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Conserved domains on  [gi|2217303428|ref|XP_047289329|]
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kinesin-like protein KIF23 isoform X11 [Homo sapiens]

Protein Classification

kinesin-like protein KIF23( domain architecture ID 10842314)

kinesin-like protein KIF23 is essential for cytokinesis in Rho-mediated signaling; it has an N-terminal motor domain and is a (+) end-directed motor

CATH:  3.40.850.10
Gene Symbol:  KIF23
SCOP:  4004055

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
24-434 0e+00

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: 609.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  24 DPVGVYCRVRPLGFP----DQECCIEVINNTTVQLHTPEGYRLN---RNGDYKETQYSFKQVFGTHTTQKELFDVVANPL 96
Cdd:cd01368     1 DPVKVYLRVRPLSKDelesEDEGCIEVINSTTVVLHPPKGSAANkseRNGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  97 VNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSfqakryvfksndrnsmdiqcevdallerqkr 176
Cdd:cd01368    81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------------------------------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 177 eampnpktssskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEEVPFDPikPKPPQSKLLREDK 256
Cdd:cd01368   130 ---------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSP--TKKRQSLRLREDH 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 257 NHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDnVLQEKEQITISQLSLV 336
Cdd:cd01368   169 NGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGD-VDQDKDQITVSQLSLV 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 337 DLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPK 416
Cdd:cd01368   248 DLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPC 327
                         410
                  ....*....|....*...
gi 2217303428 417 AEDYEENLQVMRFAEVTQ 434
Cdd:cd01368   328 ASDYDETLHVMKFSAIAQ 345
MKLP1_Arf_bdg pfam16540
Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region ...
581-684 7.06e-59

Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region of mitotic kinesin-like proteins that is necessary for the interaction with the small GTPase Arf6. MKLP1 is a Flemming body-localising protein essential for cytokinesis, so its interaction with Arf6 shows how Arf6 is involved in cytokinesis. The Arf6-MKLP1 complex plays a crucial role in cytokinesis by connecting the microtubule bundle and membranes at the cleavage plane.


:

Pssm-ID: 465166  Cd Length: 107  Bit Score: 194.45  E-value: 7.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 581 PPIRLRHRRSRSAGDRWVDHKPASNMQTETVMQPHVP---HAITVSVANEKALAKCEKYMLTHQELASDGEIETKLIKGD 657
Cdd:pfam16540   1 PVVNPRHRRSRSAGERWLDHKPPSNVPTGTILQPRIPnrkSVTKLTKPKDKALAKASKYCLTHQEQDSDGEIETKLYKGD 80
                          90       100
                  ....*....|....*....|....*..
gi 2217303428 658 IYKTRGGGQSVQFTDIETLKQESPNGS 684
Cdd:pfam16540  81 VIPTRGGGAQVQFNDIETLKQESPTGS 107
 
Name Accession Description Interval E-value
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
24-434 0e+00

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: 609.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  24 DPVGVYCRVRPLGFP----DQECCIEVINNTTVQLHTPEGYRLN---RNGDYKETQYSFKQVFGTHTTQKELFDVVANPL 96
Cdd:cd01368     1 DPVKVYLRVRPLSKDelesEDEGCIEVINSTTVVLHPPKGSAANkseRNGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  97 VNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSfqakryvfksndrnsmdiqcevdallerqkr 176
Cdd:cd01368    81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------------------------------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 177 eampnpktssskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEEVPFDPikPKPPQSKLLREDK 256
Cdd:cd01368   130 ---------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSP--TKKRQSLRLREDH 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 257 NHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDnVLQEKEQITISQLSLV 336
Cdd:cd01368   169 NGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGD-VDQDKDQITVSQLSLV 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 337 DLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPK 416
Cdd:cd01368   248 DLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPC 327
                         410
                  ....*....|....*...
gi 2217303428 417 AEDYEENLQVMRFAEVTQ 434
Cdd:cd01368   328 ASDYDETLHVMKFSAIAQ 345
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
25-442 7.15e-122

