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Conserved domains on  [gi|1039753697|ref|XP_017172991|]
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kinesin-like protein KIF6 isoform X2 [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 ...
 10-184 7.84e-104

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: 318.76  E-value: 7.84e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  10 LRKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSK--EPGSATVRHAKL 87
Cdd:cd01375   158 VTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHsrTLSSEKYITSKL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  88 HLVDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHRTHIPYRNSMMTSVLRDSLGGNCMTTMIATLSLEK 167
Cdd:cd01375   238 NLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEA 317

                         170
                  ....*....|....*..
gi 1039753697 168 RNIDESISTCRFAQRVA 184
Cdd:cd01375   318 AQLEETLSTLRFASRVK 334
 
Name Accession Description Interval E-value
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 10-184 7.84e-104

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: 318.76  E-value: 7.84e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  10 LRKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSK--EPGSATVRHAKL 87
Cdd:cd01375   158 VTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHsrTLSSEKYITSKL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  88 HLVDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHRTHIPYRNSMMTSVLRDSLGGNCMTTMIATLSLEK 167
Cdd:cd01375   238 NLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEA 317

                         170
                  ....*....|....*..
gi 1039753697 168 RNIDESISTCRFAQRVA 184
Cdd:cd01375   318 AQLEETLSTLRFASRVK 334
Kinesin pfam00225
Kinesin motor domain;
11-186 1.29e-67

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 223.99  E-value: 1.29e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  11 RKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSK---EPGSATVRHAKL 87
Cdd:pfam00225 147 RKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRnrsTGGEESVKTGKL 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  88 HLVDLAGSERVSKTGV-GGLLLTEAKYINLSLHYLEQVIIALSEKHRTHIPYRNSMMTSVLRDSLGGNCMTTMIATLSLE 166
Cdd:pfam00225 227 NLVDLAGSERASKTGAaGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPS 306

                         170       180
                  ....*....|....*....|
gi 1039753697 167 KRNIDESISTCRFAQRVALI 186
Cdd:pfam00225 307 SSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 6-193 8.96e-65

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: 216.67  E-value: 8.96e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697    6 YISLLRKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSAT--VR 83
Cdd:smart00129 145 LNPSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSgsGK 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697   84 HAKLHLVDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHR-THIPYRNSMMTSVLRDSLGGNCMTTMIAT 162
Cdd:smart00129 225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKsRHIPYRDSKLTRLLQDSLGGNSKTLMIAN 304

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1039753697  163 LSLEKRNIDESISTCRFAQRVALIKNEAILN 193
Cdd:smart00129 305 VSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
12-344 1.48e-44

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 167.61  E-value: 1.48e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  12 KVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSATVRHAKLHLVD 91
Cdd:COG5059   161 SLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETSKLSLVD 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  92 LAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHRT-HIPYRNSMMTSVLRDSLGGNCMTTMIATLSLEKRNI 170
Cdd:COG5059   241 LAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSgHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSF 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697 171 DESISTCRFAQRVALIKNEAILNEEIDP-------RLMIVRLQKEIEDLKAELAM-----ATGEQRTEALTEAELLQLEK 238
Cdd:COG5059   321 EETINTLKFASRAKSIKNKIQVNSSSDSsreieeiKFDLSEDRSEIEILVFREQSqlsqsSLSGIFAYMQSLKKETETLK 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697 239 LIASYLEDQDPESRLEVGADMRKIHHCFHHFKKLLNDKKTLENTVSSESTRQACQEPLRDEEYTKLLGLLKQRDNEINIL 318
Cdd:COG5059   401 SRIDLIMKSIISGTFERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSD 480

                         330       340
                  ....*....|....*....|....*.
gi 1039753697 319 VNMLKKEKKKTQDALQNSSLEKSDTR 344
Cdd:COG5059   481 RVESEKASKLRSSASTKLNLRSSRSH 506
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 11-221 1.75e-30

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 128.13  E-value: 1.75e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697   11 RKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTV----HLSSKEPGSATVRHAK 86
Cdd:PLN03188   251 KNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCvvesRCKSVADGLSSFKTSR 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697   87 LHLVDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHRT----HIPYRNSMMTSVLRDSLGGNCMTTMIAT 162
Cdd:PLN03188   331 INLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTgkqrHIPYRDSRLTFLLQESLGGNAKLAMVCA 410

