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Conserved domains on  [gi|1734329465|ref|NP_001360295|]
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Kinesin-like protein [Caenorhabditis elegans]

Protein Classification

kinesin family protein; myosin/kinesin family protein( domain architecture ID 581995)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has ATPase-containing motor domain; similar to N-type kinesins that are (+) end-directed motors and have an N-terminal motor domain| myosin/kinesin family protein; contains an ATPase-containing motor domain found in myosins and kinesins, which provides the driving force in myosin and kinesin mediated processes; may have a coiled-coil segment C-terminal to the motor domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Motor_domain super family cl22853
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
26-426 1.86e-121

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.


The actual alignment was detected with superfamily member cd01368:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 345  Bit Score: 368.26  E-value: 1.86e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  26 DSIEVVCRLCPYtgSTPSLIAIDEGSI-----QTVL--PPAQFR----RENAPQVEKVFRFGRVFSENDGQATVFERTSV 94
Cdd:cd01368     1 DPVKVYLRVRPL--SKDELESEDEGCIevinsTTVVlhPPKGSAanksERNGGQKETKFSFSKVFGPNTTQKEFFQGTAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  95 DLILNLLKGQNSLLFTYGVTGSGKTYTMTGkpTETGTGLLPRTLDVIFNSInnrvekcifypsalntfeiratldahlkr 174
Cdd:cd01368    79 PLVQDLLHGKNGLLFTYGVTNSGKTYTMQG--SPGDGGILPRSLDVIFNSI----------------------------- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 175 hqmaadrlstsreitdryceaiklSGYnddmvcSVFVTYVEIYNNYCYDLLEDA-RNGSRVLTKREIRHDRQQQMYVDGA 253
Cdd:cd01368   128 ------------------------GGY------SVFVSYIEIYNEYIYDLLEPSpSSPTKKRQSLRLREDHNGNMYVAGL 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 254 KDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAPRAyETKSVypTMDSSQIIVSQLCLVDLAGSER 333
Cdd:cd01368   178 TEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGD-SDGDV--DQDKDQITVSQLSLVDLAGSER 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 334 AKRTQNVGERLAEANSINQSLMTLRQCIEVLRRNQKSSSQNLeqVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYD 413
Cdd:cd01368   255 TSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKM--VPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYD 332
                         410
                  ....*....|...
gi 1734329465 414 ENMSALAFAEESQ 426
Cdd:cd01368   333 ETLHVMKFSAIAQ 345
MKLP1_Arf_bdg super family cl24941
Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region ...
673-749 1.24e-25

Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region of mitotic kinesin-like proteins that is necessary for the interaction with the small GTPase Arf6. MKLP1 is a Flemming body-localising protein essential for cytokinesis, so its interaction with Arf6 shows how Arf6 is involved in cytokinesis. The Arf6-MKLP1 complex plays a crucial role in cytokinesis by connecting the microtubule bundle and membranes at the cleavage plane.


The actual alignment was detected with superfamily member pfam16540:

Pssm-ID: 465166  Cd Length: 107  Bit Score: 101.62  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 673 YVNPKYqRRSKSA-SRLLDHQPLHRVPTGTVLQSRTPA--NAIRTTKPEMHQLNKSGEYRLTHQEVDDEGNISTNIVKVN 749
Cdd:pfam16540   2 VVNPRH-RRSRSAgERWLDHKPPSNVPTGTILQPRIPNrkSVTKLTKPKDKALAKASKYCLTHQEQDSDGEIETKLYKGD 80
 
Name Accession Description Interval E-value
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
26-426 1.86e-121

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: 368.26  E-value: 1.86e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  26 DSIEVVCRLCPYtgSTPSLIAIDEGSI-----QTVL--PPAQFR----RENAPQVEKVFRFGRVFSENDGQATVFERTSV 94
Cdd:cd01368     1 DPVKVYLRVRPL--SKDELESEDEGCIevinsTTVVlhPPKGSAanksERNGGQKETKFSFSKVFGPNTTQKEFFQGTAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  95 DLILNLLKGQNSLLFTYGVTGSGKTYTMTGkpTETGTGLLPRTLDVIFNSInnrvekcifypsalntfeiratldahlkr 174
Cdd:cd01368    79 PLVQDLLHGKNGLLFTYGVTNSGKTYTMQG--SPGDGGILPRSLDVIFNSI----------------------------- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 175 hqmaadrlstsreitdryceaiklSGYnddmvcSVFVTYVEIYNNYCYDLLEDA-RNGSRVLTKREIRHDRQQQMYVDGA 253
Cdd:cd01368   128 ------------------------GGY------SVFVSYIEIYNEYIYDLLEPSpSSPTKKRQSLRLREDHNGNMYVAGL 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 254 KDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAPRAyETKSVypTMDSSQIIVSQLCLVDLAGSER 333
Cdd:cd01368   178 TEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGD-SDGDV--DQDKDQITVSQLSLVDLAGSER 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 334 AKRTQNVGERLAEANSINQSLMTLRQCIEVLRRNQKSSSQNLeqVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYD 413
Cdd:cd01368   255 TSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKM--VPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYD 332
                         410
                  ....*....|...
gi 1734329465 414 ENMSALAFAEESQ 426
Cdd:cd01368   333 ETLHVMKFSAIAQ 345
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
27-434 1.72e-116

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: 354.96  E-value: 1.72e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465   27 SIEVVCRLCPYTGST-----PSLIAIDEGSIQTVLppaqFRRENAPQVEKVFRFGRVFSENDGQATVFERTSVDLILNLL 101
Cdd:smart00129   1 NIRVVVRVRPLNKREksrksPSVVPFPDKVGKTLT----VRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  102 KGQNSLLFTYGVTGSGKTYTMTGKPTETGtgLLPRTLDVIFNSINNRvekcifypsalntfeiratldahlkrhqmaadr 181
Cdd:smart00129  77 EGYNATIFAYGQTGSGKTYTMIGTPDSPG--IIPRALKDLFEKIDKR--------------------------------- 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  182 lstsreitdryceaiklsgyNDDMVCSVFVTYVEIYNNYCYDLLEDARNgsrvltKREIRHDRQQQMYVDGAKDVEVSSS 261
Cdd:smart00129 122 --------------------EEGWQFSVKVSYLEIYNEKIRDLLNPSSK------KLEIREDEKGGVYVKGLTEISVSSF 175
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  262 EEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAPRayetksvypTMDSSQIIVSQLCLVDLAGSERAKRTQNVG 341
Cdd:smart00129 176 EEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIK---------NSSSGSGKASKLNLVDLAGSERAKKTGAEG 246
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  342 ERLAEANSINQSLMTLRQCIEVLRRNQKSSsqnleQVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYDENMSALAF 421
Cdd:smart00129 247 DRLKEAGNINKSLSALGNVINALAQHSKSR-----HIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRF 321
                          410
                   ....*....|...
gi 1734329465  422 AEESQTIEVKKQV 434
Cdd:smart00129 322 ASRAKEIKNKPIV 334
Kinesin pfam00225
Kinesin motor domain;
70-428 9.18e-100

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 311.43  E-value: 9.18e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  70 EKVFRFGRVFSENDGQATVFERTSVDLILNLLKGQNSLLFTYGVTGSGKTYTMTGKPTETGtgLLPRTLDVIFNSINNRV 149
Cdd:pfam00225  39 TKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPG--IIPRALEDLFDRIQKTK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 150 EKCIFypsalntfeiratldahlkrhqmaadrlstsreitdryceaiklsgynddmvcSVFVTYVEIYNNYCYDLLEDAR 229
Cdd:pfam00225 117 ERSEF-----------------------------------------------------SVKVSYLEIYNEKIRDLLSPSN 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 230 NGSRVLtkrEIRHDRQQQMYVDGAKDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAPRAyetksv 309
Cdd:pfam00225 144 KNKRKL---RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRS------ 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 310 ypTMDSSQIIVSQLCLVDLAGSERAKRTQNV-GERLAEANSINQSLMTLRQCIEVLRRNQKSSsqnleqVPYRQSKLTHL 388
Cdd:pfam00225 215 --TGGEESVKTGKLNLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALADKKSKH------IPYRDSKLTRL 286
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1734329465 389 FKNYLEGNGKIRMVICVNPKPDDYDENMSALAFAEESQTI 428
Cdd:pfam00225 287 LQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
68-435 2.13e-55

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 199.97  E-value: 2.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  68 QVEKVFRFGRVFSENDGQATVFERTSVDLILNLLKGQNSLLFTYGVTGSGKTYTMTGkpTETGTGLLPRTLDVIFnsinn 147
Cdd:COG5059    53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG--TEEEPGIIPLSLKELF----- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 148 rvekcifypsalntfeiratldahlkrhqmaaDRLSTSREITDRyceAIKLSgynddmvcsvfvtYVEIYNNYCYDLLED 227
Cdd:COG5059   126 --------------------------------SKLEDLSMTKDF---AVSIS-------------YLEIYNEKIYDLLSP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 228 ARNGSRvltkreIRHDRQQQMYVDGAKDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIklvmaprayETK 307
Cdd:COG5059   158 NEESLN------IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI---------ELA 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 308 SVYPTMDSSQIivSQLCLVDLAGSERAKRTQNVGERLAEANSINQSLMTLRQCIEVLRRNQKSSSqnleqVPYRQSKLTH 387
Cdd:COG5059   223 SKNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSGH-----IPYRESKLTR 295
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1734329465 388 LFKNYLEGNGKIRMVICVNPKPDDYDENMSALAFAEESQTIEVKKQVE 435
Cdd:COG5059   296 LLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
PLN03188 PLN03188
kinesin-12 family protein; Provisional
70-465 2.15e-35

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 145.08  E-value: 2.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465   70 EKVFRFGRVFSENDGQATVFERTSVDLILNLLKGQNSLLFTYGVTGSGKTYTMTGKptetGTGLLPRTLDVIFNSINNRV 149
Cdd:PLN03188   131 GQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGP----ANGLLEEHLSGDQQGLTPRV 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  150 EKCIFypSALNTFEIRATlDAHLKRHqmaadrlstsreitdryCEaiklsgynddmvCSvfvtYVEIYNNYCYDLLEDA- 228
Cdd:PLN03188   207 FERLF--ARINEEQIKHA-DRQLKYQ-----------------CR------------CS----FLEIYNEQITDLLDPSq 250
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  229 RNgsrvltkREIRHDRQQQMYVDGAKDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIklVMAPRAyetKS 308
Cdd:PLN03188   251 KN-------LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC--VVESRC---KS 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  309 VYPTMDSSQiiVSQLCLVDLAGSERAKRTQNVGERLAEANSINQSLMTLRQCIEVLRRNQKSSSQnlEQVPYRQSKLTHL 388
Cdd:PLN03188   319 VADGLSSFK--TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQ--RHIPYRDSRLTFL 394
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1734329465  389 FKNYLEGNGKIRMVICVNPKPDDYDENMSALAFAEESQTIEVKKQVERMPSERIPH--SFFTQWNSELDgsvRMEDDGS 465
Cdd:PLN03188   395 LQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDDVNFlrEVIRQLRDELQ---RVKANGN 470
MKLP1_Arf_bdg pfam16540
Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region ...
673-749 1.24e-25

Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region of mitotic kinesin-like proteins that is necessary for the interaction with the small GTPase Arf6. MKLP1 is a Flemming body-localising protein essential for cytokinesis, so its interaction with Arf6 shows how Arf6 is involved in cytokinesis. The Arf6-MKLP1 complex plays a crucial role in cytokinesis by connecting the microtubule bundle and membranes at the cleavage plane.


Pssm-ID: 465166  Cd Length: 107  Bit Score: 101.62  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 673 YVNPKYqRRSKSA-SRLLDHQPLHRVPTGTVLQSRTPA--NAIRTTKPEMHQLNKSGEYRLTHQEVDDEGNISTNIVKVN 749
Cdd:pfam16540   2 VVNPRH-RRSRSAgERWLDHKPPSNVPTGTILQPRIPNrkSVTKLTKPKDKALAKASKYCLTHQEQDSDGEIETKLYKGD 80
 
Name Accession Description Interval E-value
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
26-426 1.86e-121

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: 368.26  E-value: 1.86e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  26 DSIEVVCRLCPYtgSTPSLIAIDEGSI-----QTVL--PPAQFR----RENAPQVEKVFRFGRVFSENDGQATVFERTSV 94
Cdd:cd01368     1 DPVKVYLRVRPL--SKDELESEDEGCIevinsTTVVlhPPKGSAanksERNGGQKETKFSFSKVFGPNTTQKEFFQGTAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  95 DLILNLLKGQNSLLFTYGVTGSGKTYTMTGkpTETGTGLLPRTLDVIFNSInnrvekcifypsalntfeiratldahlkr 174
Cdd:cd01368    79 PLVQDLLHGKNGLLFTYGVTNSGKTYTMQG--SPGDGGILPRSLDVIFNSI----------------------------- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 175 hqmaadrlstsreitdryceaiklSGYnddmvcSVFVTYVEIYNNYCYDLLEDA-RNGSRVLTKREIRHDRQQQMYVDGA 253
Cdd:cd01368   128 ------------------------GGY------SVFVSYIEIYNEYIYDLLEPSpSSPTKKRQSLRLREDHNGNMYVAGL 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 254 KDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAPRAyETKSVypTMDSSQIIVSQLCLVDLAGSER 333
Cdd:cd01368   178 TEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGD-SDGDV--DQDKDQITVSQLSLVDLAGSER 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 334 AKRTQNVGERLAEANSINQSLMTLRQCIEVLRRNQKSSSQNLeqVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYD 413
Cdd:cd01368   255 TSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKM--VPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYD 332
                         410
                  ....*....|...
gi 1734329465 414 ENMSALAFAEESQ 426
Cdd:cd01368   333 ETLHVMKFSAIAQ 345
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
27-434 1.72e-116

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: 354.96  E-value: 1.72e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465   27 SIEVVCRLCPYTGST-----PSLIAIDEGSIQTVLppaqFRRENAPQVEKVFRFGRVFSENDGQATVFERTSVDLILNLL 101
Cdd:smart00129   1 NIRVVVRVRPLNKREksrksPSVVPFPDKVGKTLT----VRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  102 KGQNSLLFTYGVTGSGKTYTMTGKPTETGtgLLPRTLDVIFNSINNRvekcifypsalntfeiratldahlkrhqmaadr 181
Cdd:smart00129  77 EGYNATIFAYGQTGSGKTYTMIGTPDSPG--IIPRALKDLFEKIDKR--------------------------------- 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  182 lstsreitdryceaiklsgyNDDMVCSVFVTYVEIYNNYCYDLLEDARNgsrvltKREIRHDRQQQMYVDGAKDVEVSSS 261
Cdd:smart00129 122 --------------------EEGWQFSVKVSYLEIYNEKIRDLLNPSSK------KLEIREDEKGGVYVKGLTEISVSSF 175
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  262 EEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAPRayetksvypTMDSSQIIVSQLCLVDLAGSERAKRTQNVG 341
Cdd:smart00129 176 EEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIK---------NSSSGSGKASKLNLVDLAGSERAKKTGAEG 246
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  342 ERLAEANSINQSLMTLRQCIEVLRRNQKSSsqnleQVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYDENMSALAF 421
Cdd:smart00129 247 DRLKEAGNINKSLSALGNVINALAQHSKSR-----HIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRF 321
                          410
                   ....*....|...
gi 1734329465  422 AEESQTIEVKKQV 434
Cdd:smart00129 322 ASRAKEIKNKPIV 334
Kinesin pfam00225
Kinesin motor domain;
70-428 9.18e-100

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 311.43  E-value: 9.18e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  70 EKVFRFGRVFSENDGQATVFERTSVDLILNLLKGQNSLLFTYGVTGSGKTYTMTGKPTETGtgLLPRTLDVIFNSINNRV 149
Cdd:pfam00225  39 TKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPG--IIPRALEDLFDRIQKTK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 150 EKCIFypsalntfeiratldahlkrhqmaadrlstsreitdryceaiklsgynddmvcSVFVTYVEIYNNYCYDLLEDAR 229
Cdd:pfam00225 117 ERSEF-----------------------------------------------------SVKVSYLEIYNEKIRDLLSPSN 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 230 NGSRVLtkrEIRHDRQQQMYVDGAKDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAPRAyetksv 309
Cdd:pfam00225 144 KNKRKL---RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRS------ 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 310 ypTMDSSQIIVSQLCLVDLAGSERAKRTQNV-GERLAEANSINQSLMTLRQCIEVLRRNQKSSsqnleqVPYRQSKLTHL 388
Cdd:pfam00225 215 --TGGEESVKTGKLNLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALADKKSKH------IPYRDSKLTRL 286
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1734329465 389 FKNYLEGNGKIRMVICVNPKPDDYDENMSALAFAEESQTI 428
Cdd:pfam00225 287 LQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
27-423 4.95e-99

