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Conserved domains on  [gi|23491102|gb|EAA22720|]
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kinesin-like protein K6 [Plasmodium yoelii yoelii]

Protein Classification

kinesin family protein( domain architecture ID 10102678)

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; such as KIF2, a plus end-directed microtubule-dependent motor expressed in neurons that has been associated with axonal transport, neuron development, and lysosomal translocation (splice variants)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
17-345 0e+00

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: 545.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  17 KIKVVVRKRPINENEKRKKDSDIVTVKDNHTICIDEPRYKVDMTKYIERHEFIVDKVFDETVDNLTVYQYSIKPLIIDIF 96
Cdd:cd01367   1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKVDLTKYIENHTFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  97 ENnCVCSCFAYGQTGSGKTYTMLGSQPyGQSNCPGIFQYASEDIFNFLNTYNNDNSKGIFISFYEIYCGKLYDLLQKRKM 176
Cdd:cd01367  81 EG-GKATCFAYGQTGSGKTYTMGGDFS-GQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLNRKKR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 177 VAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDINKNISLGKIAFIDLAGS 256
Cdd:cd01367 159 VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNKLHGKLSFVDLAGS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 257 ERGADTIAQNKQTQTDGANINRSLLALKECIRAMDSDKNHIPFRDSELTKVLRDIFVG-KSKSIMIANISPTISSCEQTL 335
Cdd:cd01367 239 ERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGeNSKTCMIATISPGASSCEHTL 318
                       330
                ....*....|
gi 23491102 336 NTLRYSSRVK 345
Cdd:cd01367 319 NTLRYADRVK 328
 
Name Accession Description Interval E-value
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
17-345 0e+00

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: 545.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  17 KIKVVVRKRPINENEKRKKDSDIVTVKDNHTICIDEPRYKVDMTKYIERHEFIVDKVFDETVDNLTVYQYSIKPLIIDIF 96
Cdd:cd01367   1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKVDLTKYIENHTFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  97 ENnCVCSCFAYGQTGSGKTYTMLGSQPyGQSNCPGIFQYASEDIFNFLNTYNNDNSKGIFISFYEIYCGKLYDLLQKRKM 176
Cdd:cd01367  81 EG-GKATCFAYGQTGSGKTYTMGGDFS-GQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLNRKKR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 177 VAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDINKNISLGKIAFIDLAGS 256
Cdd:cd01367 159 VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNKLHGKLSFVDLAGS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 257 ERGADTIAQNKQTQTDGANINRSLLALKECIRAMDSDKNHIPFRDSELTKVLRDIFVG-KSKSIMIANISPTISSCEQTL 335
Cdd:cd01367 239 ERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGeNSKTCMIATISPGASSCEHTL 318
                       330
                ....*....|
gi 23491102 336 NTLRYSSRVK 345
Cdd:cd01367 319 NTLRYADRVK 328
Kinesin pfam00225
Kinesin motor domain;
23-346 1.08e-96

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 308.35  E-value: 1.08e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102    23 RKRPINENEKRKKDSDIVTVKDNHTICIDepryKVDMTKYIERHEFIVDKVFDETVDNLTVYQYSIKPLIIDIFENNCVC 102
Cdd:pfam00225   1 RVRPLNEREKERGSSVIVSVESVDSETVE----SSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102   103 sCFAYGQTGSGKTYTMLGSqpygqSNCPGIFQYASEDIFNFLNTYNNDNSKGIFISFYEIYCGKLYDLLQKRK----MVA 178
Cdd:pfam00225  77 -IFAYGQTGSGKTYTMEGS-----DEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNknkrKLR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102   179 ALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLK------DINKNISLGKIAFID 252
Cdd:pfam00225 151 IREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEqrnrstGGEESVKTGKLNLVD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102   253 LAGSERGADTIAQNKQTQTDGANINRSLLALKECIRAM-DSDKNHIPFRDSELTKVLRDIFVGKSKSIMIANISPTISSC 331
Cdd:pfam00225 231 LAGSERASKTGAAGGQRLKEAANINKSLSALGNVISALaDKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNY 310
                         330
                  ....*....|....*
gi 23491102   332 EQTLNTLRYSSRVKN 346
Cdd:pfam00225 311 EETLSTLRFASRAKN 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
18-354 3.56e-93

