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Conserved domains on  [gi|1370513726|ref|XP_024303174|]
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kinesin-like protein KIF12 isoform X5 [Homo sapiens]

Protein Classification

kinesin family protein( domain architecture ID 10058885)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has ATPase-containing motor domain; similar to N-type kinesins that are (+) end-directed motors and have an N-terminal motor domain

CATH:  3.40.850.10
Gene Ontology:  GO:0007018|GO:0003777|GO:0005524|GO:0016887|GO:0005871
PubMed:  9368744|1618910|32842864
SCOP:  4004055

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 1-225 2.67e-98

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: 296.09  E-value: 2.67e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   1 MQRTFAWLLDRVQHLGAP---VTLRASYLEIYNEQVRDLLSLGSPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQT 77
Cdd:cd00106   106 IPRALEDIFERIDKRKETkssFSVSASYLEIYNEKIYDLLSPVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  78 GLSRRRNSAHTLNQASSRSHALLTLYISRQTAQQmpsvdPGEPPVGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSL 157
Cdd:cd00106   186 GNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREK-----SGESVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSL 260

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370513726 158 LALGHCISLLLDPQRKqsHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQ 225
Cdd:cd00106   261 SALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
243-334 9.06e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 9.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726 243 QRLETEMLQLQEENRRLQFQLDQMdckasgLSGARVAWAQRnlygmLQEFMLENERLRKEKSQLQNSRDLAQNEQRILAQ 322
Cdd:COG4717   159 RELEEELEELEAELAELQEELEEL------LEQLSLATEEE-----LQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                          90
                  ....*....|..
gi 1370513726 323 QVHALERRLLSA 334
Cdd:COG4717   228 ELEQLENELEAA 239
 
Name Accession Description Interval E-value
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 1-225 2.67e-98

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: 296.09  E-value: 2.67e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   1 MQRTFAWLLDRVQHLGAP---VTLRASYLEIYNEQVRDLLSLGSPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQT 77
Cdd:cd00106   106 IPRALEDIFERIDKRKETkssFSVSASYLEIYNEKIYDLLSPVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  78 GLSRRRNSAHTLNQASSRSHALLTLYISRQTAQQmpsvdPGEPPVGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSL 157
Cdd:cd00106   186 GNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREK-----SGESVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSL 260

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370513726 158 LALGHCISLLLDPQRKqsHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQ 225
Cdd:cd00106   261 SALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
Kinesin pfam00225
Kinesin motor domain;
1-227 1.59e-95

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 288.70  E-value: 1.59e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   1 MQRTFAWLLDRVQHLGAPV--TLRASYLEIYNEQVRDLLSLG--SPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQ 76
Cdd:pfam00225 101 IPRALEDLFDRIQKTKERSefSVKVSYLEIYNEKIRDLLSPSnkNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQ 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  77 TGLSRRRNSAHTLNQASSRSHALLTLYISRQTAQQmpsvDPGEPPVGGKLCFVDLAGSEKVAATGSR-GELMLEANSINR 155
Cdd:pfam00225 181 LGNKNRTVAATKMNEESSRSHAIFTITVEQRNRST----GGEESVKTGKLNLVDLAGSERASKTGAAgGQRLKEAANINK 256

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370513726 156 SLLALGHCISLLLDPQrkQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRV 227
Cdd:pfam00225 257 SLSALGNVISALADKK--SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 1-232 4.50e-83

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: 257.50  E-value: 4.50e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726    1 MQRTFAWLLDRVQHLGAPV--TLRASYLEIYNEQVRDLLSlGSPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQTG 78
Cdd:smart00129 107 IPRALKDLFEKIDKREEGWqfSVKVSYLEIYNEKIRDLLN-PSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKG 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   79 LSRRRNSAHTLNQASSRSHALLTLYISrqtaqQMPSVDPGEPPVGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSLL 158
Cdd:smart00129 186 NKNRTVAATKMNEESSRSHAVFTITVE-----QKIKNSSSGSGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLS 260

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370513726  159 ALGHCISLLLDPQrKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRVTTRPQ 232
Cdd:smart00129 261 ALGNVINALAQHS-KSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPI 333
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
1-331 4.12e-56