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: 309.57  E-value: 4.95e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  27 SIEVVCRLCPYTGST----PSLIAIDEGSIQTVLPPAQFRRENapqveKVFRFGRVFSENDGQATVFERTSVDLILNLLK 102
Cdd:cd00106     1 NVRVAVRVRPLNGREarsaKSVISVDGGKSVVLDPPKNRVAPP-----KTFAFDAVFDSTSTQEEVYEGTAKPLVDSALE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 103 GQNSLLFTYGVTGSGKTYTMTGKPTEtGTGLLPRTLDVIFNSINNRVEKcifypsalntfeiratldahlkrhqmaadrl 182
Cdd:cd00106    76 GYNGTIFAYGQTGSGKTYTMLGPDPE-QRGIIPRALEDIFERIDKRKET------------------------------- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 183 stsreitdryceaiklsgyndDMVCSVFVTYVEIYNNYCYDLLEDARNgsrvlTKREIRHDRQQQMYVDGAKDVEVSSSE 262
Cdd:cd00106   124 ---------------------KSSFSVSASYLEIYNEKIYDLLSPVPK-----KPLSLREDPKRGVYVKGLTEVEVGSLE 177
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 263 EALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAPRayetksvypTMDSSQIIVSQLCLVDLAGSERAKRTQNVGE 342
Cdd:cd00106   178 DALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNR---------EKSGESVTSSKLNLVDLAGSERAKKTGAEGD 248
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 343 RLAEANSINQSLMTLRQCIEVLRRNQKSssqnleQVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYDENMSALAFA 422
Cdd:cd00106   249 RLKEGGNINKSLSALGKVISALADGQNK------HIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFA 322

                  .
gi 1734329465 423 E 423
Cdd:cd00106   323 S 323
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
28-429 3.90e-69

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: 230.56  E-value: 3.90e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  28 IEVVCRLCPY----TGSTPSLIAIDEGSIQTV-LPPAQFRRenapqveKVFRFGRVFSENDGQATVFERTSvDLILNLLK 102
Cdd:cd01366     4 IRVFCRVRPLlpseENEDTSHITFPDEDGQTIeLTSIGAKQ-------KEFSFDKVFDPEASQEDVFEEVS-PLVQSALD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 103 GQNSLLFTYGVTGSGKTYTMTGkpTETGTGLLPRTLDVIFNSINNRVEKcifypsalntfeiratldahlkrhqmaadrl 182
Cdd:cd01366    76 GYNVCIFAYGQTGSGKTYTMEG--PPESPGIIPRALQELFNTIKELKEK------------------------------- 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 183 stsreitdryceaiklsGYNDDMVCSvfvtYVEIYNNYCYDLLEDARNGSrvlTKREIRHDRQQQM-YVDGAKDVEVSSS 261
Cdd:cd01366   123 -----------------GWSYTIKAS----MLEIYNETIRDLLAPGNAPQ---KKLEIRHDSEKGDtTVTNLTEVKVSSP 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 262 EEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLvmapRAYETKSvyptmdsSQIIVSQLCLVDLAGSERAKRTQNVG 341
Cdd:cd01366   179 EEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI----SGRNLQT-------GEISVGKLNLVDLAGSERLNKSGATG 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 342 ERLAEANSINQSLMTLRQCIEVLRRNQKsssqnleQVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYDENMSALAF 421
Cdd:cd01366   248 DRLKETQAINKSLSALGDVISALRQKQS-------HIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRF 320

                  ....*...
gi 1734329465 422 AEESQTIE 429
Cdd:cd01366   321 ASKVNSCE 328
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
64-429 1.53e-63

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: 216.04  E-value: 1.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  64 ENAPQV----EKVFRFGRVFSENDGQATVFERTSVDLILNLLKGQNSLLFTYGVTGSGKTYTM-TGKPTETG---TGLLP 135
Cdd:cd01372    29 PGEPQVtvgtDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMgTAYTAEEDeeqVGIIP 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 136 RTLDVIFNSINNRVEKCIFypsalntfeiratldahlkrhqmaadrlstsreitdryceaiklsgynddmvcSVFVTYVE 215
Cdd:cd01372   109 RAIQHIFKKIEKKKDTFEF-----------------------------------------------------QLKVSFLE 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 216 IYNNYCYDLLEDARNGSRVLTkreIRHDRQQQMYVDGAKDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTI 295
Cdd:cd01372   136 IYNEEIRDLLDPETDKKPTIS---IREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTI 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 296 KLVMAPRAYETKSVYPTMDSSqIIVSQLCLVDLAGSERAKRTQNVGERLAEANSINQSLMTLRQCIEVLRRNQKSSSqnl 375
Cdd:cd01372   213 TLEQTKKNGPIAPMSADDKNS-TFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGA--- 288
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1734329465 376 eQVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYDENMSALAFAEESQTIE 429
Cdd:cd01372   289 -HVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
27-422 1.29e-61