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: 299.10  E-value: 3.56e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102     18 IKVVVRKRPINENEKRKKDSDIVTVKDNH--TICIDEPrykvdmTKYIERHEFIVDKVFDETVDNLTVYQYSIKPLIIDI 95
Cdd:smart00129   2 IRVVVRVRPLNKREKSRKSPSVVPFPDKVgkTLTVRSP------KNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102     96 FE--NncvCSCFAYGQTGSGKTYTMLGSqpygqSNCPGIFQYASEDIFNFLNTYNNDNSKGIFISFYEIYCGKLYDLLQK 173
Cdd:smart00129  76 LEgyN---ATIFAYGQTGSGKTYTMIGT-----PDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNP 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102    174 RKM-VAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDINKN-----ISLGK 247
Cdd:smart00129 148 SSKkLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNsssgsGKASK 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102    248 IAFIDLAGSERGADTIAqNKQTQTDGANINRSLLALKECIRA--MDSDKNHIPFRDSELTKVLRDIFVGKSKSIMIANIS 325
Cdd:smart00129 228 LNLVDLAGSERAKKTGA-EGDRLKEAGNINKSLSALGNVINAlaQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVS 306
                          330       340
                   ....*....|....*....|....*....
gi 23491102    326 PTISSCEQTLNTLRYSSRVKNFKTKPMLN 354
Cdd:smart00129 307 PSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
23-547 5.53e-48

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 180.71  E-value: 5.53e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  23 RKRPINENEKRKKDSDIVTVKDNHTICIDEPRYKVDMT-KYIERHEFIVDKVFDETVDNLTVYQYSIKPLIIDIFENNcV 101
Cdd:COG5059  12 RLSSRNEKSVSDIKSTIRIIPGELGERLINTSKKSHVSlEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGY-N 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 102 CSCFAYGQTGSGKTYTMLGSQpygqsNCPGIFQYASEDIFNFLNTYNNDNSKGIFISFYEIYCGKLYDLLQKRKMVA-AL 180
Cdd:COG5059  91 CTVFAYGQTGSGKTYTMSGTE-----EEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLSPNEESLnIR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 181 ENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDINKN---ISLGKIAFIDLAGSE 257
Cdd:COG5059 166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVsgtSETSKLSLVDLAGSE 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 258 RGADTIAQNKQTQtDGANINRSLLALKECIRA--MDSDKNHIPFRDSELTKVLRDIFVGKSKSIMIANISPTISSCEQTL 335
Cdd:COG5059 246 RAARTGNRGTRLK-EGASINKSLLTLGNVINAlgDKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETI 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 336 NTLRYSSRVKNFKTKPMLNDGEDTaNDPNNSIHTMSYYKSSELNYSSTENFTMKSNSLLSSkpetksiEFRDKNNEKSNK 415
Cdd:COG5059 325 NTLKFASRAKSIKNKIQVNSSSDS-SREIEEIKFDLSEDRSEIEILVFREQSQLSQSSLSG-------IFAYMQSLKKET 396
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 416 KMQKNvcdKND--NKNIKHSNKNRINTIKKNNTISRKNYTFSDTSDFSSLDEMNYNLNNSEKTLFTNSKSLNQQKLKSRN 493
Cdd:COG5059 397 ETLKS---RIDliMKSIISGTFERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....
gi 23491102 494 SCDTINSKVKKNDIQVLRHSVGSKLTNFSYEKNKSKEIEFSKNTVNQSKNILFN 547
Cdd:COG5059 474 IPEETSDRVESEKASKLRSSASTKLNLRSSRSHSKFRDHLNGSNSSTKELSLNQ 527
PLN03188 PLN03188
kinesin-12 family protein; Provisional
14-355 2.70e-33

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 139.68  E-value: 2.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102    14 SNGKIKVVVRKRPINENEKRKKdsdIVTVKDNHTICIDEprykvdmtkyierHEFIVDKVFDETVDNLTVYQYSIKPLIi 93
Cdd:PLN03188   96 SDSGVKVIVRMKPLNKGEEGEM---IVQKMSNDSLTING-------------QTFTFDSIADPESTQEDIFQLVGAPLV- 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102    94 difeNNCVC----SCFAYGQTGSGKTYTMLG-----SQPYGQSNCPGIFQYASEDIFNFLNTYNNDNSKGIF-----ISF 159
Cdd:PLN03188  159 ----ENCLAgfnsSVFAYGQTGSGKTYTMWGpanglLEEHLSGDQQGLTPRVFERLFARINEEQIKHADRQLkyqcrCSF 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102   160 YEIYCGKLYDLL---QKRKMVAalENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDL 236
Cdd:PLN03188  235 LEIYNEQITDLLdpsQKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102   237 KDINKNISLG-------KIAFIDLAGSERGADTIAQNKQTQTDGaNINRSLLALKECIRAM-----DSDKNHIPFRDSEL 304
Cdd:PLN03188  313 ESRCKSVADGlssfktsRINLVDLAGSERQKLTGAAGDRLKEAG-NINRSLSQLGNLINILaeisqTGKQRHIPYRDSRL 391
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 23491102   305 TKVLRDIFVGKSKSIMIANISPTISSCEQTLNTLRYSSRVKNFKTKPMLND 355
Cdd:PLN03188  392 TFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNE 442
 
Name Accession Description Interval E-value
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
17-345 0e+00