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 193.80  E-value: 4.12e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   1 MQRTFAWLLDRVQHL--GAPVTLRASYLEIYNEQVRDLLSLGSPRPLpVRWNKTRGFYVEQLRVVEFGSLEALMELLQTG 78
Cdd:COG5059   117 IPLSLKELFSKLEDLsmTKDFAVSISYLEIYNEKIYDLLSPNEESLN-IREDSLLGVKVAGLTEKHVSSKEEILDLLRKG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  79 LSRRRNSAHTLNQASSRSHALLTLYISRQTAQQMPSVdpgeppvGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSLL 158
Cdd:COG5059   196 EKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSE-------TSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLL 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726 159 ALGHCISLLLDPqRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRVTTRPQApKSPV 238
Cdd:COG5059   269 TLGNVINALGDK-KKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQV-NSSS 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726 239 AKQPQRLET--EMLQLQEENRRLQFQLDQMDCKASGlsgarvawaqRNLYGMLQEFMLENERLrKEKSQLQNSRDLAQNE 316
Cdd:COG5059   347 DSSREIEEIkfDLSEDRSEIEILVFREQSQLSQSSL----------SGIFAYMQSLKKETETL-KSRIDLIMKSIISGTF 415

                         330
                  ....*....|....*
gi 1370513726 317 QRILAQQVHALERRL 331
Cdd:COG5059   416 ERKKLLKEEGWKYKS 430
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 22-294 2.02e-44

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 165.11  E-value: 2.02e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   22 RASYLEIYNEQVRDLLSlGSPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQTGLSRRRNSAHTLNQASSRSHALLT 101
Cdd:PLN03188   231 RCSFLEIYNEQITDLLD-PSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  102 LYIS---RQTAQQMPSVDPGeppvggKLCFVDLAGSEKVAATGSRGELMLEANSINRSLLALGHCISLLLDPQR--KQSH 176
Cdd:PLN03188   310 CVVEsrcKSVADGLSSFKTS------RINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRH 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  177 IPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRVTTRpqapkspvAKQPQRLETEMLQLQEEN 256
Cdd:PLN03188   384 IPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNK--------AVVNEVMQDDVNFLREVI 455

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1370513726  257 RRLQFQLDQMDCKASGLSGARVA----WAQRNLYGMLQEFML 294
Cdd:PLN03188   456 RQLRDELQRVKANGNNPTNPNVAystaWNARRSLNLLKSFGL 497
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
243-334 9.06e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 9.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726 243 QRLETEMLQLQEENRRLQFQLDQMdckasgLSGARVAWAQRnlygmLQEFMLENERLRKEKSQLQNSRDLAQNEQRILAQ 322
Cdd:COG4717   159 RELEEELEELEAELAELQEELEEL------LEQLSLATEEE-----LQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                          90
                  ....*....|..
gi 1370513726 323 QVHALERRLLSA 334
Cdd:COG4717   228 ELEQLENELEAA 239
 
Name Accession Description Interval E-value
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 1-225 2.67e-98

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: 296.09  E-value: 2.67e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   1 MQRTFAWLLDRVQHLGAP---VTLRASYLEIYNEQVRDLLSLGSPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQT 77
Cdd:cd00106   106 IPRALEDIFERIDKRKETkssFSVSASYLEIYNEKIYDLLSPVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  78 GLSRRRNSAHTLNQASSRSHALLTLYISRQTAQQmpsvdPGEPPVGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSL 157
Cdd:cd00106   186 GNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREK-----SGESVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSL 260

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370513726 158 LALGHCISLLLDPQRKqsHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQ 225
Cdd:cd00106   261 SALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
Kinesin pfam00225
Kinesin motor domain;
1-227 1.59e-95

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 288.70  E-value: 1.59e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   1 MQRTFAWLLDRVQHLGAPV--TLRASYLEIYNEQVRDLLSLG--SPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQ 76
Cdd:pfam00225 101 IPRALEDLFDRIQKTKERSefSVKVSYLEIYNEKIRDLLSPSnkNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQ 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  77 TGLSRRRNSAHTLNQASSRSHALLTLYISRQTAQQmpsvDPGEPPVGGKLCFVDLAGSEKVAATGSR-GELMLEANSINR 155
Cdd:pfam00225 181 LGNKNRTVAATKMNEESSRSHAIFTITVEQRNRST----GGEESVKTGKLNLVDLAGSERASKTGAAgGQRLKEAANINK 256

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370513726 156 SLLALGHCISLLLDPQrkQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRV 227
Cdd:pfam00225 257 SLSALGNVISALADKK--SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 1-232 4.50e-83

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: 257.50  E-value: 4.50e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726    1 MQRTFAWLLDRVQHLGAPV--TLRASYLEIYNEQVRDLLSlGSPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQTG 78
Cdd:smart00129 107 IPRALKDLFEKIDKREEGWqfSVKVSYLEIYNEKIRDLLN-PSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKG 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   79 LSRRRNSAHTLNQASSRSHALLTLYISrqtaqQMPSVDPGEPPVGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSLL 158
Cdd:smart00129 186 NKNRTVAATKMNEESSRSHAVFTITVE-----QKIKNSSSGSGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLS 260