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753697  163 LSLEKRNIDESISTCRFAQRVALIKNEAILNEEIDP-----RLMIVRLQKEIEDLKAELAMATG 221
Cdd:PLN03188   411 ISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDdvnflREVIRQLRDELQRVKANGNNPTN 474
 
Name Accession Description Interval E-value
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 10-184 7.84e-104

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: 318.76  E-value: 7.84e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  10 LRKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSK--EPGSATVRHAKL 87
Cdd:cd01375   158 VTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHsrTLSSEKYITSKL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  88 HLVDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHRTHIPYRNSMMTSVLRDSLGGNCMTTMIATLSLEK 167
Cdd:cd01375   238 NLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEA 317

                         170
                  ....*....|....*..
gi 1039753697 168 RNIDESISTCRFAQRVA 184
Cdd:cd01375   318 AQLEETLSTLRFASRVK 334
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 12-183 1.01e-67

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: 224.06  E-value: 1.01e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  12 KVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKE--PGSATVRHAKLHL 89
Cdd:cd00106   152 PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNreKSGESVTSSKLNL 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  90 VDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHRTHIPYRNSMMTSVLRDSLGGNCMTTMIATLSLEKRN 169
Cdd:cd00106   232 VDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSEN 311

                         170
                  ....*....|....
gi 1039753697 170 IDESISTCRFAQRV 183
Cdd:cd00106   312 FEETLSTLRFASRA 325
Kinesin pfam00225
Kinesin motor domain;
11-186 1.29e-67

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 223.99  E-value: 1.29e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  11 RKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSK---EPGSATVRHAKL 87
Cdd:pfam00225 147 RKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRnrsTGGEESVKTGKL 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  88 HLVDLAGSERVSKTGV-GGLLLTEAKYINLSLHYLEQVIIALSEKHRTHIPYRNSMMTSVLRDSLGGNCMTTMIATLSLE 166
Cdd:pfam00225 227 NLVDLAGSERASKTGAaGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPS 306

                         170       180
                  ....*....|....*....|
gi 1039753697 167 KRNIDESISTCRFAQRVALI 186
Cdd:pfam00225 307 SSNYEETLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 6-193 8.96e-65

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: 216.67  E-value: 8.96e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697    6 YISLLRKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSAT--VR 83
Cdd:smart00129 145 LNPSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSgsGK 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697   84 HAKLHLVDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHR-THIPYRNSMMTSVLRDSLGGNCMTTMIAT 162
Cdd:smart00129 225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKsRHIPYRDSKLTRLLQDSLGGNSKTLMIAN 304

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1039753697  163 LSLEKRNIDESISTCRFAQRVALIKNEAILN 193
Cdd:smart00129 305 VSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 12-186 1.79e-52

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: 183.30  E-value: 1.79e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  12 KVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSATVRHAKLHLVD 91
Cdd:cd01369   151 NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVD 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  92 LAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHRTHIPYRNSMMTSVLRDSLGGNCMTTMIATLSLEKRNID 171
Cdd:cd01369   231 LAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNES 310

                         170
                  ....*....|....*
gi 1039753697 172 ESISTCRFAQRVALI 186
Cdd:cd01369   311 ETLSTLRFGQRAKTI 325
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 3-182 3.93e-52

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: 182.66  E-value: 3.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697   3 RASYISLL-------------RKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFT 69
Cdd:cd01371   135 RVSYLEIYneeirdllgkdqtKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFT 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  70 VHLSSKEPGSATVRH---AKLHLVDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHRTHIPYRNSMMTSV 146
Cdd:cd01371   215 ITIECSEKGEDGENHirvGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTHIPYRDSKLTRL 294

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039753697 147 LRDSLGGNCMTTMIATLSLEKRNIDESISTCRFAQR 182
Cdd:cd01371   295 LQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANR 330
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 11-188 9.71e-50

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: 176.25  E-value: 9.71e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  11 RKVTILEDPDQN-IHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSATVRHAKLHL 89
Cdd:cd01366   152 KKLEIRHDSEKGdTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNL 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  90 VDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHRtHIPYRNSMMTSVLRDSLGGNCMTTMIATLSLEKRN 169
Cdd:cd01366   232 VDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS-HIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESN 310

