NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039766357|ref|XP_017175402|]
View 

kinesin-like protein KIF24 isoform X3 [Mus musculus]

Protein Classification

kinesin family protein( domain architecture ID 10175948)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 201-373 1.82e-95

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 cd01367:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 328  Bit Score: 308.07  E-value: 1.82e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  201 HSCVRLFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIKDSAK-RTFGRISFI 279
Cdd:cd01367    154 NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTnKLHGKLSFV 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  280 DLAGSERAADARDSDRQTKMEGAEINQSLLALKECIRALDQEHTHTPFRQSKLTQVLKDSFIGN-AKTCMIANISPSHIA 358
Cdd:cd01367    234 DLAGSERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGASS 313

                          170
                   ....*....|....*
gi 1039766357  359 TEHTLNTLRYADRVK 373
Cdd:cd01367    314 CEHTLNTLRYADRVK 328
SAM_KIF24-like cd09541
SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a ...
 3-62 9.49e-28

SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a putative protein-protein interaction domain. This subfamily includes proteins related to human kinesin-like protein KIF24. SAM domain is located at the N-terminus followed by kinesin motor domain. Kinesins are proteins involved in a number of different cell processes including microtubule dynamics and axonal transport. Kinesins of this group belong to N-type; they drive microtubule plus end-directed transport. SAM apparently plays the role of adaptor or scaffold domain. In many cases SAM is known as a mediator of dimerization/oligomerization.


:

Pssm-ID: 188940  Cd Length: 60  Bit Score: 106.61  E-value: 9.49e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357    3 SWLYECLCEAELAQYYPHFTALGLQKIDELAKVTMKDYSRLGVHDMNDRKRLFQLIKIIK 62
Cdd:cd09541      1 SVLYEWLEEAGLQHYYPAFAAGGVTSIEALAQLTMQDYASLGVQDMEDKQKLFRLIQTLK 60
 
Name Accession Description Interval E-value
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 201-373 1.82e-95

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: 308.07  E-value: 1.82e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  201 HSCVRLFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIKDSAK-RTFGRISFI 279
Cdd:cd01367    154 NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTnKLHGKLSFV 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  280 DLAGSERAADARDSDRQTKMEGAEINQSLLALKECIRALDQEHTHTPFRQSKLTQVLKDSFIGN-AKTCMIANISPSHIA 358
Cdd:cd01367    234 DLAGSERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGASS 313

                          170
                   ....*....|....*
gi 1039766357  359 TEHTLNTLRYADRVK 373
Cdd:cd01367    314 CEHTLNTLRYADRVK 328
Kinesin pfam00225
Kinesin motor domain;
200-374 1.28e-67

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 230.92  E-value: 1.28e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  200 PHSCVRLFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQI-------KDSAKRT 272
Cdd:pfam00225  143 NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVeqrnrstGGEESVK 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  273 FGRISFIDLAGSERAADARDSDRQTKMEGAEINQSLLALKECIRALDQEH-THTPFRQSKLTQVLKDSFIGNAKTCMIAN 351
Cdd:pfam00225  223 TGKLNLVDLAGSERASKTGAAGGQRLKEAANINKSLSALGNVISALADKKsKHIPYRDSKLTRLLQDSLGGNSKTLMIAN 302

                          170       180
                   ....*....|....*....|...
gi 1039766357  352 ISPSHIATEHTLNTLRYADRVKE 374
Cdd:pfam00225  303 ISPSSSNYEETLSTLRFASRAKN 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 209-380 1.46e-64

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: 222.45  E-value: 1.46e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357   209 REDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIKDSAK------RTFGRISFIDLA 282
Cdd:smart00129  155 REDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKnsssgsGKASKLNLVDLA 234

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357   283 GSERAADARdSDRQTKMEGAEINQSLLALKECIRALDQE--HTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHIATE 360
Cdd:smart00129  235 GSERAKKTG-AEGDRLKEAGNINKSLSALGNVINALAQHskSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLE 313

                           170       180
                    ....*....|....*....|
gi 1039766357   361 HTLNTLRYADRVKELKKGVK 380
Cdd:smart00129  314 ETLSTLRFASRAKEIKNKPI 333
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
205-377 4.67e-41