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: 210.27  E-value: 1.29e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  27 SIEVVCRLCPytgSTPSLIAIDEGSIQTVLPPAQFRRENAPQVekvFRFGRVFSENDGQATVFERTSVDLILNLLKGQNS 106
Cdd:cd01374     1 KITVTVRVRP---LNSREIGINEQVAWEIDNDTIYLVEPPSTS---FTFDHVFGGDSTNREVYELIAKPVVKSALEGYNG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 107 LLFTYGVTGSGKTYTMTGkpTETGTGLLPRTLDVIFNSINNRVEKcifypsalnTFEIRatldahlkrhqmaadrlstsr 186
Cdd:cd01374    75 TIFAYGQTSSGKTFTMSG--DEDEPGIIPLAIRDIFSKIQDTPDR---------EFLLR--------------------- 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 187 eitdryceaiklsgynddmvcsvfVTYVEIYNNYCYDLLEDARNGSRvltkreIRHDRQQQMYVDGAKDVEVSSSEEALE 266
Cdd:cd01374   123 ------------------------VSYLEIYNEKINDLLSPTSQNLK------IRDDVEKGVYVAGLTEEIVSSPEHALS 172
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 267 VFCLGEERRRVSSTLLNKDSSRSHSVFTIKlvmapraYETKSVYPTMDSSqIIVSQLCLVDLAGSERAKRTQNVGERLAE 346
Cdd:cd01374   173 LIARGEKNRHVGETDMNERSSRSHTIFRIT-------IESSERGELEEGT-VRVSTLNLIDLAGSERAAQTGAAGVRRKE 244
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1734329465 347 ANSINQSLMTLRQCIevlrrNQKSSSQNLEQVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYDENMSALAFA 422
Cdd:cd01374   245 GSHINKSLLTLGTVI-----SKLSEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFA 315
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
26-434 3.68e-61

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: 210.29  E-value: 3.68e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  26 DSIEVVCRLCPYT------GSTPSLIAIDEGSIQTVLPPAQFRRENAPQVEKVFRFGRVFSENDG-------QATVFERT 92
Cdd:cd01365     1 ANVKVAVRVRPFNsrekerNSKCIVQMSGKETTLKNPKQADKNNKATREVPKSFSFDYSYWSHDSedpnyasQEQVYEDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  93 SVDLILNLLKGQNSLLFTYGVTGSGKTYTMTGKPTETGtgLLPRTLDVIFNSINNRVekcifypsalntfeiratldahl 172
Cdd:cd01365    81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPG--IIPRLCEDLFSRIADTT----------------------- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 173 krhqmaadrlstsreitdryceaiklsgyNDDMVCSVFVTYVEIYNNYCYDLLEDARNGSRVLTKreIRHDRQQQMYVDG 252
Cdd:cd01365   136 -----------------------------NQNMSYSVEVSYMEIYNEKVRDLLNPKPKKNKGNLK--VREHPVLGPYVED 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 253 AKDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIklVMAPRAYETksvypTMDSSQIIVSQLCLVDLAGSE 332
Cdd:cd01365   185 LSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTI--VLTQKRHDA-----ETNLTTEKVSKISLVDLAGSE 257
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 333 RAKRTQNVGERLAEANSINQSLMTLRQCIEVLRRNQKS-SSQNLEQVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDD 411
Cdd:cd01365   258 RASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGkSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADIN 337
                         410       420
                  ....*....|....*....|...
gi 1734329465 412 YDENMSALAFAEESQTIEVKKQV 434
Cdd:cd01365   338 YEETLSTLRYADRAKKIVNRAVV 360
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
70-428 1.12e-59

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: 205.66  E-value: 1.12e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  70 EKVFRFGRVFSENDGQATVFERTSVDLILNLLKGQNSLLFTYGVTGSGKTYTMTGkpTETGTGLLPRTLDVIFNSInnrv 149
Cdd:cd01370    60 ELKYVFDRVFDETSTQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLG--TPQEPGLMVLTMKELFKRI---- 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 150 ekcifypsalntfeiratldahlkrhqmaadrlstsreitdrycEAIKlsgynDDMVCSVFVTYVEIYNNYCYDLLEdar 229
Cdd:cd01370   134 --------------------------------------------ESLK-----DEKEFEVSMSYLEIYNETIRDLLN--- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 230 NGSRVLtkrEIRHDRQQQMYVDGAKDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAPRayeTKSV 309
Cdd:cd01370   162 PSSGPL---ELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDK---TASI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 310 YptmdsSQIIVSQLCLVDLAGSERAKRTQNVGERLAEANSINQSLMTLRQCIEVLrrnqKSSSQNLEQVPYRQSKLTHLF 389
Cdd:cd01370   236 N-----QQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINAL----ADPGKKNKHIPYRDSKLTRLL 306
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1734329465 390 KNYLEGNGKIRMVICVNPKPDDYDENMSALAFAEESQTI 428
Cdd:cd01370   307 KDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
26-428 3.91e-57

