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Conserved domains on  [gi|372266148|ref|NP_001243199|]
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kinesin-like protein KIF22 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 1-298 0e+00

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: 527.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148   1 MDSCSLEIANWRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIP 80
Cdd:cd01376   27 IDSCSVELADPRNHGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMP 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  81 RALMDLLQLTREEGaegrpWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPA 160
Cdd:cd01376  107 LTVMDLLQMTRKEA-----WALSFTMSYLEIYQEKILDLLEPASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPA 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 161 SRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVV 240
Cdd:cd01376  182 SKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVV 261

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 372266148 241 DALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSK 298
Cdd:cd01376  262 NALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
ComEA COG1555
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ...
 528-578 1.17e-12

DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair];


:

Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 63.34  E-value: 1.17e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 372266148 528 LNEGSARDLRSLQRIGPKKAQLIVGWRELHGPFSQVEDLERVEGITGKQME 578
Cdd:COG1555   15 INTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVEDLLEVKGIGPKTLE 65
 
Name Accession Description Interval E-value
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 1-298 0e+00

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: 527.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148   1 MDSCSLEIANWRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIP 80
Cdd:cd01376   27 IDSCSVELADPRNHGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMP 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  81 RALMDLLQLTREEGaegrpWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPA 160
Cdd:cd01376  107 LTVMDLLQMTRKEA-----WALSFTMSYLEIYQEKILDLLEPASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPA 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 161 SRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVV 240
Cdd:cd01376  182 SKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVV 261

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 372266148 241 DALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSK 298
Cdd:cd01376  262 NALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 2-307 1.75e-140

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: 410.81  E-value: 1.75e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148     2 DSCSLEIANWRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPR 81
Cdd:smart00129  30 VGKTLTVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPR 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148    82 ALMDLLQLTREEGAEgrpWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPAS 161
Cdd:smart00129 110 ALKDLFEKIDKREEG---WQFSVKVSYLEIYNEKIRDLLNPSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGN 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148   162 RNRTVGATRLNQRSSRSHAVLLVKVDQRER-LAPFRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVV 240
Cdd:smart00129 187 KNRTVAATKMNEESSRSHAVFTITVEQKIKnSSSGSGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVI 266

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372266148   241 DAL--NQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTN 307
Cdd:smart00129 267 NALaqHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
1-300 6.95e-122

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 363.05  E-value: 6.95e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148    1 MDSCSLEIANWRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIP 80
Cdd:pfam00225  23 VDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIP 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148   81 RALMDLLQLTREEGAEgrpWALSVTMSYLEIYQEKVLDLLDPA---SGDLVIREDCRGNILIPGLSQKPISSFADFERHF 157
Cdd:pfam00225 103 RALEDLFDRIQKTKER---SEFSVKVSYLEIYNEKIRDLLSPSnknKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  158 LPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQ--REGKLYLIDLAGSEDNRRTGN-KGLRLKESGAINTSLF 234
Cdd:pfam00225 180 QLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEEsvKTGKLNLVDLAGSERASKTGAaGGQRLKEAANINKSLS 259

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372266148  235 VLGKVVDALNQG-LPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEV 300
Cdd:pfam00225 260 ALGNVISALADKkSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
11-311 1.18e-77

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 256.59  E-value: 1.18e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  11 WRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLT 90
Cdd:COG5059   49 SLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  91 REEGAEGRpwaLSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVGATR 170
Cdd:COG5059  129 EDLSMTKD---FAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTE 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 171 LNQRSSRSHAVLLVKVDQRERLAPFRqREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDAL--NQGLP 248
Cdd:COG5059  206 INDESSRSHSIFQIELASKNKVSGTS-ETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALgdKKKSG 284

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 372266148 249 RVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTNESLQ 311
Cdd:COG5059  285 HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSD 347
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 20-311 1.85e-51

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 191.30  E-value: 1.85e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148   20 YQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLG----------SPEQPGVIPRALMDLLQL 89
Cdd:PLN03188  134 FTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERLFAR 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148   90 TREEGAE--GRPWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVG 167
Cdd:PLN03188  214 INEEQIKhaDRQLKYQCRCSFLEIYNEQITDLLDPSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTG 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  168 ATRLNQRSSRSHAVLLVKVDQR-----ERLAPFRQreGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDA 242
Cdd:PLN03188  294 ATSINAESSRSHSVFTCVVESRcksvaDGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINI 371