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: 545.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  17 KIKVVVRKRPINENEKRKKDSDIVTVKDNHTICIDEPRYKVDMTKYIERHEFIVDKVFDETVDNLTVYQYSIKPLIIDIF 96
Cdd:cd01367   1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKVDLTKYIENHTFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  97 ENnCVCSCFAYGQTGSGKTYTMLGSQPyGQSNCPGIFQYASEDIFNFLNTYNNDNSKGIFISFYEIYCGKLYDLLQKRKM 176
Cdd:cd01367  81 EG-GKATCFAYGQTGSGKTYTMGGDFS-GQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLNRKKR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 177 VAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDINKNISLGKIAFIDLAGS 256
Cdd:cd01367 159 VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNKLHGKLSFVDLAGS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 257 ERGADTIAQNKQTQTDGANINRSLLALKECIRAMDSDKNHIPFRDSELTKVLRDIFVG-KSKSIMIANISPTISSCEQTL 335
Cdd:cd01367 239 ERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGeNSKTCMIATISPGASSCEHTL 318
                       330
                ....*....|
gi 23491102 336 NTLRYSSRVK 345
Cdd:cd01367 319 NTLRYADRVK 328
Kinesin pfam00225
Kinesin motor domain;
23-346 1.08e-96

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 308.35  E-value: 1.08e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102    23 RKRPINENEKRKKDSDIVTVKDNHTICIDepryKVDMTKYIERHEFIVDKVFDETVDNLTVYQYSIKPLIIDIFENNCVC 102
Cdd:pfam00225   1 RVRPLNEREKERGSSVIVSVESVDSETVE----SSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102   103 sCFAYGQTGSGKTYTMLGSqpygqSNCPGIFQYASEDIFNFLNTYNNDNSKGIFISFYEIYCGKLYDLLQKRK----MVA 178
Cdd:pfam00225  77 -IFAYGQTGSGKTYTMEGS-----DEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNknkrKLR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102   179 ALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLK------DINKNISLGKIAFID 252
Cdd:pfam00225 151 IREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEqrnrstGGEESVKTGKLNLVD 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102   253 LAGSERGADTIAQNKQTQTDGANINRSLLALKECIRAM-DSDKNHIPFRDSELTKVLRDIFVGKSKSIMIANISPTISSC 331
Cdd:pfam00225 231 LAGSERASKTGAAGGQRLKEAANINKSLSALGNVISALaDKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNY 310
                         330
                  ....*....|....*
gi 23491102   332 EQTLNTLRYSSRVKN 346
Cdd:pfam00225 311 EETLSTLRFASRAKN 325
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
17-345 9.33e-95

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: 303.02  E-value: 9.33e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  17 KIKVVVRKRPINENEKRKkDSDIVTVKDNHTICIDEPrykvdMTKYIERHEFIVDKVFDETVDNLTVYQYSIKPLIIDIF 96
Cdd:cd00106   1 NVRVAVRVRPLNGREARS-AKSVISVDGGKSVVLDPP-----KNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSAL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  97 ENNCVCsCFAYGQTGSGKTYTMLGSQPygqsNCPGIFQYASEDIFNFLNTYNNDNSK-GIFISFYEIYCGKLYDLLQ--K 173
Cdd:cd00106  75 EGYNGT-IFAYGQTGSGKTYTMLGPDP----EQRGIIPRALEDIFERIDKRKETKSSfSVSASYLEIYNEKIYDLLSpvP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 174 RKMVAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDINKNISL-----GKI 248
Cdd:cd00106 150 KKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGesvtsSKL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 249 AFIDLAGSERGADTIAQnKQTQTDGANINRSLLALKECIRAM-DSDKNHIPFRDSELTKVLRDIFVGKSKSIMIANISPT 327
Cdd:cd00106 230 NLVDLAGSERAKKTGAE-GDRLKEGGNINKSLSALGKVISALaDGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPS 308
                       330
                ....*....|....*...
gi 23491102 328 ISSCEQTLNTLRYSSRVK 345
Cdd:cd00106 309 SENFEETLSTLRFASRAK 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
18-354 3.56e-93

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: 299.10  E-value: 3.56e-93
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102     18 IKVVVRKRPINENEKRKKDSDIVTVKDNH--TICIDEPrykvdmTKYIERHEFIVDKVFDETVDNLTVYQYSIKPLIIDI 95
Cdd:smart00129   2 IRVVVRVRPLNKREKSRKSPSVVPFPDKVgkTLTVRSP------KNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102     96 FE--NncvCSCFAYGQTGSGKTYTMLGSqpygqSNCPGIFQYASEDIFNFLNTYNNDNSKGIFISFYEIYCGKLYDLLQK 173
Cdd:smart00129  76 LEgyN---ATIFAYGQTGSGKTYTMIGT-----PDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNP 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102    174 RKM-VAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDINKN-----ISLGK 247
Cdd:smart00129 148 SSKkLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNsssgsGKASK 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102    248 IAFIDLAGSERGADTIAqNKQTQTDGANINRSLLALKECIRA--MDSDKNHIPFRDSELTKVLRDIFVGKSKSIMIANIS 325
Cdd:smart00129 228 LNLVDLAGSERAKKTGA-EGDRLKEAGNINKSLSALGNVINAlaQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVS 306
                          330       340
                   ....*....|....*....|....*....
gi 23491102    326 PTISSCEQTLNTLRYSSRVKNFKTKPMLN 354
Cdd:smart00129 307 PSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
18-346 2.39e-72