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: 368.05  E-value: 7.15e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428   25 PVGVYCRVRPLGfpDQE------CCIEVINNTTVQLhtpegyRLNRNGDYKETQ-YSFKQVFGTHTTQKELFDVVANPLV 97
Cdd:smart00129   1 NIRVVVRVRPLN--KREksrkspSVVPFPDKVGKTL------TVRSPKNRQGEKkFTFDKVFDATASQEDVFEETAAPLV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428   98 NDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSFQakryvfksndrnsmdiqcevdallerqkre 177
Cdd:smart00129  73 DSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE------------------------------ 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  178 ampnpktssskrqvdpefadmitvqefckaeevdEDSVYGVFVSYIEIYNNYIYDLLEevpfdpikpkPPQSKL-LREDK 256
Cdd:smart00129 123 ----------------------------------EGWQFSVKVSYLEIYNEKIRDLLN----------PSSKKLeIREDE 158
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  257 NHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDAdgdnvlqEKEQITISQLSLV 336
Cdd:smart00129 159 KGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNS-------SSGSGKASKLNLV 231
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  337 DLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQmygTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPK 416
Cdd:smart00129 232 DLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS---KSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPS 308
                          410       420
                   ....*....|....*....|....*.
gi 2217303428  417 AEDYEENLQVMRFAEVTQEVEVARPV 442
Cdd:smart00129 309 SSNLEETLSTLRFASRAKEIKNKPIV 334
Kinesin pfam00225
Kinesin motor domain;
31-431 1.11e-120

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 364.59  E-value: 1.11e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  31 RVRPLgFPDQECCIEVINNTTVQLHTPEGYRLNRNGDYKETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFT 110
Cdd:pfam00225   1 RVRPL-NEREKERGSSVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 111 YGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIgsfqakryvfksndrnsmdiqcevdallerQKREampnpktssskrq 190
Cdd:pfam00225  80 YGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRI------------------------------QKTK------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 191 vdpefadmitvqefckaeevdEDSVYGVFVSYIEIYNNYIYDLLEEvpfdpiKPKPPQSKLLREDKNHNMYVAGCTEVEV 270
Cdd:pfam00225 117 ---------------------ERSEFSVKVSYLEIYNEKIRDLLSP------SNKNKRKLRIREDPKKGVYVKGLTEVEV 169
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 271 KSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGdnvlqeKEQITISQLSLVDLAGSERTNRT-RA 349
Cdd:pfam00225 170 SSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG------EESVKTGKLNLVDLAGSERASKTgAA 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 350 EGNRLREAGNINQSLMTLRTCMDVLRENQmygtNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRF 429
Cdd:pfam00225 244 GGQRLKEAANINKSLSALGNVISALADKK----SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRF 319

                  ..
gi 2217303428 430 AE 431
Cdd:pfam00225 320 AS 321
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
69-437 1.81e-60

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 213.45  E-value: 1.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  69 KETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLdmifnsigsfqa 148
Cdd:COG5059    54 KEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSL------------ 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 149 kRYVFKSNDRNSMDiqcevdallerqkreampnpktssskrqvdpefadmitvqefckaeevdedSVYGVFVSYIEIYNN 228
Cdd:COG5059   122 -KELFSKLEDLSMT---------------------------------------------------KDFAVSISYLEIYNE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 229 YIYDLLEevpfdpikpKPPQSKLLREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIK 308
Cdd:COG5059   150 KIYDLLS---------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 309 LVQApldadgDNVLQEKEQitiSQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENqmyGTNKMVPY 388
Cdd:COG5059   221 LASK------NKVSGTSET---SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDK---KKSGHIPY 288
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2217303428 389 RDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRFAEVTQEVE 437
Cdd:COG5059   289 RESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIK 337
MKLP1_Arf_bdg pfam16540
Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region ...
581-684 7.06e-59

Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region of mitotic kinesin-like proteins that is necessary for the interaction with the small GTPase Arf6. MKLP1 is a Flemming body-localising protein essential for cytokinesis, so its interaction with Arf6 shows how Arf6 is involved in cytokinesis. The Arf6-MKLP1 complex plays a crucial role in cytokinesis by connecting the microtubule bundle and membranes at the cleavage plane.