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372266148  243 LNQ----GLPR-VPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTNESLQ 311
Cdd:PLN03188  372 LAEisqtGKQRhIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQ 445
ComEA COG1555
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ...
 528-578 1.17e-12

DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair];


Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 63.34  E-value: 1.17e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 372266148 528 LNEGSARDLRSLQRIGPKKAQLIVGWRELHGPFSQVEDLERVEGITGKQME 578
Cdd:COG1555   15 INTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVEDLLEVKGIGPKTLE 65
HHH_3 pfam12836
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.
 528-581 2.78e-09

Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.


Pssm-ID: 463723 [Multi-domain]  Cd Length: 62  Bit Score: 53.25  E-value: 2.78e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 372266148  528 LNEGSARDLRSLQRIGPKKAQLIVGWRELHGPFSQVEDLERVEGITGK---QMESFL 581
Cdd:pfam12836   6 INTASAELLSRVPGLGPKLAKNIVEYREENGPFRSREDLLKVKGLGPKtfeQLAGFL 62
TIGR00426 TIGR00426
competence protein ComEA helix-hairpin-helix repeat region; Members of the subfamily ...
 528-578 2.24e-08

competence protein ComEA helix-hairpin-helix repeat region; Members of the subfamily recognized by this model include competence protein ComEA and closely related proteins from a number of species that exhibit competence for transformation by exongenous DNA, including Streptococcus pneumoniae, Bacillus subtilis, Neisseria meningitidis, and Haemophilus influenzae. This model represents a region of two tandem copies of a helix-hairpin-helix domain (pfam00633), each about 30 residues in length. Limited sequence similarity can be found among some members of this family N-terminal to the region covered by this model. [Cellular processes, DNA transformation]


Pssm-ID: 129520 [Multi-domain]  Cd Length: 69  Bit Score: 51.08  E-value: 2.24e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 372266148  528 LNEGSARDL-RSLQRIGPKKAQLIVGWRELHGPFSQVEDLERVEGITGKQME 578
Cdd:TIGR00426  10 INTATAEELqRAMNGVGLKKAEAIVSYREEYGPFKTVEDLKQVPGIGNSLVE 61
 
Name Accession Description Interval E-value
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 1-298 0e+00

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: 527.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148   1 MDSCSLEIANWRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIP 80
Cdd:cd01376   27 IDSCSVELADPRNHGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMP 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  81 RALMDLLQLTREEGaegrpWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPA 160
Cdd:cd01376  107 LTVMDLLQMTRKEA-----WALSFTMSYLEIYQEKILDLLEPASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPA 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 161 SRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVV 240
Cdd:cd01376  182 SKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVV 261

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 372266148 241 DALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSK 298
Cdd:cd01376  262 NALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 2-307 1.75e-140

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: 410.81  E-value: 1.75e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148     2 DSCSLEIANWRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPR 81
Cdd:smart00129  30 VGKTLTVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPR 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148    82 ALMDLLQLTREEGAEgrpWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPAS 161
Cdd:smart00129 110 ALKDLFEKIDKREEG---WQFSVKVSYLEIYNEKIRDLLNPSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGN 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148   162 RNRTVGATRLNQRSSRSHAVLLVKVDQRER-LAPFRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVV 240
Cdd:smart00129 187 KNRTVAATKMNEESSRSHAVFTITVEQKIKnSSSGSGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVI 266

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372266148   241 DAL--NQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTN 307
Cdd:smart00129 267 NALaqHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 2-298 1.35e-132

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: 390.46  E-value: 1.35e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148   2 DSCSLEIANWRN-HQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGS-PEQPGVI 79
Cdd:cd00106   27 GGKSVVLDPPKNrVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPdPEQRGII 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  80 PRALMDLLQLTREEGAEGrpWALSVTMSYLEIYQEKVLDLLDPA-SGDLVIREDCRGNILIPGLSQKPISSFADFERHFL 158
Cdd:cd00106  107 PRALEDIFERIDKRKETK--SSFSVSASYLEIYNEKIYDLLSPVpKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLD 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 159 PASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLA-PFRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLG 237
Cdd:cd00106  185 AGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKsGESVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALG 264

