 148
Cdd:PLN03188  157 LVENCLAGFNSSVFAYGQTGSGKTYTMWGPAngllEEHlsgdQQGLTPRVFERLFARINEeqikHADRQLKYQCRCSFLE 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  149 IYCERVRDLLNPKNKgNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQK 228
Cdd:PLN03188  237 IYNEQITDLLDPSQK-NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESR 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  229 KQDPETNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKkkkktdfIPYRD 308
Cdd:PLN03188  316 CKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRH-------IPYRD 388
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568930680  309 SVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVINE----DPN--AKLVRELKEEVTRLKD 381
Cdd:PLN03188  389 SRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVKA 467
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
6-352 4.19e-69

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: 235.75  E-value: 4.19e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    6 VKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINP----------KNPKEAPKSFSFDYSYWSHTSpedpcfasQNRVYN 75
Cdd:cd01368     3 VKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPpkgsaankseRNGGQKETKFSFSKVFGPNTT--------QKEFFQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   76 DIGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEesQAGIIPQLCEELFEKINDncneemsYSVEVSYMEIYCERVR 155
Cdd:cd01368    75 GTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPG--DGGILPRSLDVIFNSIGG-------YSVFVSYIEIYNEYIY 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  156 DLLNP------KNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKK 229
Cdd:cd01368   146 DLLEPspssptKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAP 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  230 QDPETNLSTEK----VSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEvdnctskSKKKKKTDFIP 305
Cdd:cd01368   226 GDSDGDVDQDKdqitVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE-------NQLQGTNKMVP 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 568930680  306 YRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAK 352
Cdd:cd01368   299 FRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
6-352 4.50e-69

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


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 234.70  E-value: 4.50e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    6 VKVAVRVRPFNSRETSKESK-CIIQMQGNSTSIINPKNPKEaPKSFSFDYSYwshtSPEDpcfaSQNRVYNDIGKEMLLH 84
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPsCVSGIDSCSVELADPRNHGE-TLKYQFDAFY----GEES----TQEDIYAREVQPIVPH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   85 AFEGYNVCIFAYGQTGAGKSYTMMGkqEESQAGIIPQLCEELFEkINDNcnEEMSYSVEVSYMEIYCERVRDLLNPKNKg 164
Cdd:cd01376    73 LLEGQNATVFAYGSTGAGKTFTMLG--SPEQPGLMPLTVMDLLQ-MTRK--EAWALSFTMSYLEIYQEKILDLLEPASK- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  165 NLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETNLSTekvSKI 244
Cdd:cd01376   147 ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRT---GKL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  245 SLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCtskskkkkktdfIPYRDSVLTWLLRENLGGNSR 324
Cdd:cd01376   224 NLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR------------IPYRDSKLTRLLQDSLGGGSR 291
                         330       340
                  ....*....|....*....|....*...
gi 568930680  325 TAMVAALSPADINYDETLSTLRYADRAK 352
Cdd:cd01376   292 CIMVANIAPERTFYQDTLSTLNFAARSR 319
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
531-645 4.99e-69

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: 226.35  E-value: 4.99e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  531 TPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCLFRSERSNTGEVIVTLEPCERSETYVNGK 610
Cdd:cd22726     1 TPHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSGGEAVVTLEPCEGADTYVNGK 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568930680  611 RVAHPVQLRSGNRIIMGKNHVFRFNHPEQARAERE 645
Cdd:cd22726    81 KVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
5-352 1.54e-67

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: 230.93  E-value: 1.54e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    5 SVKVAVRVRPfnsreTSKESKCIIQM--QGNSTSIINPKNPKEAP-----KSFSFDYSYWSHTspedpcfASQNRVYNDI 77
Cdd:cd01375     1 KVQAFVRVRP-----TDDFAHEMIKYgeDGKSISIHLKKDLRRGVvnnqqEDWSFKFDGVLHN-------ASQELVYETV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   78 GKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEE-SQAGIIPQLCEELFEKINDNCNEemSYSVEVSYMEIYCERVRD 156
Cdd:cd01375    69 AKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENyKHRGIIPRALQQVFRMIEERPTK--AYTVHVSYLEIYNEQLYD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  157 LLNPKNKGN-----LRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQD 231
Cdd:cd01375   147 LLSTLPYVGpsvtpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRT 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  232 PetnlSTEKV--SKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkktDFIPYRDS 309
Cdd:cd01375   227 L----SSEKYitSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDR-----------THVPFRQS 291
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 568930680  310 VLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAK 352
Cdd:cd01375   292 KLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
6-352 5.21e-67