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: 198.45  E-value: 3.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  26 DSIEVVCRLCPYTG-----STPSLIAIDEGSIQ-TVLPPaqfrRENAPQVEKVFRFGRVFSENDGQATVFERTSVDLILN 99
Cdd:cd01371     1 ENVKVVVRCRPLNGkekaaGALQIVDVDEKRGQvSVRNP----KATANEPPKTFTFDAVFDPNSKQLDVYDETARPLVDS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 100 LLKGQNSLLFTYGVTGSGKTYTMTGKPTETGT-GLLPRTLDVIFNSINNRVEKCIFYpsalntfeiratldahlkrhqma 178
Cdd:cd01371    77 VLEGYNGTIFAYGQTGTGKTYTMEGKREDPELrGIIPNSFAHIFGHIARSQNNQQFL----------------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 179 adrlstsreitdryceaiklsgynddmvcsVFVTYVEIYNNYCYDLLedarnGSRVLTKREIRHDRQQQMYVDGAKDVEV 258
Cdd:cd01371   134 ------------------------------VRVSYLEIYNEEIRDLL-----GKDQTKRLELKERPDTGVYVKDLSMFVV 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 259 SSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAPRAYETKSVyptmdssqIIVSQLCLVDLAGSERAKRTQ 338
Cdd:cd01371   179 KNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENH--------IRVGKLNLVDLAGSERQSKTG 250
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 339 NVGERLAEANSINQSLMTLRQCIEVLRRNqKSSsqnleQVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYDENMSA 418
Cdd:cd01371   251 ATGERLKEATKINLSLSALGNVISALVDG-KST-----HIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLST 324
                         410
                  ....*....|
gi 1734329465 419 LAFAEESQTI 428
Cdd:cd01371   325 LRYANRAKNI 334
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
26-428 7.27e-57

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: 197.17  E-value: 7.27e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  26 DSIEVVCRLCPytgsTPSLIAIDEGSIQTVLPPAQFRRENAPQVEKVFRFGRVFSENDGQATVFERTSVDLILNLLKGQN 105
Cdd:cd01369     2 CNIKVVCRFRP----LNELEVLQGSKSIVKFDPEDTVVIATSETGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 106 SLLFTYGVTGSGKTYTMTGKP-TETGTGLLPRTLDVIFNSINNrvekcifypsalntfeiratLDAHLKRHqmaadrlst 184
Cdd:cd01369    78 GTIFAYGQTSSGKTYTMEGKLgDPESMGIIPRIVQDIFETIYS--------------------MDENLEFH--------- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 185 sreitdryceaiklsgynddmvcsVFVTYVEIYNNYCYDLLEDARngsrvlTKREIRHDRQQQMYVDGAKDVEVSSSEEA 264
Cdd:cd01369   129 ------------------------VKVSYFEIYMEKIRDLLDVSK------TNLSVHEDKNRGPYVKGATERFVSSPEEV 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 265 LEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAprayetksvypTMDSSQIIVSQLCLVDLAGSERAKRTQNVGERL 344
Cdd:cd01369   179 LDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE-----------NVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVL 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 345 AEANSINQSLMTLRQCIEVLRRNQKSSsqnleqVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYDENMSALAFAEE 424
Cdd:cd01369   248 DEAKKINKSLSALGNVINALTDGKKTH------IPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQR 321

                  ....
gi 1734329465 425 SQTI 428
Cdd:cd01369   322 AKTI 325
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
27-423 1.50e-56

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: 196.65  E-value: 1.50e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  27 SIEVVCRLCPYTGSTPSLIAIDE-GSIQTVLPPAQFRRE--NAPQVEKVFRFGRVFsENDGQATVFERTSVDLILNLLKG 103
Cdd:cd01375     1 KVQAFVRVRPTDDFAHEMIKYGEdGKSISIHLKKDLRRGvvNNQQEDWSFKFDGVL-HNASQELVYETVAKDVVSSALAG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 104 QNSLLFTYGVTGSGKTYTMTGKPTE-TGTGLLPRTLDVIFNSINNRVEKCIfypsalntfeiratldahlkrhqmaadrl 182
Cdd:cd01375    80 YNGTIFAYGQTGAGKTFTMTGGTENyKHRGIIPRALQQVFRMIEERPTKAY----------------------------- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 183 stsreitdryceaiklsgynddmvcSVFVTYVEIYNNYCYDLLEDARNGSRVLTKREIRHDRQQQMYVDGAKDVEVSSSE 262
Cdd:cd01375   131 -------------------------TVHVSYLEIYNEQLYDLLSTLPYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEE 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 263 EALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVMAPRayetksvypTMDSSQIIVSQLCLVDLAGSERAKRTQNVGE 342
Cdd:cd01375   186 EALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSR---------TLSSEKYITSKLNLVDLAGSERLSKTGVEGQ 256
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 343 RLAEANSINQSLMTLRQCIEVLrrnqksSSQNLEQVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYDENMSALAFA 422
Cdd:cd01375   257 VLKEATYINKSLSFLEQAIIAL------SDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFA 330

                  .
gi 1734329465 423 E 423
Cdd:cd01375   331 S 331
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
68-435 2.13e-55

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 199.97  E-value: 2.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  68 QVEKVFRFGRVFSENDGQATVFERTSVDLILNLLKGQNSLLFTYGVTGSGKTYTMTGkpTETGTGLLPRTLDVIFnsinn 147
Cdd:COG5059    53 SKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG--TEEEPGIIPLSLKELF----- 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 148 rvekcifypsalntfeiratldahlkrhqmaaDRLSTSREITDRyceAIKLSgynddmvcsvfvtYVEIYNNYCYDLLED 227
Cdd:COG5059   126 --------------------------------SKLEDLSMTKDF---AVSIS-------------YLEIYNEKIYDLLSP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 228 ARNGSRvltkreIRHDRQQQMYVDGAKDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIklvmaprayETK 307
Cdd:COG5059   158 NEESLN------IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQI---------ELA 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 308 SVYPTMDSSQIivSQLCLVDLAGSERAKRTQNVGERLAEANSINQSLMTLRQCIEVLRRNQKSSSqnleqVPYRQSKLTH 387
Cdd:COG5059   223 SKNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSGH-----IPYRESKLTR 295
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1734329465 388 LFKNYLEGNGKIRMVICVNPKPDDYDENMSALAFAEESQTIEVKKQVE 435
Cdd:COG5059   296 LLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN 343
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
26-431 1.14e-53