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 160.29  E-value: 4.67e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  205 RLFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQI----KDSAKRTFGRISFID 280
Cdd:COG5059    161 SLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELasknKVSGTSETSKLSLVD 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  281 LAGSERAADARDsdRQTKM-EGAEINQSLLALKECIRAL--DQEHTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHI 357
Cdd:COG5059    241 LAGSERAARTGN--RGTRLkEGASINKSLLTLGNVINALgdKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSN 318

                          170       180
                   ....*....|....*....|
gi 1039766357  358 ATEHTLNTLRYADRVKELKK 377
Cdd:COG5059    319 SFEETINTLKFASRAKSIKN 338
SAM_KIF24-like cd09541
SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a ...
 3-62 9.49e-28

SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a putative protein-protein interaction domain. This subfamily includes proteins related to human kinesin-like protein KIF24. SAM domain is located at the N-terminus followed by kinesin motor domain. Kinesins are proteins involved in a number of different cell processes including microtubule dynamics and axonal transport. Kinesins of this group belong to N-type; they drive microtubule plus end-directed transport. SAM apparently plays the role of adaptor or scaffold domain. In many cases SAM is known as a mediator of dimerization/oligomerization.


Pssm-ID: 188940  Cd Length: 60  Bit Score: 106.61  E-value: 9.49e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357    3 SWLYECLCEAELAQYYPHFTALGLQKIDELAKVTMKDYSRLGVHDMNDRKRLFQLIKIIK 62
Cdd:cd09541      1 SVLYEWLEEAGLQHYYPAFAAGGVTSIEALAQLTMQDYASLGVQDMEDKQKLFRLIQTLK 60
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 206-376 1.24e-23

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 108.48  E-value: 1.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  206 LFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIKDSAKRTFG--------RIS 277
Cdd:PLN03188   253 LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADglssfktsRIN 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  278 FIDLAGSERAADARDSDRQTKmEGAEINQSLLALKECIRALDQ-----EHTHTPFRQSKLTQVLKDSFIGNAKTCMIANI 352
Cdd:PLN03188   333 LVDLAGSERQKLTGAAGDRLK-EAGNINRSLSQLGNLINILAEisqtgKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAI 411

                          170       180
                   ....*....|....*....|....
gi 1039766357  353 SPSHIATEHTLNTLRYADRVKELK 376
Cdd:PLN03188   412 SPSQSCKSETFSTLRFAQRAKAIK 435
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
14-62 7.06e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 36.09  E-value: 7.06e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1039766357   14 LAQYYPHFTALGLQKIDELAKVTMKDYSRLGVHDMNDRKRLFQLIKIIK 62
Cdd:pfam07647   18 LEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
 
Name Accession Description Interval E-value
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 201-373 1.82e-95

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: 308.07  E-value: 1.82e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  201 HSCVRLFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIKDSAK-RTFGRISFI 279
Cdd:cd01367    154 NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTnKLHGKLSFV 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  280 DLAGSERAADARDSDRQTKMEGAEINQSLLALKECIRALDQEHTHTPFRQSKLTQVLKDSFIGN-AKTCMIANISPSHIA 358
Cdd:cd01367    234 DLAGSERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGASS 313

                          170
                   ....*....|....*
gi 1039766357  359 TEHTLNTLRYADRVK 373
Cdd:cd01367    314 CEHTLNTLRYADRVK 328
Kinesin pfam00225
Kinesin motor domain;
200-374 1.28e-67

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 230.92  E-value: 1.28e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  200 PHSCVRLFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQI-------KDSAKRT 272
Cdd:pfam00225  143 NKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVeqrnrstGGEESVK 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  273 FGRISFIDLAGSERAADARDSDRQTKMEGAEINQSLLALKECIRALDQEH-THTPFRQSKLTQVLKDSFIGNAKTCMIAN 351
Cdd:pfam00225  223 TGKLNLVDLAGSERASKTGAAGGQRLKEAANINKSLSALGNVISALADKKsKHIPYRDSKLTRLLQDSLGGNSKTLMIAN 302

                          170       180
                   ....*....|....*....|...
gi 1039766357  352 ISPSHIATEHTLNTLRYADRVKE 374
Cdd:pfam00225  303 ISPSSSNYEETLSTLRFASRAKN 325
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 209-380 1.46e-64

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: 222.45  E-value: 1.46e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357   209 REDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIKDSAK------RTFGRISFIDLA 282
Cdd:smart00129  155 REDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKnsssgsGKASKLNLVDLA 234

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357   283 GSERAADARdSDRQTKMEGAEINQSLLALKECIRALDQE--HTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHIATE 360
Cdd:smart00129  235 GSERAKKTG-AEGDRLKEAGNINKSLSALGNVINALAQHskSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLE 313

                           170       180
                    ....*....|....*....|
gi 1039766357   361 HTLNTLRYADRVKELKKGVK 380
Cdd:smart00129  314 ETLSTLRFASRAKEIKNKPI 333
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 188-373 8.89e-60

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: 208.26  E-value: 8.89e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  188 RVSHVSGYNYGI-----PHSCVRLFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQ 262
Cdd:cd00106    130 SASYLEIYNEKIydllsPVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFT 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  263 IQIK------DSAKRTFGRISFIDLAGSERAADARdSDRQTKMEGAEINQSLLALKECIRAL-DQEHTHTPFRQSKLTQV 335
Cdd:cd00106    210 IHVKqrnrekSGESVTSSKLNLVDLAGSERAKKTG-AEGDRLKEGGNINKSLSALGKVISALaDGQNKHIPYRDSKLTRL 288

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1039766357  336 LKDSFIGNAKTCMIANISPSHIATEHTLNTLRYADRVK 373
Cdd:cd00106    289 LQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 209-375 7.07e-56

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: 197.95  E-value: 7.07e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  209 REDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIKDSAKR-------TFGRISFIDL 281
Cdd:cd01370    170 REDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTasinqqvRQGKLSLIDL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  282 AGSERAADARDsdRQTKM-EGAEINQSLLALKECIRALDQEH---THTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHI 357
Cdd:cd01370    250 AGSERASATNN--RGQRLkEGANINRSLLALGNCINALADPGkknKHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSS 327

                          170
                   ....*....|....*...
gi 1039766357  358 ATEHTLNTLRYADRVKEL 375
Cdd:cd01370    328 SYEETHNTLKYANRAKNI 345
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 209-376 8.92e-45

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: 165.58  E-value: 8.92e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  209 REDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIK-------------DSAKRTF-G 274
Cdd:cd01372    158 REDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEqtkkngpiapmsaDDKNSTFtS 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  275 RISFIDLAGSERAADARDSDRQTKmEGAEINQSLLALKECIRAL---DQEHTHTPFRQSKLTQVLKDSFIGNAKTCMIAN 351
Cdd:cd01372    238 KFHFVDLAGSERLKRTGATGDRLK-EGISINSGLLALGNVISALgdeSKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIAC 316

                          170       180
                   ....*....|....*....|....*
gi 1039766357  352 ISPSHIATEHTLNTLRYADRVKELK 376
Cdd:cd01372    317 VSPADSNFEETLNTLKYANRARNIK 341
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 174-375 1.78e-44

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: 164.04  E-value: 1.78e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  174 FSPQLGNCDIPVIQRVSHVSGYNYGI-----PHScVRLFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGAT 248
Cdd:cd01374    108 FSKIQDTPDREFLLRVSYLEIYNEKIndllsPTS-QNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGET 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  249 GVNADSSRSHAIIQIQIKDSAKR-------TFGRISFIDLAGSERAADARDSDRQTKmEGAEINQSLLALKECIRAL--D 319
Cdd:cd01374    187 DMNERSSRSHTIFRITIESSERGeleegtvRVSTLNLIDLAGSERAAQTGAAGVRRK-EGSHINKSLLTLGTVISKLseG 265

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039766357  320 QEHTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHIATEHTLNTLRYADRVKEL 375
Cdd:cd01374    266 KVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 209-376 1.30e-42

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 158.91  E-value: 1.30e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  209 REDS-KHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQI----KDSAKRTFGRISFIDLAG 283
Cdd:cd01366    157 RHDSeKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHIsgrnLQTGEISVGKLNLVDLAG 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  284 SERAADARDSDRQTKmEGAEINQSLLALKECIRALDQEHTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHIATEHTL 363
Cdd:cd01366    237 SERLNKSGATGDRLK-ETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETL 315

                          170
                   ....*....|...
gi 1039766357  364 NTLRYADRVKELK 376
Cdd:cd01366    316 NSLRFASKVNSCE 328
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
205-377 4.67e-41

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 160.29  E-value: 4.67e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  205 RLFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQI----KDSAKRTFGRISFID 280
Cdd:COG5059    161 SLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELasknKVSGTSETSKLSLVD 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  281 LAGSERAADARDsdRQTKM-EGAEINQSLLALKECIRAL--DQEHTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHI 357
Cdd:COG5059    241 LAGSERAARTGN--RGTRLkEGASINKSLLTLGNVINALgdKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSN 318

