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Conserved domains on  [gi|1799133776|ref|NP_001364642|]
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Kinesin-like protein klp-3 [Caenorhabditis elegans]

Protein Classification

PRK03918 and KISc_C_terminal domain-containing protein( domain architecture ID 13438351)

PRK03918 and KISc_C_terminal domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
234-557 3.75e-168

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: 480.94  E-value: 3.75e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 234 NGNIRVFYRIRPQLASET-DNQKPVVVIDEMDNGVVHVSNttGTRKTSAGADKVIPTDFSQDQIFNEVSPIITSCIDGYN 312
Cdd:cd01366     1 KGNIRVFCRVRPLLPSEEnEDTSHITFPDEDGQTIELTSI--GAKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 313 VCIFAYGHTGSGKTYTMDGPVTMPGINQRAIMQLFETAKERTG-DIKYDIKVAMMEIYNEKIRDLLNT---SNTNLAIRQ 388
Cdd:cd01366    79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEkGWSYTIKASMLEIYNETIRDLLAPgnaPQKKLEIRH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 389 T-EEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNLITKATTVGRLNLVDLAGSE 467
Cdd:cd01366   159 DsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGSE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 468 RVSQTNATGQLLKEAQAINKSLSELGNVVLALRQNQKHIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESISSV 547
Cdd:cd01366   239 RLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSL 318
                         330
                  ....*....|
gi 1799133776 548 NFAEKIGQVF 557
Cdd:cd01366   319 RFASKVNSCE 328
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
18-246 2.98e-03

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  18 HEVELVNMKLQMRILETHIETKDRLLRNLEDIIDEQESRIANMEDF------IQGRATSYTN----RSNMLKGISVLSLD 87
Cdd:PRK03918  236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkeLKEKAEEYIKlsefYEEYLDELREIEKR 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  88 FGNLSEENLRLKNALSQMQ-KVARVNELLETDEDYESDMTSNEDRFA-----------LRSVSPQPTGDVIKPYPQMVQS 155
Cdd:PRK03918  316 LSRLEEEINGIEERIKELEeKEERLEELKKKLKELEKRLEELEERHElyeeakakkeeLERLKKRLTGLTPEKLEKELEE 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 156 MREEGhwKKLQRCAEELKTEKDELKRLALDTKDAFN----------VCMAEMrmmltskTTDFFRVLIERYKAEM----- 220
Cdd:PRK03918  396 LEKAK--EEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpVCGREL-------TEEHRKELLEEYTAELkriek 466
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1799133776 221 ------EKRKQLHNQLVELNGNIRVFYRIRPQ 246
Cdd:PRK03918  467 elkeieEKERKLRKELRELEKVLKKESELIKL 498
 
Name Accession Description Interval E-value
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
234-557 3.75e-168

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: 480.94  E-value: 3.75e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 234 NGNIRVFYRIRPQLASET-DNQKPVVVIDEMDNGVVHVSNttGTRKTSAGADKVIPTDFSQDQIFNEVSPIITSCIDGYN 312
Cdd:cd01366     1 KGNIRVFCRVRPLLPSEEnEDTSHITFPDEDGQTIELTSI--GAKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 313 VCIFAYGHTGSGKTYTMDGPVTMPGINQRAIMQLFETAKERTG-DIKYDIKVAMMEIYNEKIRDLLNT---SNTNLAIRQ 388
Cdd:cd01366    79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEkGWSYTIKASMLEIYNETIRDLLAPgnaPQKKLEIRH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 389 T-EEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNLITKATTVGRLNLVDLAGSE 467
Cdd:cd01366   159 DsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGSE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 468 RVSQTNATGQLLKEAQAINKSLSELGNVVLALRQNQKHIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESISSV 547
Cdd:cd01366   239 RLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSL 318
                         330
                  ....*....|
gi 1799133776 548 NFAEKIGQVF 557
Cdd:cd01366   319 RFASKVNSCE 328
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
236-560 6.90e-143

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: 416.97  E-value: 6.90e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  236 NIRVFYRIRPQLASETDNQKPVVV--IDEMDNGVVHVSNTTGTRKTSAGADKVIPTDFSQDQIFNEVS-PIITSCIDGYN 312
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVpfPDKVGKTLTVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAaPLVDSVLEGYN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  313 VCIFAYGHTGSGKTYTMDGPVTMPGINQRAIMQLFETAKERTGDIKYDIKVAMMEIYNEKIRDLLNTSNTNLAIRQTEEG 392
Cdd:smart00129  81 ATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIREDEKG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  393 RSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSA--TNLITKATTVGRLNLVDLAGSERVS 470
Cdd:smart00129 161 GVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQkiKNSSSGSGKASKLNLVDLAGSERAK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  471 QTNATGQLLKEAQAINKSLSELGNVVLALRQNQK--HIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESISSVN 548
Cdd:smart00129 241 KTGAEGDRLKEAGNINKSLSALGNVINALAQHSKsrHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLR 320
                          330
                   ....*....|..
gi 1799133776  549 FAEKIGQVFTKS 560
Cdd:smart00129 321 FASRAKEIKNKP 332
Kinesin pfam00225
Kinesin motor domain;
242-556 6.50e-134

