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Conserved domains on  [gi|564473366|ref|NP_001274141|]
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kinesin-like protein KIF17 isoform c [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 ...
 1-235 1.11e-146

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: 437.66  E-value: 1.11e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   1 MQGLPDPPSQRGIIPRAFEHVFESVQCAENTK-FLVRASYLEIYNEDVRDLLGADTKQKLELKEHPEKGVYVKGLSMHTV 79
Cdd:cd01371   99 MEGKREDPELRGIIPNSFAHIFGHIARSQNNQqFLVRVSYLEIYNEEIRDLLGKDQTKRLELKERPDTGVYVKDLSMFVV 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  80 HSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKE 159
Cdd:cd01371  179 KNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKE 258

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564473366 160 ATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNI 235
Cdd:cd01371  259 ATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 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 ...
 1-235 1.11e-146

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: 437.66  E-value: 1.11e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   1 MQGLPDPPSQRGIIPRAFEHVFESVQCAENTK-FLVRASYLEIYNEDVRDLLGADTKQKLELKEHPEKGVYVKGLSMHTV 79
Cdd:cd01371   99 MEGKREDPELRGIIPNSFAHIFGHIARSQNNQqFLVRVSYLEIYNEEIRDLLGKDQTKRLELKERPDTGVYVKDLSMFVV 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  80 HSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKE 159
Cdd:cd01371  179 KNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKE 258

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564473366 160 ATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNI 235
Cdd:cd01371  259 ATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
Kinesin pfam00225
Kinesin motor domain;
1-235 5.60e-127

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 386.16  E-value: 5.60e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366    1 MQGlpdPPSQRGIIPRAFEHVFESVQ-CAENTKFLVRASYLEIYNEDVRDLLGADT--KQKLELKEHPEKGVYVKGLSMH 77
Cdd:pfam00225  91 MEG---SDEQPGIIPRALEDLFDRIQkTKERSEFSVKVSYLEIYNEKIRDLLSPSNknKRKLRIREDPKKGVYVKGLTEV 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   78 TVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDLAGSERQSKTG-ATGER 156
Cdd:pfam00225 168 EVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSERASKTGaAGGQR 247

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564473366  157 LKEATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNI 235
Cdd:pfam00225 248 LKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 1-242 1.84e-120

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: 369.59  E-value: 1.84e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366     1 MQGlpdPPSQRGIIPRAFEHVFESVQC-AENTKFLVRASYLEIYNEDVRDLLGaDTKQKLELKEHPEKGVYVKGLSMHTV 79
Cdd:smart00129  97 MIG---TPDSPGIIPRALKDLFEKIDKrEEGWQFSVKVSYLEIYNEKIRDLLN-PSSKKLEIREDEKGGVYVKGLTEISV 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366    80 HSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDErGKDHLRAGKLNLVDLAGSERQSKTGATGERLKE 159
Cdd:smart00129 173 SSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNS-SSGSGKASKLNLVDLAGSERAKKTGAEGDRLKE 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   160 ATKINLSLSALGNVISALVD-GRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIRNK 238
Cdd:smart00129 252 AGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNK 331


                   ....
gi 564473366   239 PRIN 242
Cdd:smart00129 332 PIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
1-268 5.35e-66

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 231.94  E-value: 5.35e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   1 MQGLPDPPsqrGIIPRAFEHVFESV-QCAENTKFLVRASYLEIYNEDVRDLLGADtKQKLELKEHPEKGVYVKGLSMHTV 79
Cdd:COG5059  107 MSGTEEEP---GIIPLSLKELFSKLeDLSMTKDFAVSISYLEIYNEKIYDLLSPN-EESLNIREDSLLGVKVAGLTEKHV 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  80 HSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSavdERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKE 159
Cdd:COG5059  183 SSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASK---NKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKE 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366 160 ATKINLSLSALGNVISALVD-GRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIRNK 238
Cdd:COG5059  260 GASINKSLLTLGNVINALGDkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNK 339

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564473366 239 PRINE----DPKDALLR----EYQEEIKKLKAILTQQM 268
Cdd:COG5059  340 IQVNSssdsSREIEEIKfdlsEDRSEIEILVFREQSQL 377
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 10-262 5.07e-57