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: 189.26  E-value: 1.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  26 DSIEVVCRLCPytgstPSLIAIDEGSIQ--TVLPPAQFRRENAPqvEKVFRFGRVFSENDGQATVFERTSVDLILNLLKG 103
Cdd:cd01373     1 DAVKVFVRIRP-----PAEREGDGEYGQclKKLSSDTLVLHSKP--PKTFTFDHVADSNTNQESVFQSVGKPIVESCLSG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 104 QNSLLFTYGVTGSGKTYTMTGKPTETGT------GLLPRTLDVIFNSINNRVEKcifypsalntfeiratldahlkrhqm 177
Cdd:cd01373    74 YNGTIFAYGQTGSGKTYTMWGPSESDNEsphglrGVIPRIFEYLFSLIQREKEK-------------------------- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 178 aadrlstSREITDRYCEaiklsgynddmvCSvfvtYVEIYNNYCYDLLEDArngSRVLtkrEIRHDRQQQMYVDGAKDVE 257
Cdd:cd01373   128 -------AGEGKSFLCK------------CS----FLEIYNEQIYDLLDPA---SRNL---KLREDIKKGVYVENLVEEY 178
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 258 VSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLvmaprayetKSVYPTMDSSQIIVSQLCLVDLAGSERAKRT 337
Cdd:cd01373   179 VTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI---------ESWEKKACFVNIRTSRLNLVDLAGSERQKDT 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 338 QNVGERLAEANSINQSLMTLRQCIEVLRRNQKSSSqnlEQVPYRQSKLTHLFKNYLEGNGKIrMVIC-VNPKPDDYDENM 416
Cdd:cd01373   250 HAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQ---RHVCYRDSKLTFLLRDSLGGNAKT-AIIAnVHPSSKCFGETL 325
                         410
                  ....*....|....*
gi 1734329465 417 SALAFAEESQTIEVK 431
Cdd:cd01373   326 STLRFAQRAKLIKNK 340
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
28-426 2.25e-50

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: 179.24  E-value: 2.25e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  28 IEVVCRLCPYT------GSTPSLIAIDEGSIQTVLPPAQFRRENapqvekvFRFGRVFSENDGQATVFERTSVDLILNLL 101
Cdd:cd01376     2 VRVAVRVRPFVdgtagaSDPSCVSGIDSCSVELADPRNHGETLK-------YQFDAFYGEESTQEDIYAREVQPIVPHLL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 102 KGQNSLLFTYGVTGSGKTYTMTGKPTETGtgLLPRTLDvifnsinnrvekcifypsalntfeiratldahlkrhqmaaDR 181
Cdd:cd01376    75 EGQNATVFAYGSTGAGKTFTMLGSPEQPG--LMPLTVM----------------------------------------DL 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 182 LSTSREITDRYceaiklsgynddmvcSVFVTYVEIYNNYCYDLLEDARNgsrvltKREIRHDRQQQMYVDGAKDVEVSSS 261
Cdd:cd01376   113 LQMTRKEAWAL---------------SFTMSYLEIYQEKILDLLEPASK------ELVIREDKDGNILIPGLSSKPIKSM 171
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 262 EEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLVmaPRAYETKSVYPTmdssqiivSQLCLVDLAGSERAKRTQNVG 341
Cdd:cd01376   172 AEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVD--QRERLAPFRQRT--------GKLNLIDLAGSEDNRRTGNEG 241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 342 ERLAEANSINQSLMTLRQCIEVLRrnqksssQNLEQVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYDENMSALAF 421
Cdd:cd01376   242 IRLKESGAINSSLFVLSKVVNALN-------KNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNF 314

                  ....*
gi 1734329465 422 AEESQ 426
Cdd:cd01376   315 AARSR 319
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
65-434 2.39e-46

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: 169.04  E-value: 2.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  65 NAPQVEKVFRFGRVFSENDGQATVFERTSVDLILNLLKGQNSLLFTYGVTGSGKTYTMTGKPTETG---------TGLLP 135
Cdd:cd01364    43 ADKSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDRSPNEeytweldplAGIIP 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 136 RTLDVIFNsinnrvekcifypsalntfeiratldahlkrhqmaadrlstsreitdryceaiKLSGYNDDMvcSVFVTYVE 215
Cdd:cd01364   123 RTLHQLFE-----------------------------------------------------KLEDNGTEY--SVKVSYLE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 216 IYNNYCYDLLEDARNgsrvLTKREIRHD---RQQQMYVDGAKDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSV 292
Cdd:cd01364   148 IYNEELFDLLSPSSD----VSERLRMFDdprNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSV 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 293 FTIKLVMAPRAYETKSVYPtmdssqiiVSQLCLVDLAGSERAKRTQNVGERLAEANSINQSLMTLRQCIEVLrrNQKSSs 372
Cdd:cd01364   224 FSITIHIKETTIDGEELVK--------IGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL--VERAP- 292
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1734329465 373 qnleQVPYRQSKLTHLFKNYLEGNGKIRMVICVNPKPDDYDENMSALAFAEESQTIEVKKQV 434
Cdd:cd01364   293 ----HVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEV 350
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
4-422 2.39e-39