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 393.48  E-value: 6.50e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 242 RIRPQLASETDNQ--KPVVVIDEMDNGVVHVSNTTGTRKTSAGADKVIPTDFSQDQIFNE-VSPIITSCIDGYNVCIFAY 318
Cdd:pfam00225   1 RVRPLNEREKERGssVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 319 GHTGSGKTYTMDGPVTMPGINQRAIMQLFETAKERTGDIKYDIKVAMMEIYNEKIRDLLNTSNTN---LAIRQTEEGRSS 395
Cdd:pfam00225  81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKKGVY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 396 IPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNLITK---ATTVGRLNLVDLAGSERVSQT 472
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 473 N-ATGQLLKEAQAINKSLSELGNVVLALRQNQK-HIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESISSVNFA 550
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADKKSkHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320

                  ....*.
gi 1799133776 551 EKIGQV 556
Cdd:pfam00225 321 SRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
236-552 4.74e-62

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 214.60  E-value: 4.74e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 236 NIRVFYRIRPQLASETDNQKPVVVIDEMDNGV--------VHVSNTTGTRKTSAgADKVIPTDFSQDQIFNE-VSPIITS 306
Cdd:COG5059     6 NSPLKSRLSSRNEKSVSDIKSTIRIIPGELGErlintskkSHVSLEKSKEGTYA-FDKVFGPSATQEDVYEEtIKPLIDS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 307 CIDGYNVCIFAYGHTGSGKTYTMDGPVTMPGINQRAIMQLFETAKERTGDIKYDIKVAMMEIYNEKIRDLLNTSNTNLAI 386
Cdd:COG5059    85 LLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLSPNEESLNI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 387 RQTEEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNLITKATTVGRLNLVDLAGS 466
Cdd:COG5059   165 REDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETSKLSLVDLAGS 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 467 ERVSQTNATGQLLKEAQAINKSLSELGNVVLALR--QNQKHIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESI 544
Cdd:COG5059   245 ERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETI 324

                  ....*...
gi 1799133776 545 SSVNFAEK 552
Cdd:COG5059   325 NTLKFASR 332
PLN03188 PLN03188
kinesin-12 family protein; Provisional
237-552 3.24e-53

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 196.31  E-value: 3.24e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  237 IRVFYRIRPQLASETDNqkpvVVIDEMDNGVVHVSNTTGTrktsagADKVIPTDFSQDQIFNEV-SPIITSCIDGYNVCI 315
Cdd:PLN03188   100 VKVIVRMKPLNKGEEGE----MIVQKMSNDSLTINGQTFT------FDSIADPESTQEDIFQLVgAPLVENCLAGFNSSV 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  316 FAYGHTGSGKTYTMDGPVT----------MPGINQRAIMQLF-----ETAKERTGDIKYDIKVAMMEIYNEKIRDLLNTS 380
Cdd:PLN03188   170 FAYGQTGSGKTYTMWGPANglleehlsgdQQGLTPRVFERLFarineEQIKHADRQLKYQCRCSFLEIYNEQITDLLDPS 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  381 NTNLAIRQTEEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLV-----SATNLITKATTv 455
Cdd:PLN03188   250 QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVesrckSVADGLSSFKT- 328
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  456 GRLNLVDLAGSERVSQTNATGQLLKEAQAINKSLSELGNVVLALRQ-----NQKHIPFRNCQLTRILEDSLNGDSKTLVI 530
Cdd:PLN03188   329 SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtgKQRHIPYRDSRLTFLLQESLGGNAKLAMV 408
                          330       340
                   ....*....|....*....|..
gi 1799133776  531 VHLSPDAKSLNESISSVNFAEK 552
Cdd:PLN03188   409 CAISPSQSCKSETFSTLRFAQR 430
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
18-246 2.98e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  18 HEVELVNMKLQMRILETHIETKDRLLRNLEDIIDEQESRIANMEDF------IQGRATSYTN----RSNMLKGISVLSLD 87
Cdd:PRK03918  236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkeLKEKAEEYIKlsefYEEYLDELREIEKR 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  88 FGNLSEENLRLKNALSQMQ-KVARVNELLETDEDYESDMTSNEDRFA-----------LRSVSPQPTGDVIKPYPQMVQS 155
Cdd:PRK03918  316 LSRLEEEINGIEERIKELEeKEERLEELKKKLKELEKRLEELEERHElyeeakakkeeLERLKKRLTGLTPEKLEKELEE 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 156 MREEGhwKKLQRCAEELKTEKDELKRLALDTKDAFN----------VCMAEMrmmltskTTDFFRVLIERYKAEM----- 220
Cdd:PRK03918  396 LEKAK--EEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpVCGREL-------TEEHRKELLEEYTAELkriek 466
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1799133776 221 ------EKRKQLHNQLVELNGNIRVFYRIRPQ 246
Cdd:PRK03918  467 elkeieEKERKLRKELRELEKVLKKESELIKL 498
 