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 214.41  E-value: 5.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   10 QRGIIPRAFEHVF-----ESVQCAENT-KFLVRASYLEIYNEDVRDLLgaDTKQK-LELKEHPEKGVYVKGLSMHTVHSV 82
Cdd:PLN03188  199 QQGLTPRVFERLFarineEQIKHADRQlKYQCRCSFLEIYNEQITDLL--DPSQKnLQIREDVKSGVYVENLTEEYVKTM 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   83 AQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIE---MSAVDerGKDHLRAGKLNLVDLAGSERQSKTGATGERLKE 159
Cdd:PLN03188  277 KDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVEsrcKSVAD--GLSSFKTSRINLVDLAGSERQKLTGAAGDRLKE 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  160 ATKINLSLSALGNVISALVD----GRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNI 235
Cdd:PLN03188  355 AGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAI 434

                         250       260       270
                  ....*....|....*....|....*....|...
gi 564473366  236 RNKPRINEDPKD------ALLREYQEEIKKLKA 262
Cdd:PLN03188  435 KNKAVVNEVMQDdvnflrEVIRQLRDELQRVKA 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 ...
 1-235 1.11e-146

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: 437.66  E-value: 1.11e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   1 MQGLPDPPSQRGIIPRAFEHVFESVQCAENTK-FLVRASYLEIYNEDVRDLLGADTKQKLELKEHPEKGVYVKGLSMHTV 79
Cdd:cd01371   99 MEGKREDPELRGIIPNSFAHIFGHIARSQNNQqFLVRVSYLEIYNEEIRDLLGKDQTKRLELKERPDTGVYVKDLSMFVV 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  80 HSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKE 159
Cdd:cd01371  179 KNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKE 258

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564473366 160 ATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNI 235
Cdd:cd01371  259 ATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
Kinesin pfam00225
Kinesin motor domain;
1-235 5.60e-127

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 386.16  E-value: 5.60e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366    1 MQGlpdPPSQRGIIPRAFEHVFESVQ-CAENTKFLVRASYLEIYNEDVRDLLGADT--KQKLELKEHPEKGVYVKGLSMH 77
Cdd:pfam00225  91 MEG---SDEQPGIIPRALEDLFDRIQkTKERSEFSVKVSYLEIYNEKIRDLLSPSNknKRKLRIREDPKKGVYVKGLTEV 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   78 TVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDLAGSERQSKTG-ATGER 156
Cdd:pfam00225 168 EVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSERASKTGaAGGQR 247

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564473366  157 LKEATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNI 235
Cdd:pfam00225 248 LKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 1-242 1.84e-120

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: 369.59  E-value: 1.84e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366     1 MQGlpdPPSQRGIIPRAFEHVFESVQC-AENTKFLVRASYLEIYNEDVRDLLGaDTKQKLELKEHPEKGVYVKGLSMHTV 79
Cdd:smart00129  97 MIG---TPDSPGIIPRALKDLFEKIDKrEEGWQFSVKVSYLEIYNEKIRDLLN-PSSKKLEIREDEKGGVYVKGLTEISV 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366    80 HSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDErGKDHLRAGKLNLVDLAGSERQSKTGATGERLKE 159
Cdd:smart00129 173 SSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNS-SSGSGKASKLNLVDLAGSERAKKTGAEGDRLKE 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   160 ATKINLSLSALGNVISALVD-GRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIRNK 238
Cdd:smart00129 252 AGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNK 331


                   ....
gi 564473366   239 PRIN 242
Cdd:smart00129 332 PIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 1-233 2.46e-114

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: 353.48  E-value: 2.46e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   1 MQGlpDPPSQRGIIPRAFEHVFESVQ--CAENTKFLVRASYLEIYNEDVRDLLGADTKQKLELKEHPEKGVYVKGLSMHT 78
Cdd:cd00106   95 MLG--PDPEQRGIIPRALEDIFERIDkrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLREDPKRGVYVKGLTEVE 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  79 VHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDErGKDHLRAGKLNLVDLAGSERQSKTGATGERLK 158
Cdd:cd00106  173 VGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREK-SGESVTSSKLNLVDLAGSERAKKTGAEGDRLK 251

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564473366 159 EATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAK 233
Cdd:cd00106  252 EGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 1-242 1.30e-93

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: 300.04  E-value: 1.30e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   1 MQGLPDppsQRGIIPRAFEHVFESVQC--AENTKFLVRASYLEIYNEDVRDLLGADT---KQKLELKEHPEKGVYVKGLS 75
Cdd:cd01365  110 MMGTQE---QPGIIPRLCEDLFSRIADttNQNMSYSVEVSYMEIYNEKVRDLLNPKPkknKGNLKVREHPVLGPYVEDLS 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  76 MHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVD-ERGKDHLRAGKLNLVDLAGSERQSKTGATG 154
Cdd:cd01365  187 KLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDaETNLTTEKVSKISLVDLAGSERASSTGATG 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366 155 ERLKEATKINLSLSALGNVISALVD-------GRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLR 227
Cdd:cd01365  267 DRLKEGANINKSLTTLGKVISALADmssgkskKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLR 346

                        250
                 ....*....|....*
gi 564473366 228 YANRAKNIRNKPRIN 242
Cdd:cd01365  347 YADRAKKIVNRAVVN 361
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 9-236 2.91e-93

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: 298.48  E-value: 2.91e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   9 SQRGIIPRAFEHVFESVQCAENT-KFLVRASYLEIYNEDVRDLLGADTKQK--LELKEHPEKGVYVKGLSMHTVHSVAQC 85
Cdd:cd01372  102 EQVGIIPRAIQHIFKKIEKKKDTfEFQLKVSFLEIYNEEIRDLLDPETDKKptISIREDSKGGITIVGLTEVTVLSAEDM 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  86 EHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIE---------MSAVDERGkDHLRAgKLNLVDLAGSERQSKTGATGER 156
Cdd:cd01372  182 MSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEqtkkngpiaPMSADDKN-STFTS-KFHFVDLAGSERLKRTGATGDR 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366 157 LKEATKINLSLSALGNVISALVDGRCK--HVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKN 234
Cdd:cd01372  260 LKEGISINSGLLALGNVISALGDESKKgaHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARN 339


                 ..
gi 564473366 235 IR 236
Cdd:cd01372  340 IK 341
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 1-237 5.89e-90

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: 289.11  E-value: 5.89e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   1 MQGlpdPPSQRGIIPRAFEHVFESVQCAENT--KFLVRASYLEIYNEDVRDLLGADT--KQKLELKEHPEKG-VYVKGLS 75
Cdd:cd01366   95 MEG---PPESPGIIPRALQELFNTIKELKEKgwSYTIKASMLEIYNETIRDLLAPGNapQKKLEIRHDSEKGdTTVTNLT 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  76 MHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSavDERGKDHLRaGKLNLVDLAGSERQSKTGATGE 155
Cdd:cd01366  172 EVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGR--NLQTGEISV-GKLNLVDLAGSERLNKSGATGD 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366 156 RLKEATKINLSLSALGNVISALVDGRcKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNI 235
Cdd:cd01366  249 RLKETQAINKSLSALGDVISALRQKQ-SHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSC 327


                 ..
gi 564473366 236 RN 237
Cdd:cd01366  328 EL 329
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 12-244 9.89e-88

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: 284.22  E-value: 9.89e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  12 GIIPRAFEHVFESVQcAENTKFLVRASYLEIYNEDVRDLLG--ADTKQKLELKEHPE--KGVYVKGLSMHTVHSVAQCEH 87
Cdd:cd01364  119 GIIPRTLHQLFEKLE-DNGTEYSVKVSYLEIYNEELFDLLSpsSDVSERLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQ 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  88 IMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKEATKINLSL 167
Cdd:cd01364  198 ILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSL 277

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564473366 168 SALGNVISALVDgRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIRNKPRINED 244
Cdd:cd01364  278 LTLGRVITALVE-RAPHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 1-235 2.35e-87

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: 281.91  E-value: 2.35e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   1 MQGLPDPPsqrGIIPRAFEHVFESVQCAENTKFLVRASYLEIYNEDVRDLLgADTKQKLELKEHPEKGVYVKGLSMHTVH 80
Cdd:cd01374   90 MSGDEDEP---GIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLL-SPTSQNLKIRDDVEKGVYVAGLTEEIVS 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  81 SVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKEA 160
Cdd:cd01374  166 SPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTVRVSTLNLIDLAGSERAAQTGAAGVRRKEG 245

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564473366 161 TKINLSLSALGNVISALVDGRC-KHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNI 235
Cdd:cd01374  246 SHINKSLLTLGTVISKLSEGKVgGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 1-235 1.74e-85

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: 276.90  E-value: 1.74e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   1 MQGLPDPPSQRGIIPRAFEHVFESV-QCAENTKFLVRASYLEIYNEDVRDLLGAdTKQKLELKEHPEKGVYVKGLSMHTV 79
Cdd:cd01369   94 MEGKLGDPESMGIIPRIVQDIFETIySMDENLEFHVKVSYFEIYMEKIRDLLDV-SKTNLSVHEDKNRGPYVKGATERFV 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  80 HSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDErgkDHLRAGKLNLVDLAGSERQSKTGATGERLKE 159
Cdd:cd01369  173 SSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVET---EKKKSGKLYLVDLAGSEKVSKTGAEGAVLDE 249

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564473366 160 ATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNI 235
Cdd:cd01369  250 AKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 7-244 5.35e-82

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: 268.61  E-value: 5.35e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   7 PPSQRGIIPRAFEHVFESVQ-----CAENTKFLVRASYLEIYNEDVRDLLGAdTKQKLELKEHPEKGVYVKGLSMHTVHS 81
Cdd:cd01373  103 PHGLRGVIPRIFEYLFSLIQrekekAGEGKSFLCKCSFLEIYNEQIYDLLDP-ASRNLKLREDIKKGVYVENLVEEYVTS 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  82 VAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEmSAVDERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKEAT 161
Cdd:cd01373  182 AEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIE-SWEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAG 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366 162 KINLSLSALGNVISALVD---GRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIRNK 238
Cdd:cd01373  261 NINKSLSCLGHVINALVDvahGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNK 340


                 ....*.
gi 564473366 239 PRINED 244
Cdd:cd01373  341 AVVNED 346
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 7-235 1.45e-80

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: 264.59  E-value: 1.45e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   7 PPSQRGIIPRAFEHVFESVQCAENTK-FLVRASYLEIYNEDVRDLLGADTKQkLELKEHPEKGVYVKGLSMHTVHSVAQC 85
Cdd:cd01370  115 TPQEPGLMVLTMKELFKRIESLKDEKeFEVSMSYLEIYNETIRDLLNPSSGP-LELREDAQNGIVVAGLTEHSPKSAEEI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  86 EHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKEATKINL 165
Cdd:cd01370  194 LELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINR 273

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564473366 166 SLSALGNVISALVDGRCK--HVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNI 235
Cdd:cd01370  274 SLLALGNCINALADPGKKnkHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 1-233 1.72e-67

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 228.62  E-value: 1.72e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   1 MQGLPDPPSQRGIIPRAFEHVFESVQCAENTKFLVRASYLEIYNEDVRDLLG-----ADTKQKLELKEHPEKGVYVKGLS 75
Cdd:cd01375   98 MTGGTENYKHRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLStlpyvGPSVTPMTILEDSPQNIFIKGLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  76 MHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDErGKDHLRAGKLNLVDLAGSERQSKTGATGE 155
Cdd:cd01375  178 LHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTL-SSEKYITSKLNLVDLAGSERLSKTGVEGQ 256

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564473366 156 RLKEATKINLSLSALGNVISALVDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAK 233
Cdd:cd01375  257 VLKEATYINKSLSFLEQAIIALSDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
1-268 5.35e-66

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 231.94  E-value: 5.35e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   1 MQGLPDPPsqrGIIPRAFEHVFESV-QCAENTKFLVRASYLEIYNEDVRDLLGADtKQKLELKEHPEKGVYVKGLSMHTV 79
Cdd:COG5059  107 MSGTEEEP---GIIPLSLKELFSKLeDLSMTKDFAVSISYLEIYNEKIYDLLSPN-EESLNIREDSLLGVKVAGLTEKHV 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  80 HSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSavdERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKE 159
Cdd:COG5059  183 SSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASK---NKVSGTSETSKLSLVDLAGSERAARTGNRGTRLKE 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366 160 ATKINLSLSALGNVISALVD-GRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIRNK 238
Cdd:COG5059  260 GASINKSLLTLGNVINALGDkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNK 339

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564473366 239 PRINE----DPKDALLR----EYQEEIKKLKAILTQQM 268
Cdd:COG5059  340 IQVNSssdsSREIEEIKfdlsEDRSEIEILVFREQSQL 377
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 1-233 3.70e-58

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: 203.39  E-value: 3.70e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   1 MQGlpdPPSQRGIIPRAFEHVFESVQcaentKFLVRASYLEIYNEDVRDLL------GADTKQKLELKEHPEKGVYVKGL 74
Cdd:cd01368  106 MQG---SPGDGGILPRSLDVIFNSIG-----GYSVFVSYIEIYNEYIYDLLepspssPTKKRQSLRLREDHNGNMYVAGL 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  75 SMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIEMSAVDERG-----KDHLRAGKLNLVDLAGSERQSK 149
Cdd:cd01368  178 TEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGdvdqdKDQITVSQLSLVDLAGSERTSR 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366 150 TGATGERLKEATKINLSLSALGNVISAL----VDGRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLST 225
Cdd:cd01368  258 TQNTGERLKEAGNINTSLMTLGTCIEVLrenqLQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHV 337