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: 229.10  E-value: 5.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    6 VKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNPKEAP------KSFSFDYSYWSHTSPEDpcfasqnrVYNDIGK 79
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKVDLtkyienHTFRFDYVFDESSSNET--------VYRSTVK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   80 EMLLHAFEGYNVCIFAYGQTGAGKSYTMMGK--QEESQAGIIPQLCEELFEKINDNCNEeMSYSVEVSYMEIYCERVRDL 157
Cdd:cd01367    74 PLVPHIFEGGKATCFAYGQTGSGKTYTMGGDfsGQEESKGIYALAARDVFRLLNKLPYK-DNLGVTVSFFEIYGGKVFDL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  158 LNPKNKgnLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFtqkkQDPETNLS 237
Cdd:cd01367   153 LNRKKR--VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL----RDRGTNKL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  238 tekVSKISLVDLAGSER-ADSTGAKGTRLKEGANINKSLTTLGKVISALAevdnctskskkkKKTDFIPYRDSVLTWLLR 316
Cdd:cd01367   227 ---HGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHIPFRGSKLTQVLK 291
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 568930680  317 ENL-GGNSRTAMVAALSPADINYDETLSTLRYADRAK 352
Cdd:cd01367   292 DSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
531-636 1.83e-62

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: 207.09  E-value: 1.83e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  531 TPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCLFRSErsntgEVIVTLEPCERSETYVNGK 610
Cdd:cd22705     1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENE-----DGVVTLEPCEGALTYVNGK 75
                          90       100
                  ....*....|....*....|....*.
gi 568930680  611 RVAHPVQLRSGNRIIMGKNHVFRFNH 636
Cdd:cd22705    76 RVTEPTRLKTGSRVILGKNHVFRFNH 101
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
531-636 4.30e-55

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: 186.23  E-value: 4.30e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  531 TPHLVNLNEDPLMSECLLYYIKDGITRVGQADAerrqDIVLSGAHIKEEHCLFRSERSNTGEVIVTLEPCERSETYVNGK 610
Cdd:cd22728     1 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFRSIPNPSGEVVVTLEPCEGAETYVNGK 76
                          90       100
                  ....*....|....*....|....*.
gi 568930680  611 RVAHPVQLRSGNRIIMGKNHVFRFNH 636
Cdd:cd22728    77 QVTEPLVLKSGNRIVMGKNHVFRFNH 102
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
530-637 6.12e-37

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: 134.70  E-value: 6.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  530 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCLFRSERSntgevIVTLEPCERSETYVNG 609
Cdd:cd22707     6 KLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGG-----KVTIIPVGDAETYVNG 80
                          90       100
                  ....*....|....*....|....*...
gi 568930680  610 KRVAHPVQLRSGNRIIMGKNHVFRFNHP 637
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 4.32e-36

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: 134.78  E-value: 4.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680    8 VAVRVRPFNSRETSKESKCIIqmqgnstsiinpknpkeapksfsFDYSYWSHTSPEDpcfasqnrVYNDIGKeMLLHAFE 87
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKIIV-----------------------FYRGFRRSESQPH--------VFAIADP-AYQSMLD 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   88 GYNV-CIFAYGQTGAGKSYTMMgkqeesqaGIIPQLCEELFEKINDNCNEEMSYsvevsymeiycervrdllnpknkgnl 166
Cdd:cd01363    49 GYNNqSIFAYGESGAGKTETMK--------GVIPYLASVAFNGINKGETEGWVY-------------------------- 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  167 rvrehpllgpyvedLSKLAVTSYTDIADLMDAGNKARTvAATNMNETSSRSHAVFTIVftqkkqdpetnlstekvskisl 246
Cdd:cd01363    95 --------------LTEITVTLEDQILQANPILEAFGN-AKTTRNENSSRFGKFIEIL---------------------- 137
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568930680  247 VDLAGSERadstgakgtrlkeganINKSLTTLGKVISA 284
Cdd:cd01363   138 LDIAGFEI----------------INESLNTLMNVLRA 159
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
532-637 9.05e-36

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: 131.18  E-value: 9.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  532 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCLFrserSNTGEViVTLEPC-ERSETYVNGK 610
Cdd:cd22709     1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVI----TNTDGK-VTIEPVsPGAKVIVNGV 75
                          90       100
                  ....*....|....*....|....*..
gi 568930680  611 RVAHPVQLRSGNRIIMGKNHVFRFNHP 637
Cdd:cd22709    76 PVTGETELHHLDRVILGSNHLYVFVGP 102
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
530-637 1.61e-32

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: 121.99  E-value: 1.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  530 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCLFRSERsntGEviVTLEPCERSETYVNG 609
Cdd:cd22708     7 ELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVG---GV--VTLHPLPGALCAVNG 81
                          90       100
                  ....*....|....*....|....*...
gi 568930680  610 KRVAHPVQLRSGNRIIMGKNHVFRFNHP 637
Cdd:cd22708    82 QVITQPTRLTQGDVILLGKTNMFRFNHP 109
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
534-637 9.00e-31