                         170
                  ....*....|....*....
gi 1039753697 170 IDESISTCRFAQRVALIKN 188
Cdd:cd01366   311 LNETLNSLRFASKVNSCEL 329
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 11-194 4.07e-47

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: 169.61  E-value: 4.07e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  11 RKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGS--ATVRHAKLH 88
Cdd:cd01373   157 RNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKAcfVNIRTSRLN 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  89 LVDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSE----KHRtHIPYRNSMMTSVLRDSLGGNCMTTMIATLS 164
Cdd:cd01373   237 LVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvahgKQR-HVCYRDSKLTFLLRDSLGGNAKTAIIANVH 315

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039753697 165 LEKRNIDESISTCRFAQRVALIKNEAILNE 194
Cdd:cd01373   316 PSSKCFGETLSTLRFAQRAKLIKNKAVVNE 345
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 15-182 3.39e-45

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: 163.27  E-value: 3.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  15 ILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKE---PGSATVRHAKLHLVD 91
Cdd:cd01374   146 IRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSErgeLEEGTVRVSTLNLID 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  92 LAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSE-KHRTHIPYRNSMMTSVLRDSLGGNCMTTMIATLSLEKRNI 170
Cdd:cd01374   226 LAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEgKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHV 305

                         170
                  ....*....|..
gi 1039753697 171 DESISTCRFAQR 182
Cdd:cd01374   306 EETLNTLKFASR 317
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
12-344 1.48e-44

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 167.61  E-value: 1.48e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  12 KVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSATVRHAKLHLVD 91
Cdd:COG5059   161 SLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETSKLSLVD 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  92 LAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHRT-HIPYRNSMMTSVLRDSLGGNCMTTMIATLSLEKRNI 170
Cdd:COG5059   241 LAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSgHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSF 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697 171 DESISTCRFAQRVALIKNEAILNEEIDP-------RLMIVRLQKEIEDLKAELAM-----ATGEQRTEALTEAELLQLEK 238
Cdd:COG5059   321 EETINTLKFASRAKSIKNKIQVNSSSDSsreieeiKFDLSEDRSEIEILVFREQSqlsqsSLSGIFAYMQSLKKETETLK 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697 239 LIASYLEDQDPESRLEVGADMRKIHHCFHHFKKLLNDKKTLENTVSSESTRQACQEPLRDEEYTKLLGLLKQRDNEINIL 318
Cdd:COG5059   401 SRIDLIMKSIISGTFERKKLLKEEGWKYKSTLQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPEETSD 480

                         330       340
                  ....*....|....*....|....*.
gi 1039753697 319 VNMLKKEKKKTQDALQNSSLEKSDTR 344
Cdd:COG5059   481 RVESEKASKLRSSASTKLNLRSSRSH 506
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 17-193 8.73e-44

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: 160.60  E-value: 8.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  17 EDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHL----SSKEPGSATVRHAKLHLVDL 92
Cdd:cd01365   174 EHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLtqkrHDAETNLTTEKVSKISLVDL 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  93 AGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSE-------KHRTHIPYRNSMMTSVLRDSLGGNCMTTMIATLSL 165
Cdd:cd01365   254 AGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgkskKKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISP 333

                         170       180
                  ....*....|....*....|....*...
gi 1039753697 166 EKRNIDESISTCRFAQRVALIKNEAILN 193
Cdd:cd01365   334 ADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 13-187 1.75e-43

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: 159.42  E-value: 1.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  13 VTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHL------SSKEPGSATVRH-- 84
Cdd:cd01372   155 ISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqtkknGPIAPMSADDKNst 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  85 --AKLHLVDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHR--THIPYRNSMMTSVLRDSLGGNCMTTMI 160
Cdd:cd01372   235 ftSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKkgAHVPYRDSKLTRLLQDSLGGNSHTLMI 314

                         170       180
                  ....*....|....*....|....*..
gi 1039753697 161 ATLSLEKRNIDESISTCRFAQRVALIK 187
Cdd:cd01372   315 ACVSPADSNFEETLNTLKYANRARNIK 341
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 17-182 2.63e-43