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: 243.41  E-value: 2.39e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  18 IKVVVRKRPINENEKRKKDSDIVTVKDNHTICIDEP-------RYKVDMTKYIERH----EFIVDKVFDETVDNLTVYQY 86
Cdd:cd01370   2 LTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKdeedgffHGGSNNRDRRKRRnkelKYVFDRVFDETSTQEEVYEE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  87 SIKPLIIDIFeNNCVCSCFAYGQTGSGKTYTMLGSqpygqSNCPGIFQYASEDIFNFLNTYNNDNSKGIFISFYEIYCGK 166
Cdd:cd01370  82 TTKPLVDGVL-NGYNATVFAYGATGAGKTHTMLGT-----PQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNET 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 167 LYDLLQKRKMVAAL-ENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLK------DI 239
Cdd:cd01370 156 IRDLLNPSSGPLELrEDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRqqdktaSI 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 240 NKNISLGKIAFIDLAGSERGADTIAQNKQTQtDGANINRSLLALKECIRAM---DSDKNHIPFRDSELTKVLRDIFVGKS 316
Cdd:cd01370 236 NQQVRQGKLSLIDLAGSERASATNNRGQRLK-EGANINRSLLALGNCINALadpGKKNKHIPYRDSKLTRLLKDSLGGNC 314
                       330       340       350
                ....*....|....*....|....*....|
gi 23491102 317 KSIMIANISPTISSCEQTLNTLRYSSRVKN 346
Cdd:cd01370 315 RTVMIANISPSSSSYEETHNTLKYANRAKN 344
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
18-346 7.36e-65

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: 222.34  E-value: 7.36e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  18 IKVVVRKRPINENEKRKKDSDIVTV-KDNHTICIDEPRYkvdmtkyiERHE----FIVDKVFDETVDNLTVYQYSIKPLI 92
Cdd:cd01371   3 VKVVVRCRPLNGKEKAAGALQIVDVdEKRGQVSVRNPKA--------TANEppktFTFDAVFDPNSKQLDVYDETARPLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  93 IDIFE--NNCVcscFAYGQTGSGKTYTMLGSQpyGQSNCPGIFQYASEDIFNFLNTYNNDNSKGIFISFYEIYCGKLYDL 170
Cdd:cd01371  75 DSVLEgyNGTI---FAYGQTGTGKTYTMEGKR--EDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 171 LQK--RKMVAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLK------DINKN 242
Cdd:cd01371 150 LGKdqTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIEcsekgeDGENH 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 243 ISLGKIAFIDLAGSERGADTIAQNkQTQTDGANINRSLLALKECIRAM-DSDKNHIPFRDSELTKVLRDIFVGKSKSIMI 321
Cdd:cd01371 230 IRVGKLNLVDLAGSERQSKTGATG-ERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMC 308
                       330       340
                ....*....|....*....|....*
gi 23491102 322 ANISPTISSCEQTLNTLRYSSRVKN 346
Cdd:cd01371 309 ANIGPADYNYDETLSTLRYANRAKN 333
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
17-346 1.08e-62

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: 215.66  E-value: 1.08e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  17 KIKVVVRKRPINENEKRKKDSDIVTVKDNHTICIDEPRYKvdmtkyierHEFIVDKVFDETVDNLTVYQYSIKPLIIDIF 96
Cdd:cd01369   3 NIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSETG---------KTFSFDRVFDPNTTQEDVYNFAAKPIVDDVL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  97 eNNCVCSCFAYGQTGSGKTYTMLGsqPYGQSNCPGIFQYASEDIFNFLNTYNNDNSKGIFISFYEIYCGKLYDLLQ-KRK 175
Cdd:cd01369  74 -NGYNGTIFAYGQTSSGKTYTMEG--KLGDPESMGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDvSKT 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 176 MVAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDIN---KNISLGKIAFID 252
Cdd:cd01369 151 NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENvetEKKKSGKLYLVD 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 253 LAGSERGADTIAQNkQTQTDGANINRSLLALKECIRAM-DSDKNHIPFRDSELTKVLRDIFVGKSKSIMIANISPTISSC 331
Cdd:cd01369 231 LAGSEKVSKTGAEG-AVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNE 309
                       330
                ....*....|....*
gi 23491102 332 EQTLNTLRYSSRVKN 346
Cdd:cd01369 310 SETLSTLRFGQRAKT 324
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
16-354 1.24e-62