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: 116.62  E-value: 9.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  534 LVNLNEDPLMSECLLYYIKDgITRVGQADAERRQDIVLSGAHIKEEHCLFRSErsntgEVIVTLEPCERSETYVNGKRVA 613
Cdd:cd22706     4 LVNLNADPSLNELLVYYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIE-----NEDVYLTPLEGARTCVNGSIVT 77
                          90       100
                  ....*....|....*....|....
gi 568930680  614 HPVQLRSGNRIIMGKNHVFRFNHP 637
Cdd:cd22706    78 EKTQLRHGDRILWGNNHFFRLNCP 101
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
524-646 3.56e-29

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: 112.95  E-value: 3.56e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  524 GVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCLFRSERSntgevIVTLEPCERS 603
Cdd:cd22731     1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECG-----VVTLRPAQGA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568930680  604 ETYVNGKRVAHPVQLRSGNRIIMGKNHVFRFNHPEQARAEREK 646
Cdd:cd22731    76 QCTVNGREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQR 118
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
524-645 3.37e-25

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: 101.55  E-value: 3.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  524 GVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCLFRSERSNtgeviVTLEPCERS 603
Cdd:cd22732     1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENLNGT-----VTLIPLNGA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568930680  604 ETYVNGKRVAHPVQLRSGNRIIMGKNHVFRFNHPEQARAERE 645
Cdd:cd22732    76 QCSVNGVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
534-637 4.63e-23

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: 94.60  E-value: 4.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  534 LVNLNEDPLMSECLLYYIKDGiTRVGQADAerrQDIVLSGAHIKEEHCLFrsERSNTGEVIVTlePCERSETYVNGKRVA 613
Cdd:cd22730     4 LVNLNADPALNELLVYYLKEH-TLIGSADS---QDIQLCGMGILPEHCII--DITPEGQVMLT--PQKNTRTFVNGSAVT 75
                          90       100
                  ....*....|....*....|....
gi 568930680  614 HPVQLRSGNRIIMGKNHVFRFNHP 637
Cdd:cd22730    76 SPIQLHHGDRILWGNNHFFRINLP 99
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
534-646 2.93e-22

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: 92.64  E-value: 2.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  534 LVNLNEDPLMSECLLYYIKDGiTRVGqadAERRQDIVLSGAHIKEEHCLFrsERSNTGEVIVTlePCERSETYVNGKRVA 613
Cdd:cd22729     4 LVNLNADPALNELLVYYLKDH-TRVG---ADTSQDIQLFGIGIQPEHCVI--DIAADGDVTLT--PKENARTCVNGTLVC 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 568930680  614 HPVQLRSGNRIIMGKNHVFRFNHPEQARAEREK 646
Cdd:cd22729    76 SVTQLWHGDRILWGNNHFFRINLPKRKRRDWLK 108
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
518-640 2.09e-16

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: 76.60  E-value: 2.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  518 EDGGTLGVFSPKktPHLVNLNEDPLMSECLLYYIKDGITRVGQADAErrqDIVLSGAHIKEEHCLFrsERSNTgevIVTL 597
Cdd:cd22713     5 ETGKALKVQTEK--PHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASD---IISLQGPGVEPEHCYI--ENING---TVTL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568930680  598 EPCeRSETYVNGKRVAHPVQLRSGNRIIMGKNHVFRFNHPEQA 640
Cdd:cd22713    75 YPC-GNLCSVDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEA 116
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
532-637 2.77e-16

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: 75.82  E-value: 2.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  532 PHLVNLNEDPLMSECL-LYYIKDGITRVG--QADAERRQDIVLSGAHIKEEHCLFRsersNTgEVIVTLEPCER-SETYV 607
Cdd:cd22711     2 PYLLELSPDGSDRDKPrRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVIT----HM-EGVVTVTPASQdAETYV 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 568930680  608 NGKRVAHPVQLRSGNRIIMGKNHVFRFNHP 637
Cdd:cd22711    77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
5-158 1.52e-14

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 71.87  E-value: 1.52e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680     5 SVKVAVRVRPFNSREtskeskciIQMQGNSTSIINPKNPKEApKSFSFDYSYwshtspedPCFASQNRVYNDIgkEMLLH 84
Cdd:pfam16796   21 NIRVFARVRPELLSE--------AQIDYPDETSSDGKIGSKN-KSFSFDRVF--------PPESEQEDVFQEI--SQLVQ 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568930680    85 -AFEGYNVCIFAYGQTGAGksytmmgkqeeSQAGIIPQLCEELFEKINDNCNEEmSYSVEVSYMEIYCERVRDLL 158
Cdd:pfam16796   82 sCLDGYNVCIFAYGQTGSG-----------SNDGMIPRAREQIFRFISSLKKGW-KYTIELQFVEIYNESSQDLL 144
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
533-634 1.85e-09