                          170       180
                   ....*....|....*....|
gi 1039766357  358 ATEHTLNTLRYADRVKELKK 377
Cdd:COG5059    319 SFEETINTLKFASRAKSIKN 338
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 220-376 6.66e-41

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: 154.82  E-value: 6.66e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  220 GLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIKDSAKRTFG--------RISFIDLAGSERAADAR 291
Cdd:cd01365    184 DLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETnlttekvsKISLVDLAGSERASSTG 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  292 DSDRQTKmEGAEINQSLLALKECIRALDQEHTHT--------PFRQSKLTQVLKDSFIGNAKTCMIANISPSHIATEHTL 363
Cdd:cd01365    264 ATGDRLK-EGANINKSLTTLGKVISALADMSSGKskkkssfiPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETL 342

                          170
                   ....*....|...
gi 1039766357  364 NTLRYADRVKELK 376
Cdd:cd01365    343 STLRYADRAKKIV 355
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 188-373 8.35e-40

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: 151.07  E-value: 8.35e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  188 RVSHVSGYNYGI-----PHSCVRLFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQ 262
Cdd:cd01371    135 RVSYLEIYNEEIrdllgKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFT 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  263 IQIKDSAKR-------TFGRISFIDLAGSERAADARDSDRQTKmEGAEINQSLLALKECIRAL-DQEHTHTPFRQSKLTQ 334
Cdd:cd01371    215 ITIECSEKGedgenhiRVGKLNLVDLAGSERQSKTGATGERLK-EATKINLSLSALGNVISALvDGKSTHIPYRDSKLTR 293

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1039766357  335 VLKDSFIGNAKTCMIANISPSHIATEHTLNTLRYADRVK 373
Cdd:cd01371    294 LLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAK 332
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 205-376 1.24e-38

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: 148.24  E-value: 1.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  205 RLFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAI--IQIQIKDSAKRT-----FGRIS 277
Cdd:cd01364    168 RMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVfsITIHIKETTIDGeelvkIGKLN 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  278 FIDLAGSERAADARDSDRQTKmEGAEINQSLLALKECIRALDQEHTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHI 357
Cdd:cd01364    248 LVDLAGSENIGRSGAVDKRAR-EAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSIIATISPASV 326

                          170
                   ....*....|....*....
gi 1039766357  358 ATEHTLNTLRYADRVKELK 376
Cdd:cd01364    327 NLEETLSTLEYAHRAKNIK 345
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 204-373 1.64e-38

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: 146.71  E-value: 1.64e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  204 VRLFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIK-----DSAKRTfGRISF 278
Cdd:cd01369    150 TNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKqenveTEKKKS-GKLYL 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  279 IDLAGSERAaDARDSDRQTKMEGAEINQSLLALKECIRAL-DQEHTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHI 357
Cdd:cd01369    229 VDLAGSEKV-SKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSY 307

                          170
                   ....*....|....*.
gi 1039766357  358 ATEHTLNTLRYADRVK 373
Cdd:cd01369    308 NESETLSTLRFGQRAK 323
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 209-369 2.35e-37

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: 144.07  E-value: 2.35e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  209 REDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQI------------KDSAKRTFGRI 276
Cdd:cd01368    165 REDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLvqapgdsdgdvdQDKDQITVSQL 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  277 SFIDLAGSERAADARDSDRQTKmEGAEINQSLLALKECIRALDQEHT-----HTPFRQSKLTQVLKDSFIGNAKTCMIAN 351
Cdd:cd01368    245 SLVDLAGSERTSRTQNTGERLK-EAGNINTSLMTLGTCIEVLRENQLqgtnkMVPFRDSKLTHLFQNYFDGEGKASMIVN 323

                          170
                   ....*....|....*...
gi 1039766357  352 ISPSHIATEHTLNTLRYA 369
Cdd:cd01368    324 VNPCASDYDETLHVMKFS 341
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 206-376 7.92e-33

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: 131.09  E-value: 7.92e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  206 LFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIKDSAKRT------FGRISFI 279
Cdd:cd01373    159 LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKAcfvnirTSRLNLV 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  280 DLAGSERAADArDSDRQTKMEGAEINQSLLALKECIRALDQ----EHTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPS 355
Cdd:cd01373    239 DLAGSERQKDT-HAEGVRLKEAGNINKSLSCLGHVINALVDvahgKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPS 317