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 372266148 238 KVVDALNQG-LPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSK 298
Cdd:cd00106  265 KVISALADGqNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
Kinesin pfam00225
Kinesin motor domain;
1-300 6.95e-122

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 363.05  E-value: 6.95e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148    1 MDSCSLEIANWRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIP 80
Cdd:pfam00225  23 VDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIP 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148   81 RALMDLLQLTREEGAEgrpWALSVTMSYLEIYQEKVLDLLDPA---SGDLVIREDCRGNILIPGLSQKPISSFADFERHF 157
Cdd:pfam00225 103 RALEDLFDRIQKTKER---SEFSVKVSYLEIYNEKIRDLLSPSnknKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  158 LPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQ--REGKLYLIDLAGSEDNRRTGN-KGLRLKESGAINTSLF 234
Cdd:pfam00225 180 QLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEEsvKTGKLNLVDLAGSERASKTGAaGGQRLKEAANINKSLS 259

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 372266148  235 VLGKVVDALNQG-LPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEV 300
Cdd:pfam00225 260 ALGNVISALADKkSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 12-300 9.18e-97

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: 299.26  E-value: 9.18e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  12 RNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDL---LQ 88
Cdd:cd01370   55 KRRNKELKYVFDRVFDETSTQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELfkrIE 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  89 LTREEGaegrpwALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVGA 168
Cdd:cd01370  135 SLKDEK------EFEVSMSYLEIYNETIRDLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEP 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 169 TRLNQRSSRSHAVLLVKVDQRERLAPFRQ--REGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDALNQG 246
Cdd:cd01370  209 TDANATSSRSHAVLQITVRQQDKTASINQqvRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADP 288

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 372266148 247 LPR---VPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEV 300
Cdd:cd01370  289 GKKnkhIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 13-296 2.16e-85

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: 269.08  E-value: 2.16e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  13 NHQETLKYQF--DAFYGERSTQQDIYAgSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLT 90
Cdd:cd01366   38 TSIGAKQKEFsfDKVFDPEASQEDVFE-EVSPLVQSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTI 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  91 REEGAEGrpWALSVTMSYLEIYQEKVLDLLDPASGD---LVIRED-CRGNILIPGLSQKPISSFADFERHFLPASRNRTV 166
Cdd:cd01366  117 KELKEKG--WSYTIKASMLEIYNETIRDLLAPGNAPqkkLEIRHDsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRST 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 167 GATRLNQRSSRSHAVLLVKVdQRERLAPFRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDALNQG 246
Cdd:cd01366  195 ASTAMNEHSSRSHSVFILHI-SGRNLQTGEISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQK 273

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 372266148 247 LPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAAR 296
Cdd:cd01366  274 QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASK 323
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 11-300 5.15e-85

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: 268.05  E-value: 5.15e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  11 WRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQlt 90
Cdd:cd01374   32 YLVEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFS-- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  91 REEGAEGRPWALSVtmSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFeRHFLPA-SRNRTVGAT 169
Cdd:cd01374  110 KIQDTPDREFLLRV--SYLEIYNEKINDLLSPTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHA-LSLIARgEKNRHVGET 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 170 RLNQRSSRSHAVLLVKVDQRERLAPFRQ--REGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDALNQGL 247
Cdd:cd01374  187 DMNERSSRSHTIFRITIESSERGELEEGtvRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGK 266

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 372266148 248 PR--VPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEV 300
Cdd:cd01374  267 VGghIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 20-296 1.70e-84

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: 267.27  E-value: 1.70e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  20 YQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGS------PEQPGVIPRALMDLLQLTREE 93
Cdd:cd01372   42 FTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEKK 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  94 GAEgrpWALSVTMSYLEIYQEKVLDLLDPAS---GDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVGATR 170
Cdd:cd01372  122 KDT---FEFQLKVSFLEIYNEEIRDLLDPETdkkPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTA 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 171 LNQRSSRSHAVLLVKVDQRERLAPFRQREG---------KLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVD 241
Cdd:cd01372  199 MNSQSSRSHAIFTITLEQTKKNGPIAPMSAddknstftsKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVIS 278

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 372266148 242 ALNQGLPR---VPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAAR 296
Cdd:cd01372  279 ALGDESKKgahVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANR 336
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 20-300 9.96e-80

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: 254.69  E-value: 9.96e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  20 YQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQP---GVIPRALMDLLqlTREEGAE 96
Cdd:cd01371   50 FTFDAVFDPNSKQLDVYDETARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIF--GHIARSQ 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  97 GRPWALsVTMSYLEIYQEKVLDLL-DPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVGATRLNQRS 175
Cdd:cd01371  128 NNQQFL-VRVSYLEIYNEEIRDLLgKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDS 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 176 SRSHAVLLVKVDQRERLAPFRQ--REGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDALNQG-LPRVPY 252
Cdd:cd01371  207 SRSHAIFTITIECSEKGEDGENhiRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGkSTHIPY 286

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 372266148 253 RDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEV 300
Cdd:cd01371  287 RDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 19-308 1.20e-78

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: 252.43  E-value: 1.20e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  19 KYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQP--------GVIPRALMDLLQL- 89
Cdd:cd01373   42 TFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLi 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  90 TREEGAEGRPWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVGAT 169
Cdd:cd01373  122 QREKEKAGEGKSFLCKCSFLEIYNEQIYDLLDPASRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAAT 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 170 RLNQRSSRSHAVLLVKVDQRERLAPF-RQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDAL----N 244
Cdd:cd01373  202 SMNRESSRSHAVFTCTIESWEKKACFvNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaH 281

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372266148 245 QGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTNE 308
Cdd:cd01373  282 GKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNE 345
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
11-311 1.18e-77

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 256.59  E-value: 1.18e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  11 WRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLT 90
Cdd:COG5059   49 SLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  91 REEGAEGRpwaLSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVGATR 170
Cdd:COG5059  129 EDLSMTKD---FAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTE 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 171 LNQRSSRSHAVLLVKVDQRERLAPFRqREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDAL--NQGLP 248
Cdd:COG5059  206 INDESSRSHSIFQIELASKNKVSGTS-ETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALgdKKKSG 284

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 372266148 249 RVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTNESLQ 311
Cdd:COG5059  285 HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSD 347
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 20-300 3.59e-77

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: 247.63  E-value: 3.59e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  20 YQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQP---GVIPRALMDLLQLTR--EEG 94
Cdd:cd01369   45 FSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYsmDEN 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  95 AEgrpwaLSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVGATRLNQR 174
Cdd:cd01369  125 LE-----FHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 175 SSRSHAVLLVKVDQRERLAPfRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDALNQG-LPRVPYR 253
Cdd:cd01369  200 SSRSHSIFLINVKQENVETE-KKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGkKTHIPYR 278

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 372266148 254 DSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEV 300
Cdd:cd01369  279 DSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 19-309 1.35e-75

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: 244.54  E-value: 1.35e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  19 KYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGS-----------PEQPGVIPRALMDLL 87
Cdd:cd01364   50 TYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwelDPLAGIIPRTLHQLF 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  88 QLTREEGAEgrpwaLSVTMSYLEIYQEKVLDLLDPASGD---LVIREDCR--GNILIPGLSQKPISSFADFERHFLPASR 162
Cdd:cd01364  130 EKLEDNGTE-----YSVKVSYLEIYNEELFDLLSPSSDVserLRMFDDPRnkRGVIIKGLEEITVHNKDEVYQILEKGAA 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 163 NRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQ--REGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVV 240
Cdd:cd01364  205 KRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEElvKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVI 284

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 372266148 241 DALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTNES 309
Cdd:cd01364  285 TALVERAPHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 20-307 9.06e-72

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: 234.94  E-value: 9.06e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  20 YQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQltREEGAEGRP 99
Cdd:cd01365   61 WSHDSEDPNYASQEQVYEDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFS--RIADTTNQN 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 100 WALSVTMSYLEIYQEKVLDLLDP----ASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVGATRLNQRS 175
Cdd:cd01365  139 MSYSVEVSYMEIYNEKVRDLLNPkpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTS 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 176 SRSHAVLLVKVDQrERLAPFRQREG----KLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDALNQ------ 245
Cdd:cd01365  219 SRSHAVFTIVLTQ-KRHDAETNLTTekvsKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADmssgks 297

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372266148 246 --GLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTN 307
Cdd:cd01365  298 kkKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 3-298 7.50e-71

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: 231.90  E-value: 7.50e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148   3 SCSLEIANWRNH-QETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPR 81
Cdd:cd01368   39 KGSAANKSERNGgQKETKFSFSKVFGPNTTQKEFFQGTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPR 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  82 ALmDLLQLTREEgaegrpwaLSVTMSYLEIYQEKVLDLLDPASGD-------LVIREDCRGNILIPGLSQKPISSFADFE 154
Cdd:cd01368  119 SL-DVIFNSIGG--------YSVFVSYIEIYNEYIYDLLEPSPSSptkkrqsLRLREDHNGNMYVAGLTEIEVKSTEEAR 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 155 RHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFR-------QREGKLYLIDLAGSEDNRRTGNKGLRLKESG 227
Cdd:cd01368  190 KVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGDvdqdkdqITVSQLSLVDLAGSERTSRTQNTGERLKEAG 269

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 372266148 228 AINTSLFVLGKVVDAL--NQGLPR---VPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSK 298
Cdd:cd01368  270 NINTSLMTLGTCIEVLreNQLQGTnkmVPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 13-298 1.08e-60

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: 204.74  E-value: 1.08e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  13 NHQETLKYQFDAFYgERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPE---QPGVIPRALMDLLQL 89
Cdd:cd01375   43 NQQEDWSFKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTEnykHRGIIPRALQQVFRM 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  90 TREEGAEgrpwALSVTMSYLEIYQEKVLDLLD------PASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRN 163
Cdd:cd01375  122 IEERPTK----AYTVHVSYLEIYNEQLYDLLStlpyvgPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETN 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 164 RTVGATRLNQRSSRSHAVLLVKVDQRER-LAPFRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDA 242
Cdd:cd01375  198 RIIASHTMNKNSSRSHCIFTIHLEAHSRtLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIA 277

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 372266148 243 L-NQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSK 298
Cdd:cd01375  278 LsDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 19-279 1.27e-58

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: 199.06  E-value: 1.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  19 KYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGS----PEQPGVIPRALMDLLQLTREEG 94
Cdd:cd01367   51 TFRFDYVFDESSSNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDfsgqEESKGIYALAARDVFRLLNKLP 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  95 AEGRpwaLSVTMSYLEIYQEKVLDLLDPASgDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVGATRLNQR 174
Cdd:cd01367  131 YKDN---LGVTVSFFEIYGGKVFDLLNRKK-RVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQ 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148 175 SSRSHAVLLVKVdqrERLAPFRQReGKLYLIDLAGSE-------DNRRTgnkglrLKESGAINTSLFVLGKVVDALNQGL 247
Cdd:cd01367  207 SSRSHAILQIIL---RDRGTNKLH-GKLSFVDLAGSErgadtssADRQT------RMEGAEINKSLLALKECIRALGQNK 276

                        250       260       270
                 ....*....|....*....|....*....|...
gi 372266148 248 PRVPYRDSKLTRLLQDSL-GGSAHSILIANIAP 279
Cdd:cd01367  277 AHIPFRGSKLTQVLKDSFiGENSKTCMIATISP 309
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 20-311 1.85e-51

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 191.30  E-value: 1.85e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148   20 YQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLG----------SPEQPGVIPRALMDLLQL 89
Cdd:PLN03188  134 FTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERLFAR 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148   90 TREEGAE--GRPWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVG 167
Cdd:PLN03188  214 INEEQIKhaDRQLKYQCRCSFLEIYNEQITDLLDPSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTG 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  168 ATRLNQRSSRSHAVLLVKVDQR-----ERLAPFRQreGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDA 242
Cdd:PLN03188  294 ATSINAESSRSHSVFTCVVESRcksvaDGLSSFKT--SRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINI 371