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: 216.84  E-value: 1.24e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  16 GKIKVVVRKRPINENEKRKKDSDIVTVKDNHTICIDEPRYKVDMTKYIER-HEFIVDKVFDET-------VDNLTVYQYS 87
Cdd:cd01365   1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQADKNNKATREVpKSFSFDYSYWSHdsedpnyASQEQVYEDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  88 IKPLIIDIFE--NNCVcscFAYGQTGSGKTYTMLGSQpygqsNCPGIFQYASEDIFNFLNTYNNDNSK-GIFISFYEIYC 164
Cdd:cd01365  81 GEELLQHAFEgyNVCL---FAYGQTGSGKSYTMMGTQ-----EQPGIIPRLCEDLFSRIADTTNQNMSySVEVSYMEIYN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 165 GKLYDLLQKRKM-----VAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLK-- 237
Cdd:cd01365 153 EKVRDLLNPKPKknkgnLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTqk 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 238 --DINKNISLGK---IAFIDLAGSERGADTIAqNKQTQTDGANINRSLLALKECIRAMDSDKNH--------IPFRDSEL 304
Cdd:cd01365 233 rhDAETNLTTEKvskISLVDLAGSERASSTGA-TGDRLKEGANINKSLTTLGKVISALADMSSGkskkkssfIPYRDSVL 311
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 23491102 305 TKVLRDIFVGKSKSIMIANISPTISSCEQTLNTLRYSSRVKNFKTKPMLN 354
Cdd:cd01365 312 TWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
15-346 5.68e-61

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: 210.91  E-value: 5.68e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  15 NGKIKVVVRKRPINENEKRKKDSDIVTVkdnhticiDEPRYKVDMT-KYIERHEFIVDKVFDETVDNLTVYQySIKPLII 93
Cdd:cd01366   1 KGNIRVFCRVRPLLPSEENEDTSHITFP--------DEDGQTIELTsIGAKQKEFSFDKVFDPEASQEDVFE-EVSPLVQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  94 DIFENNCVCsCFAYGQTGSGKTYTMlgsqpYGQSNCPGIFQYASEDIFNFLNTynnDNSKG----IFISFYEIYCGKLYD 169
Cdd:cd01366  72 SALDGYNVC-IFAYGQTGSGKTYTM-----EGPPESPGIIPRALQELFNTIKE---LKEKGwsytIKASMLEIYNETIRD 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 170 LL-----QKRKMVAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDIN---K 241
Cdd:cd01366 143 LLapgnaPQKKLEIRHDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNlqtG 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 242 NISLGKIAFIDLAGSERGADTIAQN---KQTQtdgaNINRSLLALKECIRAMDSDKNHIPFRDSELTKVLRDIFVGKSKS 318
Cdd:cd01366 223 EISVGKLNLVDLAGSERLNKSGATGdrlKETQ----AINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKT 298
                       330       340
                ....*....|....*....|....*...
gi 23491102 319 IMIANISPTISSCEQTLNTLRYSSRVKN 346
Cdd:cd01366 299 LMFVNISPAESNLNETLNSLRFASKVNS 326
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
18-354 3.34e-59

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: 206.79  E-value: 3.34e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  18 IKVVVRKRPINENEKRKKDSDIVTVKD-NHTICIdepRYKVDMTKYIERhEFIVDKVFDETVDNLTVYQYSIKPlIIDIF 96
Cdd:cd01364   4 IQVVVRCRPFNLRERKASSHSVVEVDPvRKEVSV---RTGGLADKSSTK-TYTFDMVFGPEAKQIDVYRSVVCP-ILDEV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  97 ENNCVCSCFAYGQTGSGKTYTMLGSQ-PYGQSNCP-----GIFQYASEDIFNFLNTYNNDNSkgIFISFYEIYCGKLYDL 170
Cdd:cd01364  79 LMGYNCTIFAYGQTGTGKTYTMEGDRsPNEEYTWEldplaGIIPRTLHQLFEKLEDNGTEYS--VKVSYLEIYNEELFDL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 171 L------QKRKMVAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDINKNIS 244
Cdd:cd01364 157 LspssdvSERLRMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTID 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 245 ------LGKIAFIDLAGSERGADTIAQNKQTQTDGaNINRSLLALKECIRAMDSDKNHIPFRDSELTKVLRDIFVGKSKS 318
Cdd:cd01364 237 geelvkIGKLNLVDLAGSENIGRSGAVDKRAREAG-NINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKT 315
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 23491102 319 IMIANISPTISSCEQTLNTLRYSSRVKNFKTKPMLN 354
Cdd:cd01364 316 SIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
17-346 1.25e-58