                          170       180
                   ....*....|....*....|.
gi 1039766357  356 HIATEHTLNTLRYADRVKELK 376
Cdd:cd01373    318 SKCFGETLSTLRFAQRAKLIK 338
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 210-373 5.48e-30

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: 122.30  E-value: 5.48e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  210 EDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIK------DSAKRTFGRISFIDLAG 283
Cdd:cd01375    165 EDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEahsrtlSSEKYITSKLNLVDLAG 244

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  284 SERAADArDSDRQTKMEGAEINQSLLALKECIRAL-DQEHTHTPFRQSKLTQVLKDSFIGNAKTCMIANIS--PSHIatE 360
Cdd:cd01375    245 SERLSKT-GVEGQVLKEATYINKSLSFLEQAIIALsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYgeAAQL--E 321

                          170
                   ....*....|...
gi 1039766357  361 HTLNTLRYADRVK 373
Cdd:cd01375    322 ETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 209-373 1.27e-29

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: 120.69  E-value: 1.27e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  209 REDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIKDSAKRTF-----GRISFIDLAG 283
Cdd:cd01376    151 REDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPfrqrtGKLNLIDLAG 230

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  284 SEraaDARDSDRQTK--MEGAEINQSLLALKECIRALDQEHTHTPFRQSKLTQVLKDSFIGNAKTCMIANISPSHIATEH 361
Cdd:cd01376    231 SE---DNRRTGNEGIrlKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQD 307

                          170
                   ....*....|..
gi 1039766357  362 TLNTLRYADRVK 373
Cdd:cd01376    308 TLSTLNFAARSR 319
SAM_KIF24-like cd09541
SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a ...
 3-62 9.49e-28

SAM domain of KIF24-like subfamily; SAM (sterile alpha motif) domain of KIF24 subfamily is a putative protein-protein interaction domain. This subfamily includes proteins related to human kinesin-like protein KIF24. SAM domain is located at the N-terminus followed by kinesin motor domain. Kinesins are proteins involved in a number of different cell processes including microtubule dynamics and axonal transport. Kinesins of this group belong to N-type; they drive microtubule plus end-directed transport. SAM apparently plays the role of adaptor or scaffold domain. In many cases SAM is known as a mediator of dimerization/oligomerization.


Pssm-ID: 188940  Cd Length: 60  Bit Score: 106.61  E-value: 9.49e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357    3 SWLYECLCEAELAQYYPHFTALGLQKIDELAKVTMKDYSRLGVHDMNDRKRLFQLIKIIK 62
Cdd:cd09541      1 SVLYEWLEEAGLQHYYPAFAAGGVTSIEALAQLTMQDYASLGVQDMEDKQKLFRLIQTLK 60
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 206-376 1.24e-23

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 108.48  E-value: 1.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  206 LFAREDSKHVVQIAGLRELQVDSVELLLQVILKGSKERSTGATGVNADSSRSHAIIQIQIKDSAKRTFG--------RIS 277
Cdd:PLN03188   253 LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADglssfktsRIN 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039766357  278 FIDLAGSERAADARDSDRQTKmEGAEINQSLLALKECIRALDQ-----EHTHTPFRQSKLTQVLKDSFIGNAKTCMIANI 352
Cdd:PLN03188   333 LVDLAGSERQKLTGAAGDRLK-EAGNINRSLSQLGNLINILAEisqtgKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAI 411

                          170       180
                   ....*....|....*....|....
gi 1039766357  353 SPSHIATEHTLNTLRYADRVKELK 376
Cdd:PLN03188   412 SPSQSCKSETFSTLRFAQRAKAIK 435
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 4-59 2.41e-06

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 45.69  E-value: 2.41e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039766357    4 WLYECLCEAELAQYYPHFTAlglQKIDE--LAKVTMKDYSRLGVHDMNDRKRLFQLIK 59
Cdd:cd09487      1 DVAEWLESLGLEQYADLFRK---NEIDGdaLLLLTDEDLKELGITSPGHRKKILRAIQ 55
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
14-62 7.06e-03

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 36.09  E-value: 7.06e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1039766357   14 LAQYYPHFTALGLQKIDELAKVTMKDYSRLGVHDMNDRKRLFQLIKIIK 62
Cdd:pfam07647   18 LEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH