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Conserved domains on  [gi|2443284|dbj|BAA22394|]
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motor domain of KIF6, partial [Mus musculus]

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 ...
 1-160 3.17e-92

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 cd01375:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 334  Bit Score: 271.38  E-value: 3.17e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAERYSDRGIIPRTLSYIFEQLQKDSSKIYTTHISYLEIYNECGYDLLDPRHEAskLEDLPKV 80
Cdd:cd01375  84 IFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLSTLPYV--GPSVTPM 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   81 TILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSK--EPGSATVRHAKLHssL 158
Cdd:cd01375 162 TILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHsrTLSSEKYITSKLN--L 239


                ..
gi 2443284  159 ID 160
Cdd:cd01375 240 VD 241
 
Name Accession Description Interval E-value
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 1-160 3.17e-92

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: 271.38  E-value: 3.17e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAERYSDRGIIPRTLSYIFEQLQKDSSKIYTTHISYLEIYNECGYDLLDPRHEAskLEDLPKV 80
Cdd:cd01375  84 IFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLSTLPYV--GPSVTPM 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   81 TILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSK--EPGSATVRHAKLHssL 158
Cdd:cd01375 162 TILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHsrTLSSEKYITSKLN--L 239


                ..
gi 2443284  159 ID 160
Cdd:cd01375 240 VD 241
Kinesin pfam00225
Kinesin motor domain;
1-160 1.02e-53

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 172.76  E-value: 1.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284      1 IFAYGQTGSGKTFTITGGAErysDRGIIPRTLSYIFEQLQKDSSKI-YTTHISYLEIYNECGYDLLDPRHEASkledlPK 79
Cdd:pfam00225  77 IFAYGQTGSGKTYTMEGSDE---QPGIIPRALEDLFDRIQKTKERSeFSVKVSYLEIYNEKIRDLLSPSNKNK-----RK 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284     80 VTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSK---EPGSATVRHAKLHs 156
Cdd:pfam00225 149 LRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRnrsTGGEESVKTGKLN- 227


                  ....
gi 2443284    157 sLID 160
Cdd:pfam00225 228 -LVD 230
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 1-160 1.86e-51

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: 166.98  E-value: 1.86e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284       1 IFAYGQTGSGKTFTITGGAErysDRGIIPRTLSYIFEQLQKDSSKI-YTTHISYLEIYNECGYDLLDPRheaskledLPK 79
Cdd:smart00129  83 IFAYGQTGSGKTYTMIGTPD---SPGIIPRALKDLFEKIDKREEGWqFSVKVSYLEIYNEKIRDLLNPS--------SKK 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284      80 VTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSAT--VRHAKLHss 157
Cdd:smart00129 152 LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSgsGKASKLN-- 229


                   ...
gi 2443284     158 LID 160
Cdd:smart00129 230 LVD 232
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
1-165 2.93e-32

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 120.23  E-value: 2.93e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAERYsdrGIIPRTLSYIFEQLQKDSS-KIYTTHISYLEIYNECGYDLLDPrheaskleDLPK 79
Cdd:COG5059  93 VFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLEDLSMtKDFAVSISYLEIYNEKIYDLLSP--------NEES 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   80 VTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSATVRHAKLhsSLI 159
Cdd:COG5059 162 LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETSKL--SLV 239


                ....*.
gi 2443284  160 DTVDLE 165
Cdd:COG5059 240 DLAGSE 245
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 1-164 2.87e-22

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 92.31  E-value: 2.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284      1 IFAYGQTGSGKTFTITGGAERYSD-------RGIIPRTLSYIFEQLQKDSSK------IYTTHISYLEIYNECGYDLLDP 67
Cdd:PLN03188  169 VFAYGQTGSGKTYTMWGPANGLLEehlsgdqQGLTPRVFERLFARINEEQIKhadrqlKYQCRCSFLEIYNEQITDLLDP 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284     68 RHEaskledlpKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSA 147
Cdd:PLN03188  249 SQK--------NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVA 320

                         170
                  ....*....|....*..
gi 2443284    148 TvRHAKLHSSLIDTVDL 164
Cdd:PLN03188  321 D-GLSSFKTSRINLVDL 336
 
Name Accession Description Interval E-value
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 1-160 3.17e-92

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: 271.38  E-value: 3.17e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAERYSDRGIIPRTLSYIFEQLQKDSSKIYTTHISYLEIYNECGYDLLDPRHEAskLEDLPKV 80
Cdd:cd01375  84 IFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLSTLPYV--GPSVTPM 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   81 TILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSK--EPGSATVRHAKLHssL 158
Cdd:cd01375 162 TILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHsrTLSSEKYITSKLN--L 239


                ..
gi 2443284  159 ID 160
Cdd:cd01375 240 VD 241
Kinesin pfam00225
Kinesin motor domain;
1-160 1.02e-53

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 172.76  E-value: 1.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284      1 IFAYGQTGSGKTFTITGGAErysDRGIIPRTLSYIFEQLQKDSSKI-YTTHISYLEIYNECGYDLLDPRHEASkledlPK 79
Cdd:pfam00225  77 IFAYGQTGSGKTYTMEGSDE---QPGIIPRALEDLFDRIQKTKERSeFSVKVSYLEIYNEKIRDLLSPSNKNK-----RK 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284     80 VTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSK---EPGSATVRHAKLHs 156
Cdd:pfam00225 149 LRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRnrsTGGEESVKTGKLN- 227


                  ....
gi 2443284    157 sLID 160
Cdd:pfam00225 228 -LVD 230
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 1-160 1.86e-51

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: 166.98  E-value: 1.86e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284       1 IFAYGQTGSGKTFTITGGAErysDRGIIPRTLSYIFEQLQKDSSKI-YTTHISYLEIYNECGYDLLDPRheaskledLPK 79
Cdd:smart00129  83 IFAYGQTGSGKTYTMIGTPD---SPGIIPRALKDLFEKIDKREEGWqFSVKVSYLEIYNEKIRDLLNPS--------SKK 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284      80 VTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSAT--VRHAKLHss 157
Cdd:smart00129 152 LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSgsGKASKLN-- 229


                   ...
gi 2443284     158 LID 160
Cdd:smart00129 230 LVD 232
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 1-160 6.45e-51

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: 165.51  E-value: 6.45e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGgaERYSDRGIIPRTLSYIFEQLQK--DSSKIYTTHISYLEIYNECGYDLLDPRHEaskledlP 78
Cdd:cd00106  81 IFAYGQTGSGKTYTMLG--PDPEQRGIIPRALEDIFERIDKrkETKSSFSVSASYLEIYNEKIYDLLSPVPK-------K 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   79 KVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKE--PGSATVRHAKLHs 156
Cdd:cd00106 152 PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNreKSGESVTSSKLN- 230


                ....
gi 2443284  157 sLID 160
Cdd:cd00106 231 -LVD 233
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 1-160 1.63e-42

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: 143.89  E-value: 1.63e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAErysDRGIIPRTLSYIFEQLQKDSSK--IYTTHISYLEIYNECGYDLLDPRHEASkledlP 78
Cdd:cd01366  81 IFAYGQTGSGKTYTMEGPPE---SPGIIPRALQELFNTIKELKEKgwSYTIKASMLEIYNETIRDLLAPGNAPQ-----K 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   79 KVTILEDPDQN-IHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSATVRHAKLHss 157
Cdd:cd01366 153 KLEIRHDSEKGdTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLN-- 230


                ...
gi 2443284  158 LID 160
Cdd:cd01366 231 LVD 233
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 1-160 8.24e-39

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: 134.51  E-value: 8.24e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAERYSDRGIIPRTLSYIFEQLQKDSS-KIYTTHISYLEIYNECGYDLLDPRHEAsKLEdlpk 79
Cdd:cd01371  85 IFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQNnQQFLVRVSYLEIYNEEIRDLLGKDQTK-RLE---- 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   80 vtILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSATVRH---AKLHs 156
Cdd:cd01371 160 --LKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHirvGKLN- 236


                ....
gi 2443284  157 sLID 160
Cdd:cd01371 237 -LVD 239
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 1-160 1.66e-37

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: 130.53  E-value: 1.66e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAerySDRGIIPRTLSYIFEQLQKDSSKIYTTHISYLEIYNECGYDLLDPrheASKledlpKV 80
Cdd:cd01374  76 IFAYGQTSSGKTFTMSGDE---DEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSP---TSQ-----NL 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   81 TILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKE---PGSATVRHAKLhsS 157
Cdd:cd01374 145 KIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSErgeLEEGTVRVSTL--N 222


                ...
gi 2443284  158 LID 160
Cdd:cd01374 223 LID 225
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 1-160 7.64e-36

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: 127.08  E-value: 7.64e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAerySDRGIIPRTLSYIFEQLQKDS-SKIYTTHISYLEIYNECGYDLLDPrhEASKLEdlpk 79
Cdd:cd01370  98 VFAYGATGAGKTHTMLGTP---QEPGLMVLTMKELFKRIESLKdEKEFEVSMSYLEIYNETIRDLLNP--SSGPLE---- 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   80 vtILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSA---TVRHAKLhs 156
Cdd:cd01370 169 --LREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASinqQVRQGKL-- 244


                ....
gi 2443284  157 SLID 160
Cdd:cd01370 245 SLID 248
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 1-160 8.86e-36

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: 126.29  E-value: 8.86e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAERYSDRGIIPRTLSYIFEQLQKDSSKI-YTTHISYLEIYNECGYDLLDPRHEaskledlpK 79
Cdd:cd01369  80 IFAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDENLeFHVKVSYFEIYMEKIRDLLDVSKT--------N 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   80 VTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSATVRHAKLHssLI 159
Cdd:cd01369 152 LSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLY--LV 229


                .
gi 2443284  160 D 160
Cdd:cd01369 230 D 230
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 1-164 1.62e-34

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: 123.21  E-value: 1.62e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAERYSD---RGIIPRTLSYIFEQLQKDSSKI-YTTHISYLEIYNECGYDLLDPRHEaskleD 76
Cdd:cd01372  77 VLAYGQTGSGKTYTMGTAYTAEEDeeqVGIIPRAIQHIFKKIEKKKDTFeFQLKVSFLEIYNEEIRDLLDPETD-----K 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   77 LPKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHL------SSKEPGSATVR 150
Cdd:cd01372 152 KPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqtkknGPIAPMSADDK 231

                       170
                ....*....|....*...
gi 2443284  151 H----AKLHsslidTVDL 164
Cdd:cd01372 232 NstftSKFH-----FVDL 244
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 1-164 3.65e-34

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: 122.62  E-value: 3.65e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAER-----YSDRGIIPRTLSYIFEQLQKDSSKI-----YTTHISYLEIYNECGYDLLDPRHE 70
Cdd:cd01373  78 IFAYGQTGSGKTYTMWGPSESdnespHGLRGVIPRIFEYLFSLIQREKEKAgegksFLCKCSFLEIYNEQIYDLLDPASR 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   71 ASKLEdlpkvtilEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSATVR 150
Cdd:cd01373 158 NLKLR--------EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFVN 229

                       170
                ....*....|....
gi 2443284  151 hakLHSSLIDTVDL 164
Cdd:cd01373 230 ---IRTSRLNLVDL 240
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 1-164 6.78e-34

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: 122.08  E-value: 6.78e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAErysDRGIIPRTLSYIFEQLQKDSSK--IYTTHISYLEIYNECGYDLLDPRHEASKledlP 78
Cdd:cd01365  96 LFAYGQTGSGKSYTMMGTQE---QPGIIPRLCEDLFSRIADTTNQnmSYSVEVSYMEIYNEKVRDLLNPKPKKNK----G 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   79 KVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSATVRHAKLhSSL 158
Cdd:cd01365 169 NLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETNLTTEK-VSK 247


                ....*.
gi 2443284  159 IDTVDL 164
Cdd:cd01365 248 ISLVDL 253
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 1-160 3.87e-33

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: 120.12  E-value: 3.87e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAERY--------SDRGIIPRTLSYIFEQLQkDSSKIYTTHISYLEIYNECGYDLLDPRHEAS 72
Cdd:cd01364  86 IFAYGQTGTGKTYTMEGDRSPNeeytweldPLAGIIPRTLHQLFEKLE-DNGTEYSVKVSYLEIYNEELFDLLSPSSDVS 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   73 KledlpKVTILEDPDQ--NIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSAT-- 148
Cdd:cd01364 165 E-----RLRMFDDPRNkrGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGee 239

                       170
                ....*....|...
gi 2443284  149 -VRHAKLHssLID 160
Cdd:cd01364 240 lVKIGKLN--LVD 250
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 1-139 1.81e-32

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: 117.88  E-value: 1.81e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAErysDRGIIPRTLSYIFEQLQKdsskiYTTHISYLEIYNECGYDLLDPRhEASKLEDLPKV 80
Cdd:cd01368  92 LFTYGVTNSGKTYTMQGSPG---DGGILPRSLDVIFNSIGG-----YSVFVSYIEIYNEYIYDLLEPS-PSSPTKKRQSL 162

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 2443284   81 TILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHL 139
Cdd:cd01368 163 RLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKL 221
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
1-165 2.93e-32

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 120.23  E-value: 2.93e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAERYsdrGIIPRTLSYIFEQLQKDSS-KIYTTHISYLEIYNECGYDLLDPrheaskleDLPK 79
Cdd:COG5059  93 VFAYGQTGSGKTYTMSGTEEEP---GIIPLSLKELFSKLEDLSMtKDFAVSISYLEIYNEKIYDLLSP--------NEES 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   80 VTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSATVRHAKLhsSLI 159
Cdd:COG5059 162 LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETSKL--SLV 239


                ....*.
gi 2443284  160 DTVDLE 165
Cdd:COG5059 240 DLAGSE 245
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 1-160 8.07e-26

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: 100.06  E-value: 8.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAERYSDRGIIPRTLSY-IFEQLQKDSSKI-YTTHISYLEIYNECGYDLLDPRheaskledlP 78
Cdd:cd01367  87 CFAYGQTGSGKTYTMGGDFSGQEESKGIYALAARdVFRLLNKLPYKDnLGVTVSFFEIYGGKVFDLLNRK---------K 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284   79 KVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSAtvrHAKLhsSL 158
Cdd:cd01367 158 RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNKL---HGKL--SF 232


                ..
gi 2443284  159 ID 160
Cdd:cd01367 233 VD 234
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 1-143 4.49e-23

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: 92.57  E-value: 4.49e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284    1 IFAYGQTGSGKTFTITGGAERYsdrGIIPRTLSYIFeQLQKDSSKIYTTHISYLEIYNECGYDLLDPrheasKLEDLPkv 80
Cdd:cd01376  81 VFAYGSTGAGKTFTMLGSPEQP---GLMPLTVMDLL-QMTRKEAWALSFTMSYLEIYQEKILDLLEP-----ASKELV-- 149

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2443284   81 tILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKE 143
Cdd:cd01376 150 -IREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRE 211
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 1-164 2.87e-22

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 92.31  E-value: 2.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284      1 IFAYGQTGSGKTFTITGGAERYSD-------RGIIPRTLSYIFEQLQKDSSK------IYTTHISYLEIYNECGYDLLDP 67
Cdd:PLN03188  169 VFAYGQTGSGKTYTMWGPANGLLEehlsgdqQGLTPRVFERLFARINEEQIKhadrqlKYQCRCSFLEIYNEQITDLLDP 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443284     68 RHEaskledlpKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSA 147
Cdd:PLN03188  249 SQK--------NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVA 320

                         170
                  ....*....|....*..
gi 2443284    148 TvRHAKLHSSLIDTVDL 164
Cdd:PLN03188  321 D-GLSSFKTSRINLVDL 336
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 1-65 2.37e-08

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 50.30  E-value: 2.37e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2443284      1 IFAYGQTGSGktftitggaerySDRGIIPRTLSYIFEQLQKDSSKI-YTTHISYLEIYNECGYDLL 65
Cdd:pfam16796  91 IFAYGQTGSG------------SNDGMIPRAREQIFRFISSLKKGWkYTIELQFVEIYNESSQDLL 144
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 1-46 3.88e-06

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: 44.64  E-value: 3.88e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 2443284    1 IFAYGQTGSGKTFTItggaerysdRGIIPRTLSYIFEQLQKDSSKI 46
Cdd:cd01363  55 IFAYGESGAGKTETM---------KGVIPYLASVAFNGINKGETEG 91
 
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.
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