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Conserved domains on  [gi|2462511773|ref|XP_054193823|]
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kinesin-like protein KIF17 isoform X11 [Homo sapiens]

Protein Classification

myosin/kinesin family protein( domain architecture ID 366212)

myosin/kinesin family protein; contains an ATPase-containing motor domain found in myosins and kinesins that provides the driving force in myosin and kinesin mediated processes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Motor_domain super family cl22853
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
4-335 0e+00

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


The actual alignment was detected with superfamily member cd01371:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 334  Bit Score: 569.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   4 EAVKVVVRCRPMNQRERELRCQPVVTVDCARAQCCIQNP-GAADEPPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEG 82
Cdd:cd01371     1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPkATANEPPKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  83 YNGTIFAYGQTGSGKSFTMQGLPDPPSQRGIIPRAFEHVFESVQCAENTK-FLVRASYLEIYNEDVRDLLGADTKQKLEL 161
Cdd:cd01371    81 YNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQqFLVRVSYLEIYNEEIRDLLGKDQTKRLEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 162 KEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDL 241
Cdd:cd01371   161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 242 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDE 321
Cdd:cd01371   241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
                         330
                  ....*....|....
gi 2462511773 322 TLSTLRYANRAKNI 335
Cdd:cd01371   321 TLSTLRYANRAKNI 334
 
Name Accession Description Interval E-value
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
4-335 0e+00

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: 569.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   4 EAVKVVVRCRPMNQRERELRCQPVVTVDCARAQCCIQNP-GAADEPPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEG 82
Cdd:cd01371     1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPkATANEPPKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  83 YNGTIFAYGQTGSGKSFTMQGLPDPPSQRGIIPRAFEHVFESVQCAENTK-FLVRASYLEIYNEDVRDLLGADTKQKLEL 161
Cdd:cd01371    81 YNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQqFLVRVSYLEIYNEEIRDLLGKDQTKRLEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 162 KEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDL 241
Cdd:cd01371   161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 242 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDE 321
Cdd:cd01371   241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
                         330
                  ....*....|....
gi 2462511773 322 TLSTLRYANRAKNI 335
Cdd:cd01371   321 TLSTLRYANRAKNI 334
Kinesin pfam00225
Kinesin motor domain;
11-335 7.36e-171

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 501.33  E-value: 7.36e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  11 RCRPMNQRERELRCQPVVTVDCARAQCCIQNPGAADEPPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEGYNGTIFAY 90
Cdd:pfam00225   1 RVRPLNEREKERGSSVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  91 GQTGSGKSFTMQGlpdPPSQRGIIPRAFEHVFESVQ-CAENTKFLVRASYLEIYNEDVRDLLGADT--KQKLELKEHPEK 167
Cdd:pfam00225  81 GQTGSGKTYTMEG---SDEQPGIIPRALEDLFDRIQkTKERSEFSVKVSYLEIYNEKIRDLLSPSNknKRKLRIREDPKK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 168 GVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDLAGSERQ 247
Cdd:pfam00225 158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSERA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 248 SKTG-ATGERLKEATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTL 326
Cdd:pfam00225 238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317

                  ....*....
gi 2462511773 327 RYANRAKNI 335
Cdd:pfam00225 318 RFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
5-342 9.74e-166

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: 488.24  E-value: 9.74e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773    5 AVKVVVRCRPMNQRERELRCQPVVTVDCARAQCCIQNPGAADEPPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEGYN 84
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   85 GTIFAYGQTGSGKSFTMQGlpdPPSQRGIIPRAFEHVFESVQC-AENTKFLVRASYLEIYNEDVRDLLGaDTKQKLELKE 163
Cdd:smart00129  81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKrEEGWQFSVKVSYLEIYNEKIRDLLN-PSSKKLEIRE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  164 HPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDErGKDHLRAGKLNLVDLAG 243
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNS-SSGSGKASKLNLVDLAG 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  244 SERQSKTGATGERLKEATKINLSLSALGNVISALVD-GRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDET 322
Cdd:smart00129 236 SERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEET 315
                          330       340
                   ....*....|....*....|
gi 2462511773  323 LSTLRYANRAKNIRNKPRIN 342
Cdd:smart00129 316 LSTLRFASRAKEIKNKPIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
49-368 7.80e-88