Pssm-ID: 465166  Cd Length: 107  Bit Score: 194.45  E-value: 7.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 581 PPIRLRHRRSRSAGDRWVDHKPASNMQTETVMQPHVP---HAITVSVANEKALAKCEKYMLTHQELASDGEIETKLIKGD 657
Cdd:pfam16540   1 PVVNPRHRRSRSAGERWLDHKPPSNVPTGTILQPRIPnrkSVTKLTKPKDKALAKASKYCLTHQEQDSDGEIETKLYKGD 80
                          90       100
                  ....*....|....*....|....*..
gi 2217303428 658 IYKTRGGGQSVQFTDIETLKQESPNGS 684
Cdd:pfam16540  81 VIPTRGGGAQVQFNDIETLKQESPTGS 107
PLN03188 PLN03188
kinesin-12 family protein; Provisional
70-431 1.52e-41

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 163.95  E-value: 1.52e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428   70 ETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFTYGVTGSGKTHTMTG----------SPGEGGLLPRCLDMI 139
Cdd:PLN03188   131 GQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERL 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  140 FNSIGSFQAKRyvfksndrnsmdiqcevdalLERQKReampnpktssskrqvdpefadmitvqefckaeevdedsvYGVF 219
Cdd:PLN03188   211 FARINEEQIKH--------------------ADRQLK---------------------------------------YQCR 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  220 VSYIEIYNNYIYDLLEevpfdpikpkPPQSKL-LREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRES 298
Cdd:PLN03188   232 CSFLEIYNEQITDLLD----------PSQKNLqIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAES 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  299 SRSHSVFNIkLVQAPLD--ADGDNVLQekeqitISQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRE 376
Cdd:PLN03188   302 SRSHSVFTC-VVESRCKsvADGLSSFK------TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAE 374
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217303428  377 NQMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRFAE 431
Cdd:PLN03188   375 ISQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQ 429
 
Name Accession Description Interval E-value
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
24-434 0e+00

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: 609.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  24 DPVGVYCRVRPLGFP----DQECCIEVINNTTVQLHTPEGYRLN---RNGDYKETQYSFKQVFGTHTTQKELFDVVANPL 96
Cdd:cd01368     1 DPVKVYLRVRPLSKDelesEDEGCIEVINSTTVVLHPPKGSAANkseRNGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  97 VNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSfqakryvfksndrnsmdiqcevdallerqkr 176
Cdd:cd01368    81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------------------------------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 177 eampnpktssskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEEVPFDPikPKPPQSKLLREDK 256
Cdd:cd01368   130 ---------------------------------------YSVFVSYIEIYNEYIYDLLEPSPSSP--TKKRQSLRLREDH 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 257 NHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDnVLQEKEQITISQLSLV 336
Cdd:cd01368   169 NGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSDGD-VDQDKDQITVSQLSLV 247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 337 DLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPK 416
Cdd:cd01368   248 DLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGKASMIVNVNPC 327
                         410
                  ....*....|....*...
gi 2217303428 417 AEDYEENLQVMRFAEVTQ 434
Cdd:cd01368   328 ASDYDETLHVMKFSAIAQ 345
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
25-434 7.85e-133

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: 395.86  E-value: 7.85e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  25 PVGVYCRVRPLGF---PDQECCIEVINNTTVQLHTPEgyrlnrNGDYKETQYSFKQVFGTHTTQKELFDVVANPLVNDLI 101
Cdd:cd00106     1 NVRVAVRVRPLNGreaRSAKSVISVDGGKSVVLDPPK------NRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 102 HGKNGLLFTYGVTGSGKTHTMTGSPGEG-GLLPRCLDMIFNSIGSFQAKryvfksndrnsmdiqcevdallerqkreamp 180
Cdd:cd00106    75 EGYNGTIFAYGQTGSGKTYTMLGPDPEQrGIIPRALEDIFERIDKRKET------------------------------- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 181 npktssskrqvdpefadmitvqefckaeevdeDSVYGVFVSYIEIYNNYIYDLLEevpfdpikPKPPQSKLLREDKNHNM 260
Cdd:cd00106   124 --------------------------------KSSFSVSASYLEIYNEKIYDLLS--------PVPKKPLSLREDPKRGV 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 261 YVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGdnvlqekEQITISQLSLVDLAG 340
Cdd:cd00106   164 YVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSG-------ESVTSSKLNLVDLAG 236
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 341 SERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQmygtNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDY 420
Cdd:cd00106   237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQ----NKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENF 312
                         410
                  ....*....|....
gi 2217303428 421 EENLQVMRFAEVTQ 434
Cdd:cd00106   313 EETLSTLRFASRAK 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
25-442 7.15e-122

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: 368.05  E-value: 7.15e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428   25 PVGVYCRVRPLGfpDQE------CCIEVINNTTVQLhtpegyRLNRNGDYKETQ-YSFKQVFGTHTTQKELFDVVANPLV 97
Cdd:smart00129   1 NIRVVVRVRPLN--KREksrkspSVVPFPDKVGKTL------TVRSPKNRQGEKkFTFDKVFDATASQEDVFEETAAPLV 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428   98 NDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSFQakryvfksndrnsmdiqcevdallerqkre 177
Cdd:smart00129  73 DSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKRE------------------------------ 122
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  178 ampnpktssskrqvdpefadmitvqefckaeevdEDSVYGVFVSYIEIYNNYIYDLLEevpfdpikpkPPQSKL-LREDK 256
Cdd:smart00129 123 ----------------------------------EGWQFSVKVSYLEIYNEKIRDLLN----------PSSKKLeIREDE 158
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  257 NHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDAdgdnvlqEKEQITISQLSLV 336
Cdd:smart00129 159 KGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNS-------SSGSGKASKLNLV 231
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  337 DLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQmygTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPK 416
Cdd:smart00129 232 DLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS---KSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPS 308
                          410       420
                   ....*....|....*....|....*.
gi 2217303428  417 AEDYEENLQVMRFAEVTQEVEVARPV 442
Cdd:smart00129 309 SSNLEETLSTLRFASRAKEIKNKPIV 334
Kinesin pfam00225
Kinesin motor domain;
31-431 1.11e-120

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 364.59  E-value: 1.11e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  31 RVRPLgFPDQECCIEVINNTTVQLHTPEGYRLNRNGDYKETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFT 110
Cdd:pfam00225   1 RVRPL-NEREKERGSSVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 111 YGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIgsfqakryvfksndrnsmdiqcevdallerQKREampnpktssskrq 190
Cdd:pfam00225  80 YGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRI------------------------------QKTK------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 191 vdpefadmitvqefckaeevdEDSVYGVFVSYIEIYNNYIYDLLEEvpfdpiKPKPPQSKLLREDKNHNMYVAGCTEVEV 270
Cdd:pfam00225 117 ---------------------ERSEFSVKVSYLEIYNEKIRDLLSP------SNKNKRKLRIREDPKKGVYVKGLTEVEV 169
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 271 KSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGdnvlqeKEQITISQLSLVDLAGSERTNRT-RA 349
Cdd:pfam00225 170 SSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGG------EESVKTGKLNLVDLAGSERASKTgAA 243
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 350 EGNRLREAGNINQSLMTLRTCMDVLRENQmygtNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRF 429
Cdd:pfam00225 244 GGQRLKEAANINKSLSALGNVISALADKK----SKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRF 319

                  ..
gi 2217303428 430 AE 431
Cdd:pfam00225 320 AS 321
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
28-431 9.34e-75

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: 244.81  E-value: 9.34e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  28 VYCRVRPLgFPDQE----CCIEVINNTTVQLHTPegyrlnrNGDYKETQYSFKQVFGTHTTQKELFDVVAnPLVNDLIHG 103
Cdd:cd01366     6 VFCRVRPL-LPSEEnedtSHITFPDEDGQTIELT-------SIGAKQKEFSFDKVFDPEASQEDVFEEVS-PLVQSALDG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 104 KNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIGSFQAKRYVFksndrnsmDIQCevdallerqkreampnpk 183
Cdd:cd01366    77 YNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSY--------TIKA------------------ 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 184 tssskrqvdpefadmitvqefckaeevdedsvygvfvSYIEIYNNYIYDLLeevpfdpIKPKPPQSKL-LREDKNHNM-Y 261
Cdd:cd01366   131 -------------------------------------SMLEIYNETIRDLL-------APGNAPQKKLeIRHDSEKGDtT 166
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 262 VAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLvqapldaDGDNvlQEKEQITISQLSLVDLAGS 341
Cdd:cd01366   167 VTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-------SGRN--LQTGEISVGKLNLVDLAGS 237
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 342 ERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMYgtnkmVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYE 421
Cdd:cd01366   238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSH-----IPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLN 312
                         410
                  ....*....|
gi 2217303428 422 ENLQVMRFAE 431
Cdd:cd01366   313 ETLNSLRFAS 322
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
28-429 2.56e-71

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: 235.69  E-value: 2.56e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  28 VYCRVRPLgfPDQEC------CIEVINNTTVQLHTPEgyrlnrngdyKETQYSFKQVFGTHTTQKELFDVVANPLVNDLI 101
Cdd:cd01369     6 VVCRFRPL--NELEVlqgsksIVKFDPEDTVVIATSE----------TGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 102 HGKNGLLFTYGVTGSGKTHTMTGSPGEG---GLLPRCLDMIFNSIGSfqakryvfksndrnsmdiqcevdallerqkrea 178
Cdd:cd01369    74 NGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYS--------------------------------- 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 179 mpnpktssskrqvdpefadmitvqefckaeeVDEDSVYGVFVSYIEIYNNYIYDLLEEVPfDPIKpkppqsklLREDKNH 258
Cdd:cd01369   121 -------------------------------MDENLEFHVKVSYFEIYMEKIRDLLDVSK-TNLS--------VHEDKNR 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 259 NMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQapldadgDNVlqEKEQITISQLSLVDL 338
Cdd:cd01369   161 GPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-------ENV--ETEKKKSGKLYLVDL 231
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 339 AGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLREnqmyGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAE 418
Cdd:cd01369   232 AGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD----GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSY 307
                         410
                  ....*....|.
gi 2217303428 419 DYEENLQVMRF 429
Cdd:cd01369   308 NESETLSTLRF 318
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
26-430 2.63e-69

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: 230.30  E-value: 2.63e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  26 VGVYCRVRPL---GFPDQECCIEVINNTTVQLHTPEGyrlnrngdykeTQYSFKQVFGTHTTQKELFDVVANPLVNDLIH 102
Cdd:cd01374     2 ITVTVRVRPLnsrEIGINEQVAWEIDNDTIYLVEPPS-----------TSFTFDHVFGGDSTNREVYELIAKPVVKSALE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 103 GKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIgsfqakryvFKSNDRNsmdiqcevdallerqkreampnp 182
Cdd:cd01374    71 GYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKI---------QDTPDRE----------------------- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 183 ktssskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEevpfdpikpkpPQSKLL--REDKNHNM 260
Cdd:cd01374   119 ---------------------------------FLLRVSYLEIYNEKINDLLS-----------PTSQNLkiRDDVEKGV 154
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 261 YVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADgdnvlqEKEQITISQLSLVDLAG 340
Cdd:cd01374   155 YVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGEL------EEGTVRVSTLNLIDLAG 228
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 341 SERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMygtNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDY 420
Cdd:cd01374   229 SERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKV---GGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHV 305
                         410
                  ....*....|
gi 2217303428 421 EENLQVMRFA 430
Cdd:cd01374   306 EETLNTLKFA 315
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
25-430 3.60e-69