Name Accession Description Interval E-value
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
234-557 3.75e-168

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: 480.94  E-value: 3.75e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 234 NGNIRVFYRIRPQLASET-DNQKPVVVIDEMDNGVVHVSNttGTRKTSAGADKVIPTDFSQDQIFNEVSPIITSCIDGYN 312
Cdd:cd01366     1 KGNIRVFCRVRPLLPSEEnEDTSHITFPDEDGQTIELTSI--GAKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 313 VCIFAYGHTGSGKTYTMDGPVTMPGINQRAIMQLFETAKERTG-DIKYDIKVAMMEIYNEKIRDLLNT---SNTNLAIRQ 388
Cdd:cd01366    79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEkGWSYTIKASMLEIYNETIRDLLAPgnaPQKKLEIRH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 389 T-EEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNLITKATTVGRLNLVDLAGSE 467
Cdd:cd01366   159 DsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGSE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 468 RVSQTNATGQLLKEAQAINKSLSELGNVVLALRQNQKHIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESISSV 547
Cdd:cd01366   239 RLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSL 318
                         330
                  ....*....|
gi 1799133776 548 NFAEKIGQVF 557
Cdd:cd01366   319 RFASKVNSCE 328
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
236-560 6.90e-143

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: 416.97  E-value: 6.90e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  236 NIRVFYRIRPQLASETDNQKPVVV--IDEMDNGVVHVSNTTGTRKTSAGADKVIPTDFSQDQIFNEVS-PIITSCIDGYN 312
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVpfPDKVGKTLTVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAaPLVDSVLEGYN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  313 VCIFAYGHTGSGKTYTMDGPVTMPGINQRAIMQLFETAKERTGDIKYDIKVAMMEIYNEKIRDLLNTSNTNLAIRQTEEG 392
Cdd:smart00129  81 ATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIREDEKG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  393 RSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSA--TNLITKATTVGRLNLVDLAGSERVS 470
Cdd:smart00129 161 GVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQkiKNSSSGSGKASKLNLVDLAGSERAK 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  471 QTNATGQLLKEAQAINKSLSELGNVVLALRQNQK--HIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESISSVN 548
Cdd:smart00129 241 KTGAEGDRLKEAGNINKSLSALGNVINALAQHSKsrHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLR 320
                          330
                   ....*....|..
gi 1799133776  549 FAEKIGQVFTKS 560
Cdd:smart00129 321 FASRAKEIKNKP 332
Kinesin pfam00225
Kinesin motor domain;
242-556 6.50e-134

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 393.48  E-value: 6.50e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 242 RIRPQLASETDNQ--KPVVVIDEMDNGVVHVSNTTGTRKTSAGADKVIPTDFSQDQIFNE-VSPIITSCIDGYNVCIFAY 318
Cdd:pfam00225   1 RVRPLNEREKERGssVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 319 GHTGSGKTYTMDGPVTMPGINQRAIMQLFETAKERTGDIKYDIKVAMMEIYNEKIRDLLNTSNTN---LAIRQTEEGRSS 395
Cdd:pfam00225  81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKKGVY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 396 IPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNLITK---ATTVGRLNLVDLAGSERVSQT 472
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 473 N-ATGQLLKEAQAINKSLSELGNVVLALRQNQK-HIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESISSVNFA 550
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADKKSkHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320

                  ....*.
gi 1799133776 551 EKIGQV 556
Cdd:pfam00225 321 SRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
236-553 2.86e-107

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: 325.36  E-value: 2.86e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 236 NIRVFYRIRPQLASETDNQKPVVVIDEMDNGVVHVSNTTGTRKTSAGADKVIPTDFSQDQIFNEV-SPIITSCIDGYNVC 314
Cdd:cd00106     1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYNGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 315 IFAYGHTGSGKTYTMDGPVTM-PGINQRAIMQLFETAKER-TGDIKYDIKVAMMEIYNEKIRDLLNTSN-TNLAIRQTEE 391
Cdd:cd00106    81 IFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKRkETKSSFSVSASYLEIYNEKIYDLLSPVPkKPLSLREDPK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 392 GRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNLITK--ATTVGRLNLVDLAGSERV 469
Cdd:cd00106   161 RGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSgeSVTSSKLNLVDLAGSERA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 470 SQTNATGQLLKEAQAINKSLSELGNVVLALRQNQ-KHIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESISSVN 548
Cdd:cd00106   241 KKTGAEGDRLKEGGNINKSLSALGKVISALADGQnKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLR 320