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: 204.10  E-value: 1.25e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  17 KIKVVVRKRPINENEKRKKDSDIVTVkDNHTIcIDEPRYKVdmtkyierhEFIVDKVFDETVDNLTVYQYSIKPlIIDIF 96
Cdd:cd01374   1 KITVTVRVRPLNSREIGINEQVAWEI-DNDTI-YLVEPPST---------SFTFDHVFGGDSTNREVYELIAKP-VVKSA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  97 ENNCVCSCFAYGQTGSGKTYTMLGSQPYgqsncPGIFQYASEDIFNFLNTYNNDNSKgIFISFYEIYCGKLYDLL----Q 172
Cdd:cd01374  69 LEGYNGTIFAYGQTSSGKTFTMSGDEDE-----PGIIPLAIRDIFSKIQDTPDREFL-LRVSYLEIYNEKINDLLsptsQ 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 173 KRKMVaalENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDINKNISLGK----- 247
Cdd:cd01374 143 NLKIR---DDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGtvrvs 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 248 -IAFIDLAGSERGADTIAQNKQTQtDGANINRSLLALKECIRAMDSDK--NHIPFRDSELTKVLRDIFVGKSKSIMIANI 324
Cdd:cd01374 220 tLNLIDLAGSERAAQTGAAGVRRK-EGSHINKSLLTLGTVISKLSEGKvgGHIPYRDSKLTRILQPSLGGNSRTAIICTI 298
                       330       340
                ....*....|....*....|..
gi 23491102 325 SPTISSCEQTLNTLRYSSRVKN 346
Cdd:cd01374 299 TPAESHVEETLNTLKFASRAKK 320
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
18-348 3.74e-55

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: 195.24  E-value: 3.74e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  18 IKVVVRKRPINENEKRKKDSDIVTVKDNhticidEPRYKVDmtkyiERHEFIVDKVFDETVDNLTVYQYSIKPLIIDIFE 97
Cdd:cd01372   3 VRVAVRVRPLLPKEIIEGCRICVSFVPG------EPQVTVG-----TDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  98 --NncvCSCFAYGQTGSGKTYTMLGSQPyGQSNCP--GIFQYASEDIFNFLNTYNNDNSKGIFISFYEIYCGKLYDLL-- 171
Cdd:cd01372  72 gyN---ATVLAYGQTGSGKTYTMGTAYT-AEEDEEqvGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLdp 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 172 --QKRKMVAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDL------------K 237
Cdd:cd01372 148 etDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqtkkngpiapmS 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 238 DINKNISL-GKIAFIDLAGSERGADTIAQNKQTQtDGANINRSLLALKECIRAMDSDK---NHIPFRDSELTKVLRDIFV 313
Cdd:cd01372 228 ADDKNSTFtSKFHFVDLAGSERLKRTGATGDRLK-EGISINSGLLALGNVISALGDESkkgAHVPYRDSKLTRLLQDSLG 306
                       330       340       350
                ....*....|....*....|....*....|....*
gi 23491102 314 GKSKSIMIANISPTISSCEQTLNTLRYSSRVKNFK 348
Cdd:cd01372 307 GNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
17-341 1.93e-51

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: 184.52  E-value: 1.93e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  17 KIKVVVRKRPINENEKRKKDSDIVTVKDNHTICIDEPR----YKVDMTKYIERHEFIVDKVFDETVDNLTVYQYSIKPLI 92
Cdd:cd01368   2 PVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKgsaaNKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  93 IDIF--ENNCVcscFAYGQTGSGKTYTMLGSqpygqSNCPGIFQYASEDIFNFLNTYnndnskGIFISFYEIYCGKLYDL 170
Cdd:cd01368  82 QDLLhgKNGLL---FTYGVTNSGKTYTMQGS-----PGDGGILPRSLDVIFNSIGGY------SVFVSYIEIYNEYIYDL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 171 L--------QKRKMVAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNI-------- 234
Cdd:cd01368 148 LepspssptKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIklvqapgd 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 235 ---DLKDINKNISLGKIAFIDLAGSERGADTIAQNKQTQtDGANINRSLLALKECIRA-----MDSDKNHIPFRDSELTK 306
Cdd:cd01368 228 sdgDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLK-EAGNINTSLMTLGTCIEVlrenqLQGTNKMVPFRDSKLTH 306
                       330       340       350
                ....*....|....*....|....*....|....*
gi 23491102 307 VLRDIFVGKSKSIMIANISPTISSCEQTLNTLRYS 341
Cdd:cd01368 307 LFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
18-345 8.26e-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: 8.26e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  18 IKVVVRKRPINENEKRKKDSDIVTVKDNHTICIDEPRYKVDMTKYierhEFivDKVFDETVDNLTVYQYSIKPLIIDIFE 97
Cdd:cd01376   2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPRNHGETLKY----QF--DAFYGEESTQEDIYAREVQPIVPHLLE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  98 NNCVcSCFAYGQTGSGKTYTMLGSQpygqsNCPGIFQYASEDIFNFlnTYNNDNSKGIFISFYEIYCGKLYDLLQ-KRKM 176
Cdd:cd01376  76 GQNA-TVFAYGSTGAGKTFTMLGSP-----EQPGLMPLTVMDLLQM--TRKEAWALSFTMSYLEIYQEKILDLLEpASKE 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 177 VAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDINKNISL----GKIAFID 252
Cdd:cd01376 148 LVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFrqrtGKLNLID 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 253 LAGSERGADTIAQNKQTQTDGAnINRSLLALKECIRAMDSDKNHIPFRDSELTKVLRDIFVGKSKSIMIANISPTISSCE 332
Cdd:cd01376 228 LAGSEDNRRTGNEGIRLKESGA-INSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQ 306
                       330
                ....*....|...
gi 23491102 333 QTLNTLRYSSRVK 345
Cdd:cd01376 307 DTLSTLNFAARSR 319
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
18-359 2.22e-48

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: 175.77  E-value: 2.22e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  18 IKVVVRKRPINENEKRKKDSDIVTVKDNHTI-CIDEPrykvdmtkyiERHeFIVDKVFDETVDNLTVYQYSIKPLIIDIF 96
Cdd:cd01373   3 VKVFVRIRPPAEREGDGEYGQCLKKLSSDTLvLHSKP----------PKT-FTFDHVADSNTNQESVFQSVGKPIVESCL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  97 E--NNCVcscFAYGQTGSGKTYTMLG------SQPYG-QSNCPGIFQYasedIFNFLNTYNNDNSKGIFI----SFYEIY 163
Cdd:cd01373  72 SgyNGTI---FAYGQTGSGKTYTMWGpsesdnESPHGlRGVIPRIFEY----LFSLIQREKEKAGEGKSFlckcSFLEIY 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 164 CGKLYDLL-QKRKMVAALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDINK- 241
Cdd:cd01373 145 NEQIYDLLdPASRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKk 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 242 ----NISLGKIAFIDLAGSERGADTIAQnKQTQTDGANINRSLLALKECIRAM----DSDKNHIPFRDSELTKVLRDIFV 313
Cdd:cd01373 225 acfvNIRTSRLNLVDLAGSERQKDTHAE-GVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLG 303
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 23491102 314 GKSKSIMIANISPTISSCEQTLNTLRYSSRVKNFKTKPMLNdgEDT 359
Cdd:cd01373 304 GNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVN--EDT 347
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
23-547 5.53e-48

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 180.71  E-value: 5.53e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  23 RKRPINENEKRKKDSDIVTVKDNHTICIDEPRYKVDMT-KYIERHEFIVDKVFDETVDNLTVYQYSIKPLIIDIFENNcV 101
Cdd:COG5059  12 RLSSRNEKSVSDIKSTIRIIPGELGERLINTSKKSHVSlEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGY-N 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 102 CSCFAYGQTGSGKTYTMLGSQpygqsNCPGIFQYASEDIFNFLNTYNNDNSKGIFISFYEIYCGKLYDLLQKRKMVA-AL 180
Cdd:COG5059  91 CTVFAYGQTGSGKTYTMSGTE-----EEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLSPNEESLnIR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 181 ENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDINKN---ISLGKIAFIDLAGSE 257
Cdd:COG5059 166 EDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVsgtSETSKLSLVDLAGSE 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 258 RGADTIAQNKQTQtDGANINRSLLALKECIRA--MDSDKNHIPFRDSELTKVLRDIFVGKSKSIMIANISPTISSCEQTL 335
Cdd:COG5059 246 RAARTGNRGTRLK-EGASINKSLLTLGNVINAlgDKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETI 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 336 NTLRYSSRVKNFKTKPMLNDGEDTaNDPNNSIHTMSYYKSSELNYSSTENFTMKSNSLLSSkpetksiEFRDKNNEKSNK 415
Cdd:COG5059 325 NTLKFASRAKSIKNKIQVNSSSDS-SREIEEIKFDLSEDRSEIEILVFREQSQLSQSSLSG-------IFAYMQSLKKET 396
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 416 KMQKNvcdKND--NKNIKHSNKNRINTIKKNNTISRKNYTFSDTSDFSSLDEMNYNLNNSEKTLFTNSKSLNQQKLKSRN 493
Cdd:COG5059 397 ETLKS---RIDliMKSIISGTFERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSS 473
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....
gi 23491102 494 SCDTINSKVKKNDIQVLRHSVGSKLTNFSYEKNKSKEIEFSKNTVNQSKNILFN 547
Cdd:COG5059 474 IPEETSDRVESEKASKLRSSASTKLNLRSSRSHSKFRDHLNGSNSSTKELSLNQ 527
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
17-345 3.86e-41