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: 230.30  E-value: 3.60e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  25 PVGVYCRVRPLGFPDQ----ECCIEVINNTT-VQLHTPEGYrlnrngdyketqySFKQVFGTHTTQKELFDVVANPLVND 99
Cdd:cd01372     2 SVRVAVRVRPLLPKEIiegcRICVSFVPGEPqVTVGTDKSF-------------TFDYVFDPSTEQEEVYNTCVAPLVDG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 100 LIHGKNGLLFTYGVTGSGKTHTM-TGSPGEG-----GLLPRCLDMIFNSIgsfqakryvfksndrnsmdiqcevdaller 173
Cdd:cd01372    69 LFEGYNATVLAYGQTGSGKTYTMgTAYTAEEdeeqvGIIPRAIQHIFKKI------------------------------ 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 174 qkreampnpktssSKRQVDPEFAdmitvqefckaeevdedsvygVFVSYIEIYNNYIYDLLEevPFDPIKPKPPqsklLR 253
Cdd:cd01372   119 -------------EKKKDTFEFQ---------------------LKVSFLEIYNEEIRDLLD--PETDKKPTIS----IR 158
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 254 EDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGD-NVLQEKEQITISQ 332
Cdd:cd01372   159 EDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIApMSADDKNSTFTSK 238
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 333 LSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQMYGTNkmVPYRDSKLTHLFKNYFDGEGKVRMIVC 412
Cdd:cd01372   239 FHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAH--VPYRDSKLTRLLQDSLGGNSHTLMIAC 316
                         410
                  ....*....|....*...
gi 2217303428 413 VNPKAEDYEENLQVMRFA 430
Cdd:cd01372   317 VSPADSNFEETLNTLKYA 334
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
26-430 2.35e-68

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: 229.16  E-value: 2.35e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  26 VGVYCRVRPLG----FPDQECCIEVINNTTVQLHTPEGYRLNRNGDYKETQYSFKQVFGTHT-------TQKELFDVVAN 94
Cdd:cd01365     3 VKVAVRVRPFNsrekERNSKCIVQMSGKETTLKNPKQADKNNKATREVPKSFSFDYSYWSHDsedpnyaSQEQVYEDLGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  95 PLVNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIgsfqakryvfksndrnsmdiqcevdallerq 174
Cdd:cd01365    83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRI------------------------------- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 175 krEAMPNPKTSsskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLeevpfDPIKPKPPQSKLLRE 254
Cdd:cd01365   132 --ADTTNQNMS------------------------------YSVEVSYMEIYNEKVRDLL-----NPKPKKNKGNLKVRE 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 255 DKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDnVLQEKeqitISQLS 334
Cdd:cd01365   175 HPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN-LTTEK----VSKIS 249
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 335 LVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQ---MYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIV 411
Cdd:cd01365   250 LVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSsgkSKKKSSFIPYRDSVLTWLLKENLGGNSKTAMIA 329
                         410
                  ....*....|....*....
gi 2217303428 412 CVNPKAEDYEENLQVMRFA 430
Cdd:cd01365   330 AISPADINYEETLSTLRYA 348
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
28-430 2.47e-66