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: 159.05  E-value: 2.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  17 EDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSA---TVRHAKLHLVDLA 93
Cdd:cd01370   171 EDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASinqQVRQGKLSLIDLA 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  94 GSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHR--THIPYRNSMMTSVLRDSLGGNCMTTMIATLSLEKRNID 171
Cdd:cd01370   251 GSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYE 330

                         170
                  ....*....|.
gi 1039753697 172 ESISTCRFAQR 182
Cdd:cd01370   331 ETHNTLKYANR 341
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 11-194 2.56e-39

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: 147.86  E-value: 2.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  11 RKVTILEDPDQ--NIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSAT---VRHA 85
Cdd:cd01364   165 ERLRMFDDPRNkrGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGeelVKIG 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  86 KLHLVDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEkHRTHIPYRNSMMTSVLRDSLGGNCMTTMIATLSL 165
Cdd:cd01364   245 KLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE-RAPHVPYRESKLTRLLQDSLGGRTKTSIIATISP 323

                         170       180
                  ....*....|....*....|....*....
gi 1039753697 166 EKRNIDESISTCRFAQRVALIKNEAILNE 194
Cdd:cd01364   324 ASVNLEETLSTLEYAHRAKNIKNKPEVNQ 352
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 11-221 1.75e-30

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 128.13  E-value: 1.75e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697   11 RKVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTV----HLSSKEPGSATVRHAK 86
Cdd:PLN03188   251 KNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCvvesRCKSVADGLSSFKTSR 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697   87 LHLVDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSEKHRT----HIPYRNSMMTSVLRDSLGGNCMTTMIAT 162
Cdd:PLN03188   331 INLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTgkqrHIPYRDSRLTFLLQESLGGNAKLAMVCA 410

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039753697  163 LSLEKRNIDESISTCRFAQRVALIKNEAILNEEIDP-----RLMIVRLQKEIEDLKAELAMATG 221
Cdd:PLN03188   411 ISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDdvnflREVIRQLRDELQRVKANGNNPTN 474
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 12-183 1.31e-27

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: 113.93  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  12 KVTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSAtvrHAKLHLVD 91
Cdd:cd01367   158 RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNKL---HGKLSFVD 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  92 LAGSERVSKTGVGG-LLLTEAKYINLSLHYLEQVIIALSEKHRtHIPYRNSMMTSVLRDSL-GGNCMTTMIATLSLEKRN 169
Cdd:cd01367   235 LAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKA-HIPFRGSKLTQVLKDSFiGENSKTCMIATISPGASS 313

                         170
                  ....*....|....
gi 1039753697 170 IDESISTCRFAQRV 183
Cdd:cd01367   314 CEHTLNTLRYADRV 327
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 13-182 2.39e-26

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: 109.90  E-value: 2.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  13 VTILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLSSKEPGSA-TVRHAKLHLVD 91
Cdd:cd01376   148 LVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPfRQRTGKLNLID 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  92 LAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSeKHRTHIPYRNSMMTSVLRDSLGGNCMTTMIATLSLEKRNID 171
Cdd:cd01376   228 LAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALN-KNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQ 306

                         170
                  ....*....|.
gi 1039753697 172 ESISTCRFAQR 182
Cdd:cd01376   307 DTLSTLNFAAR 317
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 15-180 1.85e-25

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: 107.86  E-value: 1.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  15 ILEDPDQNIHLKNLSLHQATTEEEALNLLFLGDTNRMIAETPMNQASTRSHCIFTVHLsSKEPGSAT---------VRHA 85
Cdd:cd01368   164 LREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKL-VQAPGDSDgdvdqdkdqITVS 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039753697  86 KLHLVDLAGSERVSKTGVGGLLLTEAKYINLSLHYLEQVIIALSE----KHRTHIPYRNSMMTSVLRDSLGGNCMTTMIA 161
Cdd:cd01368   243 QLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLREnqlqGTNKMVPFRDSKLTHLFQNYFDGEGKASMIV 322

                         170
                  ....*....|....*....
gi 1039753697 162 TLSLEKRNIDESISTCRFA 180
Cdd:cd01368   323 NVNPCASDYDETLHVMKFS 341
 
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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