                  ....*
gi 1799133776 549 FAEKI 553
Cdd:cd00106   321 FASRA 325
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
236-556 3.07e-91

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: 283.84  E-value: 3.07e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 236 NIRVFYRIRPQLASET-DNQKPVVVIDEMDNGVVHVSNTTGTRKTsagaDKVIPTDFSQDQIFNE-VSPIITSCIDGYNV 313
Cdd:cd01369     3 NIKVVCRFRPLNELEVlQGSKSIVKFDPEDTVVIATSETGKTFSF----DRVFDPNTTQEDVYNFaAKPIVDDVLNGYNG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 314 CIFAYGHTGSGKTYTMDGPVTMP---GINQRAIMQLFETAKERTGDIKYDIKVAMMEIYNEKIRDLLNTSNTNLAIRQTE 390
Cdd:cd01369    79 TIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 391 EGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNLITKATTVGRLNLVDLAGSERVS 470
Cdd:cd01369   159 NRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEKVS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 471 QTNATGQLLKEAQAINKSLSELGNVVLALRQNQK-HIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESISSVNF 549
Cdd:cd01369   239 KTGAEGAVLDEAKKINKSLSALGNVINALTDGKKtHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRF 318

                  ....*..
gi 1799133776 550 AEKIGQV 556
Cdd:cd01369   319 GQRAKTI 325
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
236-550 3.93e-85

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: 268.83  E-value: 3.93e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 236 NIRVFYRIRPQLASETD-NQKPVV--------VIDEMDNGVVHVSNTTGTRKTSAGA--------DKVIPTDFSQDQIFN 298
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNeGFRRIVkvmdnhmlVFDPKDEEDGFFHGGSNNRDRRKRRnkelkyvfDRVFDETSTQEEVYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 299 E-VSPIITSCIDGYNVCIFAYGHTGSGKTYTMDGPVTMPGINQRAIMQLFETAKERTGDIKYDIKVAMMEIYNEKIRDLL 377
Cdd:cd01370    81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 378 NTSNTNLAIRQTEEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNL---ITKATT 454
Cdd:cd01370   161 NPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKtasINQQVR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 455 VGRLNLVDLAGSERVSQTNATGQLLKEAQAINKSLSELGNVVLALRQ---NQKHIPFRNCQLTRILEDSLNGDSKTLVIV 531
Cdd:cd01370   241 QGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADpgkKNKHIPYRDSKLTRLLKDSLGGNCRTVMIA 320
                         330
                  ....*....|....*....
gi 1799133776 532 HLSPDAKSLNESISSVNFA 550
Cdd:cd01370   321 NISPSSSSYEETHNTLKYA 339
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
236-550 2.66e-82

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: 260.73  E-value: 2.66e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 236 NIRVFYRIRPqLASETDNQKPVVVIDEMDNGVVHVSNTtgtrKTSAGADKVIPTDFSQDQIFNEVS-PIITSCIDGYNVC 314
Cdd:cd01374     1 KITVTVRVRP-LNSREIGINEQVAWEIDNDTIYLVEPP----STSFTFDHVFGGDSTNREVYELIAkPVVKSALEGYNGT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 315 IFAYGHTGSGKTYTMDGPVTMPGINQRAIMQLFETAKErTGDIKYDIKVAMMEIYNEKIRDLLNTSNTNLAIRQTEEGRS 394
Cdd:cd01374    76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD-TPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDDVEKGV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 395 SIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSAT---NLITKATTVGRLNLVDLAGSERVSQ 471
Cdd:cd01374   155 YVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSergELEEGTVRVSTLNLIDLAGSERAAQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 472 TNATGQLLKEAQAINKSLSELGNVVLAL--RQNQKHIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESISSVNF 549
Cdd:cd01374   235 TGAAGVRRKEGSHINKSLLTLGTVISKLseGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKF 314

                  .
gi 1799133776 550 A 550
Cdd:cd01374   315 A 315
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
237-550 3.24e-82