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370513726  159 ALGHCISLLLDPQrKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRVTTRPQ 232
Cdd:smart00129 261 ALGNVINALAQHS-KSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPI 333
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 20-224 1.97e-68

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: 219.89  E-value: 1.97e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  20 TLRASYLEIYNEQVRDLLSLGSPR--PLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQTGLSRRRNSAHTLNQASSRSH 97
Cdd:cd01372   128 QLKVSFLEIYNEEIRDLLDPETDKkpTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSH 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  98 ALLTLYIsrqtaQQMPSVDPGEPPVGG--------KLCFVDLAGSEKVAATGSRGELMLEANSINRSLLALGHCISLLLD 169
Cdd:cd01372   208 AIFTITL-----EQTKKNGPIAPMSADdknstftsKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGD 282

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370513726 170 PQRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRA 224
Cdd:cd01372   283 ESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRA 337
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 1-224 6.91e-67

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: 216.06  E-value: 6.91e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   1 MQRTFAWLLDRVQHLGAP--VTLRASYLEIYNEQVRDLLSLGSpRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQTG 78
Cdd:cd01370   122 MVLTMKELFKRIESLKDEkeFEVSMSYLEIYNETIRDLLNPSS-GPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKG 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  79 LSRRRNSAHTLNQASSRSHALLTLYISrqtaQQMPSVDPGEPPVGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSLL 158
Cdd:cd01370   201 NRNRTQEPTDANATSSRSHAVLQITVR----QQDKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLL 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370513726 159 ALGHCISLLLDPQRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRA 224
Cdd:cd01370   277 ALGNCINALADPGKKNKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRA 342
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 20-228 4.41e-64

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: 208.22  E-value: 4.41e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  20 TLRASYLEIYNEQVRDLLS--LGSPRPLPVRWNKTRG-FYVEQLRVVEFGSLEALMELLQTGLSRRRNSAHTLNQASSRS 96
Cdd:cd01366   127 TIKASMLEIYNETIRDLLApgNAPQKKLEIRHDSEKGdTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  97 HALLTLYISR---QTAQQmpsvdpgeppVGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSLLALGHCISLLLdpqRK 173
Cdd:cd01366   207 HSVFILHISGrnlQTGEI----------SVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR---QK 273

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370513726 174 QSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRVT 228
Cdd:cd01366   274 QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCE 328
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 24-233 2.06e-62

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 204.89  E-value: 2.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  24 SYLEIYNEQVRDLLS---LGSPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQTGLSRRRNSAHTLNQASSRSHALL 100
Cdd:cd01365   146 SYMEIYNEKVRDLLNpkpKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVF 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726 101 TLyISRQTAQQMPSVDPGEppVGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSLLALGHCISLLLDPQR-----KQS 175
Cdd:cd01365   226 TI-VLTQKRHDAETNLTTE--KVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSS 302

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370513726 176 HIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRVTTRPQA 233
Cdd:cd01365   303 FIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVV 360
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 22-227 3.29e-59

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: 195.76  E-value: 3.29e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  22 RASYLEIYNEQVRDLLSLGSPRPLPVRWNKTRGFYVEQL---RVVEFGSLEALMELlqtGLSRRRNSAHTLNQASSRSHA 98
Cdd:cd01371   135 RVSYLEIYNEEIRDLLGKDQTKRLELKERPDTGVYVKDLsmfVVKNADEMEHVMNL---GNKNRSVGATNMNEDSSRSHA 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  99 LLTLYISRQTAqqmpsVDPGEPPVG-GKLCFVDLAGSEKVAATGSRGELMLEANSINRSLLALGHCISLLLDPqrKQSHI 177
Cdd:cd01371   212 IFTITIECSEK-----GEDGENHIRvGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHI 284

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370513726 178 PFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRV 227
Cdd:cd01371   285 PYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
1-331 4.12e-56