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372266148  243 LNQ----GLPR-VPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTNESLQ 311
Cdd:PLN03188  372 LAEisqtGKQRhIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQ 445
ComEA COG1555
DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair]; ...
 528-578 1.17e-12

DNA uptake protein ComE or related DNA-binding protein [Replication, recombination and repair];


Pssm-ID: 441164 [Multi-domain]  Cd Length: 72  Bit Score: 63.34  E-value: 1.17e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 372266148 528 LNEGSARDLRSLQRIGPKKAQLIVGWRELHGPFSQVEDLERVEGITGKQME 578
Cdd:COG1555   15 INTATAEELQTLPGIGPKLAQRIVEYREKNGPFKSVEDLLEVKGIGPKTLE 65
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 23-242 6.43e-11

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


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 61.21  E-value: 6.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  23 DAFYGER---STQQDIYAgSVQPILRHLLEGQN-ASVLAYGPTGAGKTHTMLgspeqpGVIPRALMDLlqLTREEGAEGR 98
Cdd:cd01363   20 IVFYRGFrrsESQPHVFA-IADPAYQSMLDGYNnQSIFAYGESGAGKTETMK------GVIPYLASVA--FNGINKGETE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148  99 PWAlSVTMSYLEIYQEkVLDLLdpasgdlviredcrgnilipglsqkpissfadferHFLPASRNrtvGATRLNQRSSRS 178
Cdd:cd01363   91 GWV-YLTEITVTLEDQ-ILQAN-----------------------------------PILEAFGN---AKTTRNENSSRF 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 372266148 179 HAVLLVkvdqrerlapfrqregklyLIDLAGSEdnrrtgnkglrlkesgAINTSLFVLGKVVDA 242
Cdd:cd01363  131 GKFIEI-------------------LLDIAGFE----------------IINESLNTLMNVLRA 159
HHH_3 pfam12836
Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.
 528-581 2.78e-09

Helix-hairpin-helix motif; The HhH domain is a short DNA-binding domain.


Pssm-ID: 463723 [Multi-domain]  Cd Length: 62  Bit Score: 53.25  E-value: 2.78e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 372266148  528 LNEGSARDLRSLQRIGPKKAQLIVGWRELHGPFSQVEDLERVEGITGK---QMESFL 581
Cdd:pfam12836   6 INTASAELLSRVPGLGPKLAKNIVEYREENGPFRSREDLLKVKGLGPKtfeQLAGFL 62
TIGR00426 TIGR00426
competence protein ComEA helix-hairpin-helix repeat region; Members of the subfamily ...
 528-578 2.24e-08

competence protein ComEA helix-hairpin-helix repeat region; Members of the subfamily recognized by this model include competence protein ComEA and closely related proteins from a number of species that exhibit competence for transformation by exongenous DNA, including Streptococcus pneumoniae, Bacillus subtilis, Neisseria meningitidis, and Haemophilus influenzae. This model represents a region of two tandem copies of a helix-hairpin-helix domain (pfam00633), each about 30 residues in length. Limited sequence similarity can be found among some members of this family N-terminal to the region covered by this model. [Cellular processes, DNA transformation]


Pssm-ID: 129520 [Multi-domain]  Cd Length: 69  Bit Score: 51.08  E-value: 2.24e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 372266148  528 LNEGSARDL-RSLQRIGPKKAQLIVGWRELHGPFSQVEDLERVEGITGKQME 578
Cdd:TIGR00426  10 INTATAEELqRAMNGVGLKKAEAIVSYREEYGPFKTVEDLKQVPGIGNSLVE 61
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 8-120 1.25e-07

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 51.07  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 372266148    8 IANWRNHQETLKYQFDAFYGERSTQQDIYagsvQPIlRHL----LEGQNASVLAYGPTGAGKThtmlgspeqPGVIPRAL 83
Cdd:pfam16796  45 SSDGKIGSKNKSFSFDRVFPPESEQEDVF----QEI-SQLvqscLDGYNVCIFAYGQTGSGSN---------DGMIPRAR 110

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 372266148   84 MDLLQlTREEGAEGrpWALSVTMSYLEIYQEKVLDLL 120
Cdd:pfam16796 111 EQIFR-FISSLKKG--WKYTIELQFVEIYNESSQDLL 144
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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