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: 261.11  E-value: 3.24e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 237 IRVFYRIRPQLASETDNQKPVVVidEMDNGVVHVsnTTGTRKTSAgADKVIPTDFSQDQIFNE-VSPIITSCIDGYNVCI 315
Cdd:cd01372     3 VRVAVRVRPLLPKEIIEGCRICV--SFVPGEPQV--TVGTDKSFT-FDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNATV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 316 FAYGHTGSGKTYTMDG------PVTMPGINQRAIMQLFETAKERTGDIKYDIKVAMMEIYNEKIRDLLNTSN---TNLAI 386
Cdd:cd01372    78 LAYGQTGSGKTYTMGTaytaeeDEEQVGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETdkkPTISI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 387 RQTEEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNLITKA----------TTVG 456
Cdd:cd01372   158 REDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIapmsaddknsTFTS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 457 RLNLVDLAGSERVSQTNATGQLLKEAQAINKSLSELGNVVLALRQNQK---HIPFRNCQLTRILEDSLNGDSKTLVIVHL 533
Cdd:cd01372   238 KFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKkgaHVPYRDSKLTRLLQDSLGGNSHTLMIACV 317
                         330
                  ....*....|....*..
gi 1799133776 534 SPDAKSLNESISSVNFA 550
Cdd:cd01372   318 SPADSNFEETLNTLKYA 334
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
236-552 1.22e-77

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: 248.92  E-value: 1.22e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 236 NIRVFYRIRPQLASET-DNQKPVVVIDEMdNGVVHVSNTTGTRKTSAGA---DKVIPTDFSQDQIFNE-VSPIITSCIDG 310
Cdd:cd01371     2 NVKVVVRCRPLNGKEKaAGALQIVDVDEK-RGQVSVRNPKATANEPPKTftfDAVFDPNSKQLDVYDEtARPLVDSVLEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 311 YNVCIFAYGHTGSGKTYTMDG---PVTMPGINQRAIMQLFETAKERTGDIKYDIKVAMMEIYNEKIRDLL-NTSNTNLAI 386
Cdd:cd01371    81 YNGTIFAYGQTGTGKTYTMEGkreDPELRGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLgKDQTKRLEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 387 RQTEEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNLITKAT---TVGRLNLVDL 463
Cdd:cd01371   161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGEnhiRVGKLNLVDL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 464 AGSERVSQTNATGQLLKEAQAINKSLSELGNVVLALRQNQ-KHIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNE 542
Cdd:cd01371   241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKsTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
                         330
                  ....*....|
gi 1799133776 543 SISSVNFAEK 552
Cdd:cd01371   321 TLSTLRYANR 330
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
235-559 4.52e-75

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: 243.41  E-value: 4.52e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 235 GNIRVFYRIRPQLASETDNQKPVVVidEMDNGVVHVSNTTGTRKTSAGADKViPTDF-----------------SQDQIF 297
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIV--QMSGKETTLKNPKQADKNNKATREV-PKSFsfdysywshdsedpnyaSQEQVY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 298 NEVS-PIITSCIDGYNVCIFAYGHTGSGKTYTMDGPVTMPGINQRAIMQLFE-TAKERTGDIKYDIKVAMMEIYNEKIRD 375
Cdd:cd01365    78 EDLGeELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSrIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 376 LLNTSNT----NLAIRQTEEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNL--I 449
Cdd:cd01365   158 LLNPKPKknkgNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHdaE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 450 TKATT--VGRLNLVDLAGSERVSQTNATGQLLKEAQAINKSLSELGNVVLALRQNQKH--------IPFRNCQLTRILED 519
Cdd:cd01365   238 TNLTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGkskkkssfIPYRDSVLTWLLKE 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1799133776 520 SLNGDSKTLVIVHLSPDAKSLNESISSVNFAEKIGQVFTK 559
Cdd:cd01365   318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNR 357
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
236-552 4.35e-74

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: 240.10  E-value: 4.35e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 236 NIRVFYRIRPQLASETDNQKPVVVIDEMDNGVVHVSNttgtRKTSAGADKVIPTDFSQDQIFNEVS-PIITSCIDGYNVC 314
Cdd:cd01373     2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSK----PPKTFTFDHVADSNTNQESVFQSVGkPIVESCLSGYNGT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 315 IFAYGHTGSGKTYTMDGPVT--------MPGINQRAIMQLF---ETAKERTGD-IKYDIKVAMMEIYNEKIRDLLNTSNT 382
Cdd:cd01373    78 IFAYGQTGSGKTYTMWGPSEsdnesphgLRGVIPRIFEYLFsliQREKEKAGEgKSFLCKCSFLEIYNEQIYDLLDPASR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 383 NLAIRQTEEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSA---TNLITKaTTVGRLN 459
Cdd:cd01373   158 NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESwekKACFVN-IRTSRLN 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 460 LVDLAGSERVSQTNATGQLLKEAQAINKSLSELGNVVLALRQN----QKHIPFRNCQLTRILEDSLNGDSKTLVIVHLSP 535
Cdd:cd01373   237 LVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVahgkQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHP 316
                         330
                  ....*....|....*..
gi 1799133776 536 DAKSLNESISSVNFAEK 552
Cdd:cd01373   317 SSKCFGETLSTLRFAQR 333
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
236-552 6.56e-72