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 292.80  E-value: 7.80e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  49 PKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEGYNGTIFAYGQTGSGKSFTMQGLPDPPsqrGIIPRAFEHVFESV-QC 127
Cdd:COG5059    55 EGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLeDL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 128 AENTKFLVRASYLEIYNEDVRDLLGADtKQKLELKEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDS 207
Cdd:COG5059   132 SMTKDFAVSISYLEIYNEKIYDLLSPN-EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDES 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 208 SRSHSIFTISIEMSavdERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-GRCKHVP 286
Cdd:COG5059   211 SRSHSIFQIELASK---NKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDkKKSGHIP 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 287 YRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIRNKPRINE----DPKDALLR----EYQEEIK 358
Cdd:COG5059   288 YRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdsSREIEEIKfdlsEDRSEIE 367
                         330
                  ....*....|
gi 2462511773 359 KLKAILTQQM 368
Cdd:COG5059   368 ILVFREQSQL 377
PLN03188 PLN03188
kinesin-12 family protein; Provisional
1-362 6.99e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 266.42  E-value: 6.99e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773    1 MASEAVKVVVRCRPMNQRERELRCQPVVTVDcaraqcciqnpgAADEPPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVT 80
Cdd:PLN03188    95 VSDSGVKVIVRMKPLNKGEEGEMIVQKMSND------------SLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCL 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   81 EGYNGTIFAYGQTGSGKSFTMQGLPDPPS-------QRGIIPRAFEHVF-----ESVQCAENT-KFLVRASYLEIYNEDV 147
Cdd:PLN03188   163 AGFNSSVFAYGQTGSGKTYTMWGPANGLLeehlsgdQQGLTPRVFERLFarineEQIKHADRQlKYQCRCSFLEIYNEQI 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  148 RDLLgaDTKQK-LELKEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIE---MSAV 223
Cdd:PLN03188   243 TDLL--DPSQKnLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVEsrcKSVA 320
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  224 DerGKDHLRAGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD----GRCKHVPYRDSKLTRLLQDS 299
Cdd:PLN03188   321 D--GLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQES 398
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462511773  300 LGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIRNKPRINEDPKD------ALLREYQEEIKKLKA 362
Cdd:PLN03188   399 LGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDdvnflrEVIRQLRDELQRVKA 467
 
Name Accession Description Interval E-value
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
4-335 0e+00

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: 569.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   4 EAVKVVVRCRPMNQRERELRCQPVVTVDCARAQCCIQNP-GAADEPPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEG 82
Cdd:cd01371     1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPkATANEPPKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  83 YNGTIFAYGQTGSGKSFTMQGLPDPPSQRGIIPRAFEHVFESVQCAENTK-FLVRASYLEIYNEDVRDLLGADTKQKLEL 161
Cdd:cd01371    81 YNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNNQqFLVRVSYLEIYNEEIRDLLGKDQTKRLEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 162 KEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDL 241
Cdd:cd01371   161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 242 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDE 321
Cdd:cd01371   241 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDE 320
                         330
                  ....*....|....
gi 2462511773 322 TLSTLRYANRAKNI 335
Cdd:cd01371   321 TLSTLRYANRAKNI 334
Kinesin pfam00225
Kinesin motor domain;
11-335 7.36e-171

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 501.33  E-value: 7.36e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  11 RCRPMNQRERELRCQPVVTVDCARAQCCIQNPGAADEPPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEGYNGTIFAY 90
Cdd:pfam00225   1 RVRPLNEREKERGSSVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  91 GQTGSGKSFTMQGlpdPPSQRGIIPRAFEHVFESVQ-CAENTKFLVRASYLEIYNEDVRDLLGADT--KQKLELKEHPEK 167
Cdd:pfam00225  81 GQTGSGKTYTMEG---SDEQPGIIPRALEDLFDRIQkTKERSEFSVKVSYLEIYNEKIRDLLSPSNknKRKLRIREDPKK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 168 GVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDLAGSERQ 247
Cdd:pfam00225 158 GVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSERA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 248 SKTG-ATGERLKEATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTL 326
Cdd:pfam00225 238 SKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTL 317

                  ....*....
gi 2462511773 327 RYANRAKNI 335
Cdd:pfam00225 318 RFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
5-342 9.74e-166

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: 488.24  E-value: 9.74e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773    5 AVKVVVRCRPMNQRERELRCQPVVTVDCARAQCCIQNPGAADEPPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEGYN 84
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   85 GTIFAYGQTGSGKSFTMQGlpdPPSQRGIIPRAFEHVFESVQC-AENTKFLVRASYLEIYNEDVRDLLGaDTKQKLELKE 163
Cdd:smart00129  81 ATIFAYGQTGSGKTYTMIG---TPDSPGIIPRALKDLFEKIDKrEEGWQFSVKVSYLEIYNEKIRDLLN-PSSKKLEIRE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  164 HPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDErGKDHLRAGKLNLVDLAG 243
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNS-SSGSGKASKLNLVDLAG 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  244 SERQSKTGATGERLKEATKINLSLSALGNVISALVD-GRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDET 322
Cdd:smart00129 236 SERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEET 315
                          330       340
                   ....*....|....*....|
gi 2462511773  323 LSTLRYANRAKNIRNKPRIN 342
Cdd:smart00129 316 LSTLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
5-333 3.29e-153

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


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 455.95  E-value: 3.29e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   5 AVKVVVRCRPMNQRERElRCQPVVTVDcARAQCCIQNPGAADEPPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEGYN 84
Cdd:cd00106     1 NVRVAVRVRPLNGREAR-SAKSVISVD-GGKSVVLDPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  85 GTIFAYGQTGSGKSFTMQGlpDPPSQRGIIPRAFEHVFESVQ--CAENTKFLVRASYLEIYNEDVRDLLGADTKQKLELK 162
Cdd:cd00106    79 GTIFAYGQTGSGKTYTMLG--PDPEQRGIIPRALEDIFERIDkrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 163 EHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDErGKDHLRAGKLNLVDLA 242
Cdd:cd00106   157 EDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREK-SGESVTSSKLNLVDLA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 243 GSERQSKTGATGERLKEATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDET 322
Cdd:cd00106   236 GSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEET 315
                         330
                  ....*....|.
gi 2462511773 323 LSTLRYANRAK 333
Cdd:cd00106   316 LSTLRFASRAK 326
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
5-336 3.53e-128

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: 391.31  E-value: 3.53e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   5 AVKVVVRCRPMNQRERELRCQPVVTVDCARAQCCIqnpgaadEPPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEGYN 84
Cdd:cd01372     2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTV-------GTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  85 GTIFAYGQTGSGKSFTMQG---LPDPPSQRGIIPRAFEHVFESVQCAENT-KFLVRASYLEIYNEDVRDLLGADTKQK-- 158
Cdd:cd01372    75 ATVLAYGQTGSGKTYTMGTaytAEEDEEQVGIIPRAIQHIFKKIEKKKDTfEFQLKVSFLEIYNEEIRDLLDPETDKKpt 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 159 LELKEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIE---------MSAVDERGkD 229
Cdd:cd01372   155 ISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEqtkkngpiaPMSADDKN-S 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 230 HLRAgKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGRCK--HVPYRDSKLTRLLQDSLGGNTKTL 307
Cdd:cd01372   234 TFTS-KFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKgaHVPYRDSKLTRLLQDSLGGNSHTL 312
                         330       340
                  ....*....|....*....|....*....
gi 2462511773 308 MVACLSPADNNYDETLSTLRYANRAKNIR 336
Cdd:cd01372   313 MIACVSPADSNFEETLNTLKYANRARNIK 341
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
6-342 1.38e-127

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: 390.56  E-value: 1.38e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   6 VKVVVRCRPMNQRERELRCQPVVTVDcaRAQCCIQNPGAADEP-------PKQFTFDGAY-HVD----HVTEQ--IYNEI 71
Cdd:cd01365     3 VKVAVRVRPFNSREKERNSKCIVQMS--GKETTLKNPKQADKNnkatrevPKSFSFDYSYwSHDsedpNYASQeqVYEDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  72 AYPLVEGVTEGYNGTIFAYGQTGSGKSFTMQGLPDppsQRGIIPRAFEHVFESVQC--AENTKFLVRASYLEIYNEDVRD 149
Cdd:cd01365    81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE---QPGIIPRLCEDLFSRIADttNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 150 LLGADT---KQKLELKEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVD-E 225
Cdd:cd01365   158 LLNPKPkknKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDaE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 226 RGKDHLRAGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-------GRCKHVPYRDSKLTRLLQD 298
Cdd:cd01365   238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskKKSSFIPYRDSVLTWLLKE 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2462511773 299 SLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIRNKPRIN 342
Cdd:cd01365   318 NLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
6-344 3.60e-122

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: 376.28  E-value: 3.60e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   6 VKVVVRCRPMNQRERELRCQPVVTVDCARAQCCIQNPGAADE-PPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEGYN 84
Cdd:cd01364     4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGGLADKsSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  85 GTIFAYGQTGSGKSFTMQGLPDP--------PSQRGIIPRAFEHVFESVQcAENTKFLVRASYLEIYNEDVRDLLG--AD 154
Cdd:cd01364    84 CTIFAYGQTGTGKTYTMEGDRSPneeytwelDPLAGIIPRTLHQLFEKLE-DNGTEYSVKVSYLEIYNEELFDLLSpsSD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 155 TKQKLELKEHPE--KGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLR 232
Cdd:cd01364   163 VSERLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEELVK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 233 AGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDgRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACL 312
Cdd:cd01364   243 IGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE-RAPHVPYRESKLTRLLQDSLGGRTKTSIIATI 321
                         330       340       350
                  ....*....|....*....|....*....|..
gi 2462511773 313 SPADNNYDETLSTLRYANRAKNIRNKPRINED 344
Cdd:cd01364   322 SPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
6-337 2.67e-118

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: 364.99  E-value: 2.67e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   6 VKVVVRCRPMNQRERELRCQPVVTVDCARAQCCIQNPGAAdepPKQFTFDGAYHVDHVTEQIYNEIAyPLVEGVTEGYNG 85
Cdd:cd01366     4 IRVFCRVRPLLPSEENEDTSHITFPDEDGQTIELTSIGAK---QKEFSFDKVFDPEASQEDVFEEVS-PLVQSALDGYNV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  86 TIFAYGQTGSGKSFTMQGlpdPPSQRGIIPRAFEHVFESVQCAENT--KFLVRASYLEIYNEDVRDLLGADT--KQKLEL 161
Cdd:cd01366    80 CIFAYGQTGSGKTYTMEG---PPESPGIIPRALQELFNTIKELKEKgwSYTIKASMLEIYNETIRDLLAPGNapQKKLEI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 162 KEHPEKG-VYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSavDERGKDHLRaGKLNLVD 240
Cdd:cd01366   157 RHDSEKGdTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGR--NLQTGEISV-GKLNLVD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 241 LAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGRcKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYD 320
Cdd:cd01366   234 LAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQ-SHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLN 312
                         330
                  ....*....|....*..
gi 2462511773 321 ETLSTLRYANRAKNIRN 337
Cdd:cd01366   313 ETLNSLRFASKVNSCEL 329
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
5-335 6.77e-118

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: 363.96  E-value: 6.77e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   5 AVKVVVRCRPMNQRERELrcqpvvTVDCARAqccIQNPGAADE--PPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEG 82
Cdd:cd01374     1 KITVTVRVRPLNSREIGI------NEQVAWE---IDNDTIYLVepPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  83 YNGTIFAYGQTGSGKSFTMQGLPDPPsqrGIIPRAFEHVFESVQCAENTKFLVRASYLEIYNEDVRDLLgADTKQKLELK 162
Cdd:cd01374    72 YNGTIFAYGQTSSGKTFTMSGDEDEP---GIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLL-SPTSQNLKIR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 163 EHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDLA 242
Cdd:cd01374   148 DDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTVRVSTLNLIDLA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 243 GSERQSKTGATGERLKEATKINLSLSALGNVISALVDGRC-KHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDE 321
Cdd:cd01374   228 GSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVgGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEE 307
                         330
                  ....*....|....
gi 2462511773 322 TLSTLRYANRAKNI 335
Cdd:cd01374   308 TLNTLKFASRAKKI 321
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
6-335 9.44e-117

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: 360.88  E-value: 9.44e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   6 VKVVVRCRPMNQRERELRCQPVVtvdCARAQCCIQNPGAADEppKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEGYNG 85
Cdd:cd01369     4 IKVVCRFRPLNELEVLQGSKSIV---KFDPEDTVVIATSETG--KTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  86 TIFAYGQTGSGKSFTMQGLPDPPSQRGIIPRAFEHVFESV-QCAENTKFLVRASYLEIYNEDVRDLLGAdTKQKLELKEH 164
Cdd:cd01369    79 TIFAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIySMDENLEFHVKVSYFEIYMEKIRDLLDV-SKTNLSVHED 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 165 PEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDErgkDHLRAGKLNLVDLAGS 244
Cdd:cd01369   158 KNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVET---EKKKSGKLYLVDLAGS 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 245 ERQSKTGATGERLKEATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLS 324
Cdd:cd01369   235 EKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLS 314
                         330
                  ....*....|.
gi 2462511773 325 TLRYANRAKNI 335
Cdd:cd01369   315 TLRFGQRAKTI 325
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
5-344 1.60e-111

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: 347.96  E-value: 1.60e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   5 AVKVVVRCRPMNQRERELRCQPVVTVDCARAQCCIQNPgaadepPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEGYN 84
Cdd:cd01373     2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSKP------PKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  85 GTIFAYGQTGSGKSFTMQGLPD-----PPSQRGIIPRAFEHVFESVQ-----CAENTKFLVRASYLEIYNEDVRDLLGAd 154
Cdd:cd01373    76 GTIFAYGQTGSGKTYTMWGPSEsdnesPHGLRGVIPRIFEYLFSLIQrekekAGEGKSFLCKCSFLEIYNEQIYDLLDP- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 155 TKQKLELKEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEmSAVDERGKDHLRAG 234
Cdd:cd01373   155 ASRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIE-SWEKKACFVNIRTS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 235 KLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD---GRCKHVPYRDSKLTRLLQDSLGGNTKTLMVAC 311
Cdd:cd01373   234 RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIAN 313
                         330       340       350
                  ....*....|....*....|....*....|...
gi 2462511773 312 LSPADNNYDETLSTLRYANRAKNIRNKPRINED 344
Cdd:cd01373   314 VHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
6-335 1.90e-109

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: 342.40  E-value: 1.90e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   6 VKVVVRCRPMNQRERELRCQPVV---------------TVDCARAQCCIQNPGAADEPPKQFTFDGAYHVDHVTEQIYNE 70
Cdd:cd01370     2 LTVAVRVRPFSEKEKNEGFRRIVkvmdnhmlvfdpkdeEDGFFHGGSNNRDRRKRRNKELKYVFDRVFDETSTQEEVYEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  71 IAYPLVEGVTEGYNGTIFAYGQTGSGKSFTMQGLPDPPsqrGIIPRAFEHVFESVQCAENTK-FLVRASYLEIYNEDVRD 149
Cdd:cd01370    82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP---GLMVLTMKELFKRIESLKDEKeFEVSMSYLEIYNETIRD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 150 LLGADTKQkLELKEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKD 229
Cdd:cd01370   159 LLNPSSGP-LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 230 HLRAGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGRCK--HVPYRDSKLTRLLQDSLGGNTKTL 307
Cdd:cd01370   238 QVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKnkHIPYRDSKLTRLLKDSLGGNCRTV 317
                         330       340
                  ....*....|....*....|....*...
gi 2462511773 308 MVACLSPADNNYDETLSTLRYANRAKNI 335
Cdd:cd01370   318 MIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
52-333 1.71e-89

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: 289.10  E-value: 1.71e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  52 FTFDGAYHvDHVTEQIYNEIAYPLVEGVTEGYNGTIFAYGQTGSGKSFTMQGLPDPPSQRGIIPRAFEHVFESVQCAENT 131
Cdd:cd01375    50 FKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEERPTK 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 132 KFLVRASYLEIYNEDVRDLLG-----ADTKQKLELKEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKD 206
Cdd:cd01375   129 AYTVHVSYLEIYNEQLYDLLStlpyvGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKN 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 207 SSRSHSIFTISIEMSAvDERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGRCKHVP 286
Cdd:cd01375   209 SSRSHCIFTIHLEAHS-RTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVP 287
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2462511773 287 YRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAK 333
Cdd:cd01375   288 FRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
49-368 7.80e-88

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 292.80  E-value: 7.80e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  49 PKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEGYNGTIFAYGQTGSGKSFTMQGLPDPPsqrGIIPRAFEHVFESV-QC 127
Cdd:COG5059    55 EGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLeDL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 128 AENTKFLVRASYLEIYNEDVRDLLGADtKQKLELKEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDS 207
Cdd:COG5059   132 SMTKDFAVSISYLEIYNEKIYDLLSPN-EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDES 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 208 SRSHSIFTISIEMSavdERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-GRCKHVP 286
Cdd:COG5059   211 SRSHSIFQIELASK---NKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDkKKSGHIP 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 287 YRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIRNKPRINE----DPKDALLR----EYQEEIK 358
Cdd:COG5059   288 YRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdsSREIEEIKfdlsEDRSEIE 367
                         330
                  ....*....|
gi 2462511773 359 KLKAILTQQM 368
Cdd:COG5059   368 ILVFREQSQL 377
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
4-333 1.36e-78

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: 260.02  E-value: 1.36e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   4 EAVKVVVRCRPMNQRERELRCQPVVTV-----------DCARAQcciQNPGAADEPPKQFTFDGAYHVDHVTEQIYNEIA 72
Cdd:cd01368     1 DPVKVYLRVRPLSKDELESEDEGCIEVinsttvvlhppKGSAAN---KSERNGGQKETKFSFSKVFGPNTTQKEFFQGTA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  73 YPLVEGVTEGYNGTIFAYGQTGSGKSFTMQGlpdPPSQRGIIPRAFEHVFESVQcaentKFLVRASYLEIYNEDVRDLL- 151
Cdd:cd01368    78 LPLVQDLLHGKNGLLFTYGVTNSGKTYTMQG---SPGDGGILPRSLDVIFNSIG-----GYSVFVSYIEIYNEYIYDLLe 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 152 -----GADTKQKLELKEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDER 226
Cdd:cd01368   150 pspssPTKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 227 G-----KDHLRAGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISAL----VDGRCKHVPYRDSKLTRLLQ 297
Cdd:cd01368   230 GdvdqdKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLrenqLQGTNKMVPFRDSKLTHLFQ 309
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2462511773 298 DSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAK 333
Cdd:cd01368   310 NYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
6-333 6.27e-75

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: 249.34  E-value: 6.27e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   6 VKVVVRCRPMNQRERELRCQPVVTVdCARAQCCIQNPGAADEPpKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVTEGYNG 85
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPSCVSG-IDSCSVELADPRNHGET-LKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  86 TIFAYGQTGSGKSFTMQGLPDPPsqrGIIPRAFEHVFE-SVQCAENTKFLVraSYLEIYNEDVRDLLGADTKQkLELKEH 164
Cdd:cd01376    80 TVFAYGSTGAGKTFTMLGSPEQP---GLMPLTVMDLLQmTRKEAWALSFTM--SYLEIYQEKILDLLEPASKE-LVIRED 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 165 PEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISiemsaVDERGKD---HLRAGKLNLVDL 241
Cdd:cd01376   154 KDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIK-----VDQRERLapfRQRTGKLNLIDL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 242 AGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG-RCkhVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYD 320
Cdd:cd01376   229 AGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNlPR--IPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQ 306
                         330
                  ....*....|...
gi 2462511773 321 ETLSTLRYANRAK 333
Cdd:cd01376   307 DTLSTLNFAARSR 319
PLN03188 PLN03188
kinesin-12 family protein; Provisional
1-362 6.99e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 266.42  E-value: 6.99e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773    1 MASEAVKVVVRCRPMNQRERELRCQPVVTVDcaraqcciqnpgAADEPPKQFTFDGAYHVDHVTEQIYNEIAYPLVEGVT 80
Cdd:PLN03188    95 VSDSGVKVIVRMKPLNKGEEGEMIVQKMSND------------SLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCL 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   81 EGYNGTIFAYGQTGSGKSFTMQGLPDPPS-------QRGIIPRAFEHVF-----ESVQCAENT-KFLVRASYLEIYNEDV 147
Cdd:PLN03188   163 AGFNSSVFAYGQTGSGKTYTMWGPANGLLeehlsgdQQGLTPRVFERLFarineEQIKHADRQlKYQCRCSFLEIYNEQI 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  148 RDLLgaDTKQK-LELKEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIE---MSAV 223
Cdd:PLN03188   243 TDLL--DPSQKnLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVEsrcKSVA 320
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  224 DerGKDHLRAGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD----GRCKHVPYRDSKLTRLLQDS 299
Cdd:PLN03188   321 D--GLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQES 398
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462511773  300 LGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIRNKPRINEDPKD------ALLREYQEEIKKLKA 362
Cdd:PLN03188   399 LGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDdvnflrEVIRQLRDELQRVKA 467
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
6-333 2.88e-70

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: 236.81  E-value: 2.88e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   6 VKVVVRCRPMNQRERELRCQPVVTVDCAraqCCIqnpgAADEPPKQ-----------FTFDGAYHVDHVTEQIYNEIAYP 74
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKEIDVVSVPSK---LTL----IVHEPKLKvdltkyienhtFRFDYVFDESSSNETVYRSTVKP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  75 LVEGVTEGYNGTIFAYGQTGSGKSFTMQG-LPDPPSQRGIIPRAFEHVFE--SVQCAENTKFlVRASYLEIYNEDVRDLL 151
Cdd:cd01367    75 LVPHIFEGGKATCFAYGQTGSGKTYTMGGdFSGQEESKGIYALAARDVFRllNKLPYKDNLG-VTVSFFEIYGGKVFDLL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 152 gaDTKQKLELKEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEmsavdERGKDHL 231
Cdd:cd01367   154 --NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILR-----DRGTNKL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 232 RaGKLNLVDLAGSERQSKT-GATGERLKEATKINLSLSALGNVISALVDGRcKHVPYRDSKLTRLLQDSL-GGNTKTLMV 309
Cdd:cd01367   227 H-GKLSFVDLAGSERGADTsSADRQTRMEGAEINKSLLALKECIRALGQNK-AHIPFRGSKLTQVLKDSFiGENSKTCMI 304
                         330       340
                  ....*....|....*....|....
gi 2462511773 310 ACLSPADNNYDETLSTLRYANRAK 333
Cdd:cd01367   305 ATISPGASSCEHTLNTLRYADRVK 328
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
8-314 2.88e-22