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 193.80  E-value: 4.12e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   1 MQRTFAWLLDRVQHL--GAPVTLRASYLEIYNEQVRDLLSLGSPRPLpVRWNKTRGFYVEQLRVVEFGSLEALMELLQTG 78
Cdd:COG5059   117 IPLSLKELFSKLEDLsmTKDFAVSISYLEIYNEKIYDLLSPNEESLN-IREDSLLGVKVAGLTEKHVSSKEEILDLLRKG 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  79 LSRRRNSAHTLNQASSRSHALLTLYISRQTAQQMPSVdpgeppvGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSLL 158
Cdd:COG5059   196 EKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSE-------TSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLL 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726 159 ALGHCISLLLDPqRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRVTTRPQApKSPV 238
Cdd:COG5059   269 TLGNVINALGDK-KKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQV-NSSS 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726 239 AKQPQRLET--EMLQLQEENRRLQFQLDQMDCKASGlsgarvawaqRNLYGMLQEFMLENERLrKEKSQLQNSRDLAQNE 316
Cdd:COG5059   347 DSSREIEEIkfDLSEDRSEIEILVFREQSQLSQSSL----------SGIFAYMQSLKKETETL-KSRIDLIMKSIISGTF 415

                         330
                  ....*....|....*
gi 1370513726 317 QRILAQQVHALERRL 331
Cdd:COG5059   416 ERKKLLKEEGWKYKS 430
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 3-232 1.76e-55

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: 186.38  E-value: 1.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   3 RTFAWLLDRVQHLGAPVTLRASYLEIYNEQVRDLLSLGSPRPLPVR----WNKTRGFYVEQLRVVEFGSLEALMELLQTG 78
Cdd:cd01364   123 RTLHQLFEKLEDNGTEYSVKVSYLEIYNEELFDLLSPSSDVSERLRmfddPRNKRGVIIKGLEEITVHNKDEVYQILEKG 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  79 LSRRRNSAHTLNQASSRSHAL--LTLYISRQTAQqmpsvdpGEPPVG-GKLCFVDLAGSEKVAATGSRGELMLEANSINR 155
Cdd:cd01364   203 AAKRKTAATLMNAQSSRSHSVfsITIHIKETTID-------GEELVKiGKLNLVDLAGSENIGRSGAVDKRAREAGNINQ 275

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370513726 156 SLLALGHCISLLLDpqrKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRVTTRPQ 232
Cdd:cd01364   276 SLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPE 349
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 20-227 4.98e-55

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: 184.46  E-value: 4.98e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  20 TLRASYLEIYNEQVRDLLSLgSPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQTGLSRRRNSAHTLNQASSRSHAL 99
Cdd:cd01369   128 HVKVSYFEIYMEKIRDLLDV-SKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSI 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726 100 LTLYI---SRQTAQQMpsvdpgeppvGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSLLALGHCISLLLDpqRKQSH 176
Cdd:cd01369   207 FLINVkqeNVETEKKK----------SGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD--GKKTH 274

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370513726 177 IPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRV 227
Cdd:cd01369   275 IPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 21-227 5.69e-55

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: 184.46  E-value: 5.69e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  21 LRASYLEIYNEQVRDLLSLGSpRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQTGLSRRRNSAHTLNQASSRSHALL 100
Cdd:cd01374   121 LRVSYLEIYNEKINDLLSPTS-QNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIF 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726 101 TLYISRQTAQQmpsvDPGEPPVGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSLLALGHCISLLLDpQRKQSHIPFR 180
Cdd:cd01374   200 RITIESSERGE----LEEGTVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYR 274

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370513726 181 DSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRV 227
Cdd:cd01374   275 DSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 1-223 7.66e-48

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: 166.22  E-value: 7.66e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   1 MQRTFAWLLDRVQHLgapVTLRASYLEIYNEQVRDLLS-----LGSPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELL 75
Cdd:cd01375   115 LQQVFRMIEERPTKA---YTVHVSYLEIYNEQLYDLLStlpyvGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  76 QTGLSRRRNSAHTLNQASSRSHALLTLYISrqtaqqMPSVDPG-EPPVGGKLCFVDLAGSEKVAATGSRGELMLEANSIN 154
Cdd:cd01375   192 FLGETNRIIASHTMNKNSSRSHCIFTIHLE------AHSRTLSsEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYIN 265

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370513726 155 RSLLALGHCISLLLDPQRkqSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASR 223
Cdd:cd01375   266 KSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASR 332
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 3-231 3.77e-46

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: 161.91  E-value: 3.77e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   3 RTFAWLLDRVQH------LGAPVTLRASYLEIYNEQVRDLLSLGSpRPLPVRWNKTRGFYVEQL--RVVEfgSLEALMEL 74
Cdd:cd01373   112 RIFEYLFSLIQRekekagEGKSFLCKCSFLEIYNEQIYDLLDPAS-RNLKLREDIKKGVYVENLveEYVT--SAEDVYQV 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  75 LQTGLSRRRNSAHTLNQASSRSHALLTLYI-SRQTAQQMPSVDPGeppvggKLCFVDLAGSEKVAATGSRGELMLEANSI 153
Cdd:cd01373   189 LSKGWSNRKVAATSMNRESSRSHAVFTCTIeSWEKKACFVNIRTS------RLNLVDLAGSERQKDTHAEGVRLKEAGNI 262

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370513726 154 NRSLLALGHCISLLLD-PQRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRVTTRP 231
Cdd:cd01373   263 NKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKA 341
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 23-223 8.56e-46

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: 160.54  E-value: 8.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  23 ASYLEIYNEQVRDLLSLGspRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQTGLSRRRNSAHTLNQASSRSHALLTL 102
Cdd:cd01367   139 VSFFEIYGGKVFDLLNRK--KRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQI 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726 103 YISRQTAQQMPsvdpgeppvgGKLCFVDLAGSEKVAATGSRG-ELMLEANSINRSLLALGHCISLLldpQRKQSHIPFRD 181
Cdd:cd01367   217 ILRDRGTNKLH----------GKLSFVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRAL---GQNKAHIPFRG 283

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370513726 182 SKLTKLLADSL-GGRGVTLMVACVSPSAQCLPETLSTLRYASR 223
Cdd:cd01367   284 SKLTQVLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADR 326
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 24-225 9.19e-46

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: 160.64  E-value: 9.19e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  24 SYLEIYNEQVRDLL-----SLGSPR-PLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQTGLSRRRNSAHTLNQASSRSH 97
Cdd:cd01368   135 SYIEIYNEYIYDLLepspsSPTKKRqSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSH 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  98 ALLTLYISR-QTAQQMPSVDPGEPPVGGKLCFVDLAGSEKVAATGSRGELMLEANSINRSLLALGHCISLLLDPQ--RKQ 174
Cdd:cd01368   215 SVFTIKLVQaPGDSDGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQlqGTN 294

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370513726 175 SHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQ 225
Cdd:cd01368   295 KMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 22-294 2.02e-44

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 165.11  E-value: 2.02e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   22 RASYLEIYNEQVRDLLSlGSPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQTGLSRRRNSAHTLNQASSRSHALLT 101
Cdd:PLN03188   231 RCSFLEIYNEQITDLLD-PSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  102 LYIS---RQTAQQMPSVDPGeppvggKLCFVDLAGSEKVAATGSRGELMLEANSINRSLLALGHCISLLLDPQR--KQSH 176
Cdd:PLN03188   310 CVVEsrcKSVADGLSSFKTS------RINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRH 383

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  177 IPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQRVTTRpqapkspvAKQPQRLETEMLQLQEEN 256
Cdd:PLN03188   384 IPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNK--------AVVNEVMQDDVNFLREVI 455

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1370513726  257 RRLQFQLDQMDCKASGLSGARVA----WAQRNLYGMLQEFML 294
Cdd:PLN03188   456 RQLRDELQRVKANGNNPTNPNVAystaWNARRSLNLLKSFGL 497
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 1-225 7.56e-41

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: 147.26  E-value: 7.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726   1 MQRTFAWLLDRVQHLGAPVTLRASYLEIYNEQVRDLLSlGSPRPLPVRWNKTRGFYVEQLRVVEFGSLEALMELLQTGlS 80
Cdd:cd01376   105 MPLTVMDLLQMTRKEAWALSFTMSYLEIYQEKILDLLE-PASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPA-S 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726  81 RRRNSAHT-LNQASSRSHALLTL-YISRQTAQQMPSVDpgeppvgGKLCFVDLAGSEKVAATGSRGELMLEANSINRSLL 158
Cdd:cd01376   183 KNRTVAATrLNDNSSRSHAVLLIkVDQRERLAPFRQRT-------GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLF 255

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370513726 159 ALGHCISLLLdpqRKQSHIPFRDSKLTKLLADSLGGRGVTLMVACVSPSAQCLPETLSTLRYASRAQ 225
Cdd:cd01376   256 VLSKVVNALN---KNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
243-334 9.06e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 9.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370513726 243 QRLETEMLQLQEENRRLQFQLDQMdckasgLSGARVAWAQRnlygmLQEFMLENERLRKEKSQLQNSRDLAQNEQRILAQ 322
Cdd:COG4717   159 RELEEELEELEAELAELQEELEEL------LEQLSLATEEE-----LQDLAEELEELQQRLAELEEELEEAQEELEELEE 227

                          90
                  ....*....|..
gi 1370513726 323 QVHALERRLLSA 334
Cdd:COG4717   228 ELEQLENELEAA 239
 
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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