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: 234.53  E-value: 6.56e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 236 NIRVFYRIRPQLASETDNQKPVVVIDEMDNGVVHVSNTTGTRKTSAGA---DKVIPTDFSQDQIFNE-VSPIITSCIDGY 311
Cdd:cd01364     3 NIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGGLADKSSTKTytfDMVFGPEAKQIDVYRSvVCPILDEVLMGY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 312 NVCIFAYGHTGSGKTYTMDGPVT-----------MPGINQRAIMQLFETAKERtgDIKYDIKVAMMEIYNEKIRDLLNTS 380
Cdd:cd01364    83 NCTIFAYGQTGTGKTYTMEGDRSpneeytweldpLAGIIPRTLHQLFEKLEDN--GTEYSVKVSYLEIYNEELFDLLSPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 381 NTN---LAIRQTEEGRSS--IPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSatnliTKATT- 454
Cdd:cd01364   161 SDVserLRMFDDPRNKRGviIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIH-----IKETTi 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 455 -------VGRLNLVDLAGSERVSQTNATGQLLKEAQAINKSLSELGNVVLALRQNQKHIPFRNCQLTRILEDSLNGDSKT 527
Cdd:cd01364   236 dgeelvkIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKT 315
                         330       340
                  ....*....|....*....|....*
gi 1799133776 528 LVIVHLSPDAKSLNESISSVNFAEK 552
Cdd:cd01364   316 SIIATISPASVNLEETLSTLEYAHR 340
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
236-552 7.50e-70

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


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 228.16  E-value: 7.50e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 236 NIRVFYRIRPQLASETDNQKPVVViDEMDNGVVHVSNTTGTRKT-SAGADKVIPTDFSQDQIFN-EVSPIITSCIDGYNV 313
Cdd:cd01376     1 NVRVAVRVRPFVDGTAGASDPSCV-SGIDSCSVELADPRNHGETlKYQFDAFYGEESTQEDIYArEVQPIVPHLLEGQNA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 314 CIFAYGHTGSGKTYTMDGPVTMPGINQRAIMQLFETAkeRTGDIKYDIKVAMMEIYNEKIRDLLNTSNTNLAIRQTEEGR 393
Cdd:cd01376    80 TVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMT--RKEAWALSFTMSYLEIYQEKILDLLEPASKELVIREDKDGN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 394 SSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLV-SATNLITKATTVGRLNLVDLAGSERVSQT 472
Cdd:cd01376   158 ILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVdQRERLAPFRQRTGKLNLIDLAGSEDNRRT 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 473 NATGQLLKEAQAINKSLSELGNVVLALRQNQKHIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESISSVNFAEK 552
Cdd:cd01376   238 GNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAAR 317
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
237-553 3.44e-64

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: 213.98  E-value: 3.44e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 237 IRVFYRIRPQ-------LASETDNQK-PVVVIDEMDNGVVHVSNTTGTRKTsagaDKVIpTDFSQDQIFNEVS-PIITSC 307
Cdd:cd01375     2 VQAFVRVRPTddfahemIKYGEDGKSiSIHLKKDLRRGVVNNQQEDWSFKF----DGVL-HNASQELVYETVAkDVVSSA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 308 IDGYNVCIFAYGHTGSGKTYTMDGPVTM---PGINQRAIMQLFETAKERTGDIkYDIKVAMMEIYNEKIRDLLNT----- 379
Cdd:cd01375    77 LAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTKA-YTVHVSYLEIYNEQLYDLLSTlpyvg 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 380 -SNTNLAIRQTEEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNLITKATTV--G 456
Cdd:cd01375   156 pSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLSSEKYitS 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 457 RLNLVDLAGSERVSQTNATGQLLKEAQAINKSLSELGNVVLAL-RQNQKHIPFRNCQLTRILEDSLNGDSKTLVIVHLSP 535
Cdd:cd01375   236 KLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYG 315
                         330
                  ....*....|....*...
gi 1799133776 536 DAKSLNESISSVNFAEKI 553
Cdd:cd01375   316 EAAQLEETLSTLRFASRV 333
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
237-551 6.89e-64