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: 94.72  E-value: 2.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   8 VVVRCRPMNQRERelrcqpvvtvdcaRAQCCIqnpgaadeppkqftfDGAYHVDHVTE---QIYNeIAYPLVEGVTEGYN 84
Cdd:cd01363     1 VLVRVNPFKELPI-------------YRDSKI---------------IVFYRGFRRSEsqpHVFA-IADPAYQSMLDGYN 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  85 G-TIFAYGQTGSGKSFTMqglpdppsqRGIIPRAFEHVFESvqcaentkflvrasyleiynedvrdllgaDTKQKLELKE 163
Cdd:cd01363    52 NqSIFAYGESGAGKTETM---------KGVIPYLASVAFNG-----------------------------INKGETEGWV 93
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 164 HPEKGvyvkglsmhTVHSVAQCEHIMETGWKNRsVGYTLMNKDSSRSHSIFTIsiemsavdergkdhlragklnLVDLAG 243
Cdd:cd01363    94 YLTEI---------TVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI---------------------LLDIAG 142
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462511773 244 SERqsktgatgerlkeatkINLSLSALGNVISAlvdgrckhvpyrdskltrllqdslggnTKTLMVACLSP 314
Cdd:cd01363   143 FEI----------------INESLNTLMNVLRA---------------------------TRPHFVRCISP 170
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
6-151 2.25e-15

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 74.18  E-value: 2.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773   6 VKVVVRCRPMNQRErelrcqpvvtvdcaraqCCIQNP------GAADEPPKQFTFDGAYHVDHVTEQIYNEIAYpLVEGV 79
Cdd:pfam16796  22 IRVFARVRPELLSE-----------------AQIDYPdetssdGKIGSKNKSFSFDRVFPPESEQEDVFQEISQ-LVQSC 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462511773  80 TEGYNGTIFAYGQTGSGKSFTMqglpdppsqrgiIPRAFEHVFESVQCAENT-KFLVRASYLEIYNEDVRDLL 151
Cdd:pfam16796  84 LDGYNVCIFAYGQTGSGSNDGM------------IPRAREQIFRFISSLKKGwKYTIELQFVEIYNESSQDLL 144
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
87-280 2.65e-04

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 44.73  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773  87 IFAYGQTGSGKSFTMqglpdPPSQRGIIPRAFEHVFEsVQCAENTKFLVRASYLEIyNEDVRDLLGADTKQKL----ELK 162
Cdd:COG5059   385 IFAYMQSLKKETETL-----KSRIDLIMKSIISGTFE-RKKLLKEEGWKYKSTLQF-LRIEIDRLLLLREEELskkkTKI 457
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462511773 163 EHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTIsiEMSAVDERGKDHLragkLNLVDLA 242
Cdd:COG5059   458 HKLNKLRHDLSSLLSSIPEETSDRVESEKASKLRSSASTKLNLRSSRSHSKFRD--HLNGSNSSTKELS----LNQVDLA 531
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2462511773 243 GSERQSKTgATGERLKEATKINLSLSALGNVISALVDG 280
Cdd:COG5059   532 GSERKVSQ-SVGELLRETQSLNKSLSSLGDVIHALGSK 568
 
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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