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


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 55.74  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  533 HLVNLNEDPLMSEcllYYIKDGITRVGQADAerrQDIVLSGAHIKEEHCLFRSERSNtgeviVTLEPCERS-ETYVNGKR 611
Cdd:cd00060     1 RLIVLDGDGGGRE---FPLTKGVVTIGRSPD---CDIVLDDPSVSRRHARIEVDGGG-----VYLEDLGSTnGTFVNGKR 69
                          90       100
                  ....*....|....*....|...
gi 568930680  612 VAHPVQLRSGNRIIMGkNHVFRF 634
Cdd:cd00060    70 ITPPVPLQDGDVIRLG-DTTFRF 91
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
531-637 5.53e-07

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: 49.61  E-value: 5.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  531 TPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQ-DIVLSGAHIKEEHC-LFRSE---------RSNTGEVIVTLEP 599
Cdd:cd22712     3 YPYLLTLRGFSPKQDLLVYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCwIRRKPeplsddedsDKESADYRVVLSP 82
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568930680  600 CERSETYVNGKRVAHPVQLRSGNRIIMGKNHVFRFNHP 637
Cdd:cd22712    83 LRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
556-624 1.36e-06

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 46.80  E-value: 1.36e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568930680   556 TRVGQADaerRQDIVLSGAHIKEEHCLFRSERSNTgeviVTLEPC-ERSETYVNGKRVAH-PVQLRSGNRI 624
Cdd:pfam00498    1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYDGGGR----FYLEDLgSTNGTFVNGQRLGPePVRLKDGDVI 64
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
530-637 3.73e-06

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: 47.10  E-value: 3.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  530 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCLFRSER---SNTGEVIVtLEPCERSETY 606
Cdd:cd22733     4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRRVRlpkHRSEEKLV-LEPIPGAHVS 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 568930680  607 VNGKRVAHPVQLRSGNRIIMGKNHVFRFNHP 637
Cdd:cd22733    83 VNFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
551-634 5.29e-06

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 46.10  E-value: 5.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  551 IKDGITRVGQADaerRQDIVLSGAHIKEEHCLFRseRSNTGEVIVTLEpcERSETYVNGKRVAHPVQLRSGNRIIMGKnH 630
Cdd:COG1716    18 LDGGPLTIGRAP---DNDIVLDDPTVSRRHARIR--RDGGGWVLEDLG--STNGTFVNGQRVTEPAPLRDGDVIRLGK-T 89

                  ....
gi 568930680  631 VFRF 634
Cdd:COG1716    90 ELRF 93
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
568-634 2.68e-05

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: 44.13  E-value: 2.68e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568930680  568 DIVLSGAHIKEEHClfRSERSNTGEVivTLEP-CERSETYVNGKRVAHPVQLRSGNRIIMGkNHVFRF 634
Cdd:cd22673    32 DIRIQLPGVSREHC--RIEVDENGKA--YLENlSTTNPTLVNGKAIEKSAELKDGDVITIG-GRSFRF 94
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
93-285 4.21e-05

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 47.81  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680   93 IFAYGQTGAGKSYTMMgkqeESQAGIIPQLCEELFEKINDNCNEEMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHp 172
Cdd:COG5059   385 IFAYMQSLKKETETLK----SRIDLIMKSIISGTFERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHK- 459
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  173 llgpyVEDLSKLAVTSYT-------DIADLMDAGNKaRTVAATNMNETSSRSHAVFtivftqKKQDPETNLSTEKVSKIs 245
Cdd:COG5059   460 -----LNKLRHDLSSLLSsipeetsDRVESEKASKL-RSSASTKLNLRSSRSHSKF------RDHLNGSNSSTKELSLN- 526
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568930680  246 LVDLAGSERaDSTGAKGTRLKEGANINKSLTTLGKVISAL 285
Cdd:COG5059   527 QVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
545-636 1.99e-03

forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438722 [Multi-domain]  Cd Length: 105  Bit Score: 39.13  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568930680  545 ECLLYYIKDGITRVGQadaERRQDIVLSGAHIKEEHCLFRSER-SNTGEVIVTLEPCERSETYVNGKRV--AHPVQLRSG 621
Cdd:cd22670    13 DIVLPIYKNQVITIGR---SPSCDIVINDPFVSRTHCRIYSVQfDESSAPLVYVEDLSSNGTYLNGKLIgrNNTVLLSDG 89
                          90
                  ....*....|....*
gi 568930680  622 NRIIMGKNHVFRFNH 636
Cdd:cd22670    90 DVIEIAHSATFVYVH 104
 
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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