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: 213.41  E-value: 6.89e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 237 IRVFYRIRPQLASETDNQkpvvvidemDNGVVHVSNTT-------------GTRKTSAGAD------KVIPTDFSQDQIF 297
Cdd:cd01368     3 VKVYLRVRPLSKDELESE---------DEGCIEVINSTtvvlhppkgsaanKSERNGGQKEtkfsfsKVFGPNTTQKEFF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 298 NEV-SPIITSCIDGYNVCIFAYGHTGSGKTYTMDGPVTMPGINQRAIMQLFETAKErtgdikYDIKVAMMEIYNEKIRDL 376
Cdd:cd01368    74 QGTaLPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------YSVFVSYIEIYNEYIYDL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 377 LNTSN-------TNLAIRQTEEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRV-LVSATNL 448
Cdd:cd01368   148 LEPSPssptkkrQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIkLVQAPGD 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 449 ITKAT-------TVGRLNLVDLAGSERVSQTNATGQLLKEAQAINKSLSELGNVVLALRQNQ-----KHIPFRNCQLTRI 516
Cdd:cd01368   228 SDGDVdqdkdqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQlqgtnKMVPFRDSKLTHL 307
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1799133776 517 LEDSLNGDSKTLVIVHLSPDAKSLNESISSVNFAE 551
Cdd:cd01368   308 FQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSA 342
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
236-552 4.74e-62

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 214.60  E-value: 4.74e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 236 NIRVFYRIRPQLASETDNQKPVVVIDEMDNGV--------VHVSNTTGTRKTSAgADKVIPTDFSQDQIFNE-VSPIITS 306
Cdd:COG5059     6 NSPLKSRLSSRNEKSVSDIKSTIRIIPGELGErlintskkSHVSLEKSKEGTYA-FDKVFGPSATQEDVYEEtIKPLIDS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 307 CIDGYNVCIFAYGHTGSGKTYTMDGPVTMPGINQRAIMQLFETAKERTGDIKYDIKVAMMEIYNEKIRDLLNTSNTNLAI 386
Cdd:COG5059    85 LLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLSPNEESLNI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 387 RQTEEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLVSATNLITKATTVGRLNLVDLAGS 466
Cdd:COG5059   165 REDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETSKLSLVDLAGS 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 467 ERVSQTNATGQLLKEAQAINKSLSELGNVVLALR--QNQKHIPFRNCQLTRILEDSLNGDSKTLVIVHLSPDAKSLNESI 544
Cdd:COG5059   245 ERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETI 324

                  ....*...
gi 1799133776 545 SSVNFAEK 552
Cdd:COG5059   325 NTLKFASR 332
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
236-539 2.16e-56

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: 192.90  E-value: 2.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 236 NIRVFYRIRPQLASE-TDNQKPVVVIDEMDNGVVHVSNTT--GTRKTSAGA---DKVIPTDFSQDQIFNE-VSPIITSCI 308
Cdd:cd01367     1 KIKVCVRKRPLNKKEvAKKEIDVVSVPSKLTLIVHEPKLKvdLTKYIENHTfrfDYVFDESSSNETVYRStVKPLVPHIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 309 DGYNVCIFAYGHTGSGKTYTMDG----PVTMPGINQRAIMQLFETAKERTGDIKYDIKVAMMEIYNEKIRDLLNtSNTNL 384
Cdd:cd01367    81 EGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLLN-RKKRV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 385 AIRQTEEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVlvsatNLITKAT--TVGRLNLVD 462
Cdd:cd01367   160 RLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI-----ILRDRGTnkLHGKLSFVD 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799133776 463 LAGSERVSQTN-ATGQLLKEAQAINKSLSELGNVVLALRQNQKHIPFRNCQLTRILEDSLNGD-SKTLVIVHLSPDAKS 539
Cdd:cd01367   235 LAGSERGADTSsADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGASS 313
PLN03188 PLN03188
kinesin-12 family protein; Provisional
237-552 3.24e-53

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 196.31  E-value: 3.24e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  237 IRVFYRIRPQLASETDNqkpvVVIDEMDNGVVHVSNTTGTrktsagADKVIPTDFSQDQIFNEV-SPIITSCIDGYNVCI 315
Cdd:PLN03188   100 VKVIVRMKPLNKGEEGE----MIVQKMSNDSLTINGQTFT------FDSIADPESTQEDIFQLVgAPLVENCLAGFNSSV 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  316 FAYGHTGSGKTYTMDGPVT----------MPGINQRAIMQLF-----ETAKERTGDIKYDIKVAMMEIYNEKIRDLLNTS 380
Cdd:PLN03188   170 FAYGQTGSGKTYTMWGPANglleehlsgdQQGLTPRVFERLFarineEQIKHADRQLKYQCRCSFLEIYNEQITDLLDPS 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  381 NTNLAIRQTEEGRSSIPGLEEVSVNSAEEVTETLARGRKNKAVAATEANIESSRSHVIVRVLV-----SATNLITKATTv 455
Cdd:PLN03188   250 QKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVesrckSVADGLSSFKT- 328
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  456 GRLNLVDLAGSERVSQTNATGQLLKEAQAINKSLSELGNVVLALRQ-----NQKHIPFRNCQLTRILEDSLNGDSKTLVI 530
Cdd:PLN03188   329 SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtgKQRHIPYRDSRLTFLLQESLGGNAKLAMV 408
                          330       340
                   ....*....|....*....|..
gi 1799133776  531 VHLSPDAKSLNESISSVNFAEK 552
Cdd:PLN03188   409 CAISPSQSCKSETFSTLRFAQR 430
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
216-377 2.15e-35