                 ....*...
gi 564473366 226 LRYANRAK 233
Cdd:cd01368  338 MKFSAIAQ 345
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 10-262 5.07e-57

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 214.41  E-value: 5.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   10 QRGIIPRAFEHVF-----ESVQCAENT-KFLVRASYLEIYNEDVRDLLgaDTKQK-LELKEHPEKGVYVKGLSMHTVHSV 82
Cdd:PLN03188  199 QQGLTPRVFERLFarineEQIKHADRQlKYQCRCSFLEIYNEQITDLL--DPSQKnLQIREDVKSGVYVENLTEEYVKTM 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   83 AQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISIE---MSAVDerGKDHLRAGKLNLVDLAGSERQSKTGATGERLKE 159
Cdd:PLN03188  277 KDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVEsrcKSVAD--GLSSFKTSRINLVDLAGSERQKLTGAAGDRLKE 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  160 ATKINLSLSALGNVISALVD----GRCKHVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNI 235
Cdd:PLN03188  355 AGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAI 434

                         250       260       270
                  ....*....|....*....|....*....|...
gi 564473366  236 RNKPRINEDPKD------ALLREYQEEIKKLKA 262
Cdd:PLN03188  435 KNKAVVNEVMQDdvnflrEVIRQLRDELQRVKA 467
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 1-233 2.43e-53

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: 188.87  E-value: 2.43e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366   1 MQGLPDPPsqrGIIPRAFEHVFE-SVQCAENTKFLVraSYLEIYNEDVRDLLGADTKQkLELKEHPEKGVYVKGLSMHTV 79
Cdd:cd01376   95 MLGSPEQP---GLMPLTVMDLLQmTRKEAWALSFTM--SYLEIYQEKILDLLEPASKE-LVIREDKDGNILIPGLSSKPI 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  80 HSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIFTISiemsaVDERGKD---HLRAGKLNLVDLAGSERQSKTGATGER 156
Cdd:cd01376  169 KSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIK-----VDQRERLapfRQRTGKLNLIDLAGSEDNRRTGNEGIR 243

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564473366 157 LKEATKINLSLSALGNVISALVDG-RCkhVPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAK 233
Cdd:cd01376  244 LKESGAINSSLFVLSKVVNALNKNlPR--IPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 35-233 1.82e-45

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: 166.70  E-value: 1.82e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  35 VRASYLEIYNEDVRDLLgaDTKQKLELKEHPEKGVYVKGLSMHTVHSVAQCEHIMETGWKNRSVGYTLMNKDSSRSHSIF 114
Cdd:cd01367  137 VTVSFFEIYGGKVFDLL--NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAIL 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366 115 TISIEmsavdERGKDHLRaGKLNLVDLAGSERQSKTG-ATGERLKEATKINLSLSALGNVISALVDGRcKHVPYRDSKLT 193
Cdd:cd01367  215 QIILR-----DRGTNKLH-GKLSFVDLAGSERGADTSsADRQTRMEGAEINKSLLALKECIRALGQNK-AHIPFRGSKLT 287

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564473366 194 RLLQDSL-GGNTKTLMVACLSPADNNYDETLSTLRYANRAK 233
Cdd:cd01367  288 QVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 73-214 4.30e-10

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


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 59.67  E-value: 4.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564473366  73 GLSMHTVHSVAQCEHIMETGWKNRsVGYTLMNKDSSRSHSIFTIsiemsavdergkdhlragklnLVDLAGSERqsktga 152
Cdd:cd01363   94 YLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI---------------------LLDIAGFEI------ 145

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564473366 153 tgerlkeatkINLSLSALGNVISAlvdgrckhvpyrdskltrllqdslggnTKTLMVACLSP 214
Cdd:cd01363  146 ----------INESLNTLMNVLRA---------------------------TRPHFVRCISP 170
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 3-51 5.09e-05

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 44.13  E-value: 5.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 564473366    3 GLPDPPSQRGIIPRAFEHVFESVQCAENT-KFLVRASYLEIYNEDVRDLL 51
Cdd:pfam16796  95 GQTGSGSNDGMIPRAREQIFRFISSLKKGwKYTIELQFVEIYNESSQDLL 144
 
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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