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: 154.66  E-value: 3.86e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  17 KIKVVVRKRPINenekRKKDSDIVTVKDNHTICIDEPrykVDMTKYI-----ERHEFIVDKVFDETVDNLtVYQYSIKPL 91
Cdd:cd01375   1 KVQAFVRVRPTD----DFAHEMIKYGEDGKSISIHLK---KDLRRGVvnnqqEDWSFKFDGVLHNASQEL-VYETVAKDV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  92 IIDIFE--NNCVcscFAYGQTGSGKTYTMLG-SQPYGQSncpGIFQYASEDIFNFLNTyNNDNSKGIFISFYEIYCGKLY 168
Cdd:cd01375  73 VSSALAgyNGTI---FAYGQTGAGKTFTMTGgTENYKHR---GIIPRALQQVFRMIEE-RPTKAYTVHVSYLEIYNEQLY 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 169 DLLQKRKMV-------AALENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDLKDINK 241
Cdd:cd01375 146 DLLSTLPYVgpsvtpmTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSR 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 242 NIS-----LGKIAFIDLAGSERGADTiAQNKQTQTDGANINRSLLALKECIRAM-DSDKNHIPFRDSELTKVLRDIFVGK 315
Cdd:cd01375 226 TLSsekyiTSKLNLVDLAGSERLSKT-GVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGN 304
                       330       340       350
                ....*....|....*....|....*....|
gi 23491102 316 SKSIMIANISPTISSCEQTLNTLRYSSRVK 345
Cdd:cd01375 305 CNTVMVANIYGEAAQLEETLSTLRFASRVK 334
PLN03188 PLN03188
kinesin-12 family protein; Provisional
14-355 2.70e-33

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 139.68  E-value: 2.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102    14 SNGKIKVVVRKRPINENEKRKKdsdIVTVKDNHTICIDEprykvdmtkyierHEFIVDKVFDETVDNLTVYQYSIKPLIi 93
Cdd:PLN03188   96 SDSGVKVIVRMKPLNKGEEGEM---IVQKMSNDSLTING-------------QTFTFDSIADPESTQEDIFQLVGAPLV- 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102    94 difeNNCVC----SCFAYGQTGSGKTYTMLG-----SQPYGQSNCPGIFQYASEDIFNFLNTYNNDNSKGIF-----ISF 159
Cdd:PLN03188  159 ----ENCLAgfnsSVFAYGQTGSGKTYTMWGpanglLEEHLSGDQQGLTPRVFERLFARINEEQIKHADRQLkyqcrCSF 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102   160 YEIYCGKLYDLL---QKRKMVAalENGKKEVIVKDLKILRVINKDELIQKMIEGVMLRKIGVNSQNDESSRSHAILNIDL 236
Cdd:PLN03188  235 LEIYNEQITDLLdpsQKNLQIR--EDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVV 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102   237 KDINKNISLG-------KIAFIDLAGSERGADTIAQNKQTQTDGaNINRSLLALKECIRAM-----DSDKNHIPFRDSEL 304
Cdd:PLN03188  313 ESRCKSVADGlssfktsRINLVDLAGSERQKLTGAAGDRLKEAG-NINRSLSQLGNLINILaeisqTGKQRHIPYRDSRL 391
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 23491102   305 TKVLRDIFVGKSKSIMIANISPTISSCEQTLNTLRYSSRVKNFKTKPMLND 355
Cdd:PLN03188  392 TFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNE 442
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
20-289 9.46e-10

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: 58.51  E-value: 9.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102  20 VVVRKRPINENEKRKkdsdivtvkDNHTICIDEPRYKVDMTKYIERhefIVDKVFDETVDNltvyqysikpliidiFENN 99
Cdd:cd01363   1 VLVRVNPFKELPIYR---------DSKIIVFYRGFRRSESQPHVFA---IADPAYQSMLDG---------------YNNQ 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 100 CvcsCFAYGQTGSGKTYTMLgsqpygqsncpGIFQYASEDIFNFLNTYNNDNskgifisfyEIYCGKLYdllqkrkmvaa 179
Cdd:cd01363  54 S---IFAYGESGAGKTETMK-----------GVIPYLASVAFNGINKGETEG---------WVYLTEIT----------- 99
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23491102 180 lengkkevivkdlkilrVINKDELIQKMIEGVMLRKIGVNSqNDESSRSHAILNIDLkdinknislgkiafiDLAGSERg 259
Cdd:cd01363 100 -----------------VTLEDQILQANPILEAFGNAKTTR-NENSSRFGKFIEILL---------------DIAGFEI- 145
                       250       260       270
                ....*....|....*....|....*....|
gi 23491102 260 adtiaqnkqtqtdganINRSLLALKECIRA 289
Cdd:cd01363 146 ----------------INESLNTLMNVLRA 159
 
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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