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 130.03  E-value: 2.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 216 YKAEMEKRKQLHNQLVELNGNIRVFYRIRPQLASEtdnqkpvVVIDEMDNgvvHVSNTTGTRKT-SAGADKVIPTDFSQD 294
Cdd:pfam16796   1 LEEEETLRRKLENSIQELKGNIRVFARVRPELLSE-------AQIDYPDE---TSSDGKIGSKNkSFSFDRVFPPESEQE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 295 QIFNEVSPIITSCIDGYNVCIFAYGHTGSGKTytmdgpvtmPGINQRAIMQLFETAKERTGDIKYDIKVAMMEIYNEKIR 374
Cdd:pfam16796  71 DVFQEISQLVQSCLDGYNVCIFAYGQTGSGSN---------DGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQ 141

                  ...
gi 1799133776 375 DLL 377
Cdd:pfam16796 142 DLL 144
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
292-500 4.50e-17

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: 78.93  E-value: 4.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 292 SQDQIFNEVSPIITSCIDGYNV-CIFAYGHTGSGKTYTMDGpvtmpginqraIMQLFetakertgdikydikvamMEIYN 370
Cdd:cd01363    31 SQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMKG-----------VIPYL------------------ASVAF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 371 EKIRDLLNtsntnlairqteegrSSIPGLEEVSVNSAEEVTETLARGRKNKaVAATEANIESSRSHVIVRVlvsatnlit 450
Cdd:cd01363    82 NGINKGET---------------EGWVYLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI--------- 136
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1799133776 451 kattvgrlnLVDLAGSERvsqtnatgqllkeaqaINKSLSELGNVVLALR 500
Cdd:cd01363   137 ---------LLDIAGFEI----------------INESLNTLMNVLRATR 161
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
315-499 1.82e-04

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 44.34  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 315 IFAYGHTGSGKTYTMDGPVtmPGINQRAIMQLFETAK-ERTGDIKYDIKVAMMEIYNEKIRDLLNTSNTNLA--IRQTEE 391
Cdd:COG5059   385 IFAYMQSLKKETETLKSRI--DLIMKSIISGTFERKKlLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKtkIHKLNK 462
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 392 GRSSIPGLEEVSVNSAEEVTETLARGrKNKAVAATEANIESSRSHVIVRVLVSATNLITKATtvgRLNLVDLAGSERVSq 471
Cdd:COG5059   463 LRHDLSSLLSSIPEETSDRVESEKAS-KLRSSASTKLNLRSSRSHSKFRDHLNGSNSSTKEL---SLNQVDLAGSERKV- 537
                         170       180
                  ....*....|....*....|....*...
gi 1799133776 472 TNATGQLLKEAQAINKSLSELGNVVLAL 499
Cdd:COG5059   538 SQSVGELLRETQSLNKSLSSLGDVIHAL 565
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
18-246 2.98e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  18 HEVELVNMKLQMRILETHIETKDRLLRNLEDIIDEQESRIANMEDF------IQGRATSYTN----RSNMLKGISVLSLD 87
Cdd:PRK03918  236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkeLKEKAEEYIKlsefYEEYLDELREIEKR 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776  88 FGNLSEENLRLKNALSQMQ-KVARVNELLETDEDYESDMTSNEDRFA-----------LRSVSPQPTGDVIKPYPQMVQS 155
Cdd:PRK03918  316 LSRLEEEINGIEERIKELEeKEERLEELKKKLKELEKRLEELEERHElyeeakakkeeLERLKKRLTGLTPEKLEKELEE 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799133776 156 MREEGhwKKLQRCAEELKTEKDELKRLALDTKDAFN----------VCMAEMrmmltskTTDFFRVLIERYKAEM----- 220
Cdd:PRK03918  396 LEKAK--EEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpVCGREL-------TEEHRKELLEEYTAELkriek 466
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1799133776 221 ------EKRKQLHNQLVELNGNIRVFYRIRPQ 246
Cdd:PRK03918  467 elkeieEKERKLRKELRELEKVLKKESELIKL 498
 
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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