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: 148.60  E-value: 2.39e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465   4 RKRgitPSRDQVRRKKlsieETDSIEVVCRLCPYtgstpsliaIDEgsiqtvlppAQFRRENAPQVEK-VFRFGRVFSEN 82
Cdd:cd01367     7 RKR---PLNKKEVAKK----EIDVVSVPSKLTLI---------VHE---------PKLKVDLTKYIENhTFRFDYVFDES 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  83 DGQATVFERTSVDLILNLLKGQNSLLFTYGVTGSGKTYTMTGKptetgtgllprtldvifnsinnrvekcifYPSALNTF 162
Cdd:cd01367    62 SSNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGD-----------------------------FSGQEESK 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 163 EIratldahlkrHQMAAdrlstsREITDRyceaikLSGYNDDMVCSVFVTYVEIYNNYCYDLLEDArngsrvlTKREIRH 242
Cdd:cd01367   113 GI----------YALAA------RDVFRL------LNKLPYKDNLGVTVSFFEIYGGKVFDLLNRK-------KRVRLRE 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 243 DRQQQMYVDGAKDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIKLvmapRAYETksvyptmdssQIIVSQ 322
Cdd:cd01367   164 DGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL----RDRGT----------NKLHGK 229
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 323 LCLVDLAGSER-AKRTQNVGERLAEANSINQSLMTLRQCIEVLRRNQKsssqnleQVPYRQSKLTHLFKNYLEGN-GKIR 400
Cdd:cd01367   230 LSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKA-------HIPFRGSKLTQVLKDSFIGEnSKTC 302
                         410       420
                  ....*....|....*....|..
gi 1734329465 401 MVICVNPKPDDYDENMSALAFA 422
Cdd:cd01367   303 MIATISPGASSCEHTLNTLRYA 324
PLN03188 PLN03188
kinesin-12 family protein; Provisional
70-465 2.15e-35

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 145.08  E-value: 2.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465   70 EKVFRFGRVFSENDGQATVFERTSVDLILNLLKGQNSLLFTYGVTGSGKTYTMTGKptetGTGLLPRTLDVIFNSINNRV 149
Cdd:PLN03188   131 GQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGP----ANGLLEEHLSGDQQGLTPRV 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  150 EKCIFypSALNTFEIRATlDAHLKRHqmaadrlstsreitdryCEaiklsgynddmvCSvfvtYVEIYNNYCYDLLEDA- 228
Cdd:PLN03188   207 FERLF--ARINEEQIKHA-DRQLKYQ-----------------CR------------CS----FLEIYNEQITDLLDPSq 250
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  229 RNgsrvltkREIRHDRQQQMYVDGAKDVEVSSSEEALEVFCLGEERRRVSSTLLNKDSSRSHSVFTIklVMAPRAyetKS 308
Cdd:PLN03188   251 KN-------LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC--VVESRC---KS 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  309 VYPTMDSSQiiVSQLCLVDLAGSERAKRTQNVGERLAEANSINQSLMTLRQCIEVLRRNQKSSSQnlEQVPYRQSKLTHL 388
Cdd:PLN03188   319 VADGLSSFK--TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQ--RHIPYRDSRLTFL 394
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1734329465  389 FKNYLEGNGKIRMVICVNPKPDDYDENMSALAFAEESQTIEVKKQVERMPSERIPH--SFFTQWNSELDgsvRMEDDGS 465
Cdd:PLN03188   395 LQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDDVNFlrEVIRQLRDELQ---RVKANGN 470
MKLP1_Arf_bdg pfam16540
Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region ...
673-749 1.24e-25

Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region of mitotic kinesin-like proteins that is necessary for the interaction with the small GTPase Arf6. MKLP1 is a Flemming body-localising protein essential for cytokinesis, so its interaction with Arf6 shows how Arf6 is involved in cytokinesis. The Arf6-MKLP1 complex plays a crucial role in cytokinesis by connecting the microtubule bundle and membranes at the cleavage plane.


Pssm-ID: 465166  Cd Length: 107  Bit Score: 101.62  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465 673 YVNPKYqRRSKSA-SRLLDHQPLHRVPTGTVLQSRTPA--NAIRTTKPEMHQLNKSGEYRLTHQEVDDEGNISTNIVKVN 749
Cdd:pfam16540   2 VVNPRH-RRSRSAgERWLDHKPPSNVPTGTILQPRIPNrkSVTKLTKPKDKALAKASKYCLTHQEQDSDGEIETKLYKGD 80
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
70-157 2.29e-07

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: 51.19  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  70 EKVFRFGRVFSENDGQATVFeRTSVDLILNLLKGQNSL-LFTYGVTGSGKTYTMtgkptetgTGLLPRTLDVIFNSINNR 148
Cdd:cd01363    17 SKIIVFYRGFRRSESQPHVF-AIADPAYQSMLDGYNNQsIFAYGESGAGKTETM--------KGVIPYLASVAFNGINKG 87

                  ....*....
gi 1734329465 149 VEKCIFYPS 157
Cdd:cd01363    88 ETEGWVYLT 96
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
12-145 3.51e-07

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 50.30  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734329465  12 RDQVRRKKL--SIEETD-SIEVVCRLCPYTGSTPSLIAIDEGSIQTvlppaQFRRENapqveKVFRFGRVFSENDGQATV 88
Cdd:pfam16796   3 EEETLRRKLenSIQELKgNIRVFARVRPELLSEAQIDYPDETSSDG-----KIGSKN-----KSFSFDRVFPPESEQEDV 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1734329465  89 FERTSVdLILNLLKGQNSLLFTYGVTGSGKTytmtgkptetgTGLLPRTLDVIFNSI 145
Cdd:pfam16796  73 FQEISQ-LVQSCLDGYNVCIFAYGQTGSGSN-----------DGMIPRAREQIFRFI 117
 
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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