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: 222.99  E-value: 2.47e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  28 VYCRVRPLGFPD----QECCIEVINN----------TTVQLHTPEGYRLNRNGDYKETQYSFKQVFGTHTTQKELFDVVA 93
Cdd:cd01370     4 VAVRVRPFSEKEknegFRRIVKVMDNhmlvfdpkdeEDGFFHGGSNNRDRRKRRNKELKYVFDRVFDETSTQEEVYEETT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  94 NPLVNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMIFNSIgsfqakryvfksndrnsmdiqcevdaller 173
Cdd:cd01370    84 KPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRI------------------------------ 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 174 qkreampnpktssskrqvdpefadmitvqefckaEEVDEDSVYGVFVSYIEIYNNYIYDLLEevpfdpikpkpPQSKLL- 252
Cdd:cd01370   134 ----------------------------------ESLKDEKEFEVSMSYLEIYNETIRDLLN-----------PSSGPLe 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 253 -REDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADgdnvlqEKEQITIS 331
Cdd:cd01370   169 lREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTAS------INQQVRQG 242
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 332 QLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQmyGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIV 411
Cdd:cd01370   243 KLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPG--KKNKHIPYRDSKLTRLLKDSLGGNCRTVMIA 320
                         410
                  ....*....|....*....
gi 2217303428 412 CVNPKAEDYEENLQVMRFA 430
Cdd:cd01370   321 NISPSSSSYEETHNTLKYA 339
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
24-431 6.22e-64

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: 216.61  E-value: 6.22e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  24 DPVGVYCRVRPLGFPDQEC----CIEVINNTTVQLHTpegyrlnrngdYKETQYSFKQVFGTHTTQKELFDVVANPLVND 99
Cdd:cd01373     1 DAVKVFVRIRPPAEREGDGeygqCLKKLSSDTLVLHS-----------KPPKTFTFDHVADSNTNQESVFQSVGKPIVES 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 100 LIHGKNGLLFTYGVTGSGKTHTMTGSPGEG--------GLLPRCLDMIFNSIgsfqaKRYVFKSNDRNSMDIQCevdall 171
Cdd:cd01373    70 CLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLI-----QREKEKAGEGKSFLCKC------ 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 172 erqkreampnpktssskrqvdpefadmitvqefckaeevdedsvygvfvSYIEIYNNYIYDLLEevpfdpikpkPPQSKL 251
Cdd:cd01373   139 -------------------------------------------------SFLEIYNEQIYDLLD----------PASRNL 159
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 252 -LREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDNvlqekeqITI 330
Cdd:cd01373   160 kLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFVN-------IRT 232
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 331 SQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENqMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMI 410
Cdd:cd01373   233 SRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDV-AHGKQRHVCYRDSKLTFLLRDSLGGNAKTAII 311
                         410       420
                  ....*....|....*....|.
gi 2217303428 411 VCVNPKAEDYEENLQVMRFAE 431
Cdd:cd01373   312 ANVHPSSKCFGETLSTLRFAQ 332
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
28-430 1.52e-61

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: 210.26  E-value: 1.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  28 VYCRVRPlgFPDQECCIeviNNTTVQLHTPEGYRL-----NRNGDYKETQYSFKQVFGTHTTQKELFDVVANPLVNDLIH 102
Cdd:cd01364     6 VVVRCRP--FNLRERKA---SSHSVVEVDPVRKEVsvrtgGLADKSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 103 GKNGLLFTYGVTGSGKTHTMTG--SPGEG---------GLLPRCLDMIFNSigsfqakryvfksndrnsmdiqcevdalL 171
Cdd:cd01364    81 GYNCTIFAYGQTGTGKTYTMEGdrSPNEEytweldplaGIIPRTLHQLFEK----------------------------L 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 172 ERQKREampnpktssskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEevpfdpikPKPPQSKL 251
Cdd:cd01364   133 EDNGTE--------------------------------------YSVKVSYLEIYNEELFDLLS--------PSSDVSER 166
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 252 LR----EDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDNVLQekeq 327
Cdd:cd01364   167 LRmfddPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEELVK---- 242
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 328 itISQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENqmygtNKMVPYRDSKLTHLFKNYFDGEGKV 407
Cdd:cd01364   243 --IGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVER-----APHVPYRESKLTRLLQDSLGGRTKT 315
                         410       420
                  ....*....|....*....|...
gi 2217303428 408 RMIVCVNPKAEDYEENLQVMRFA 430
Cdd:cd01364   316 SIIATISPASVNLEETLSTLEYA 338
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
69-437 1.81e-60

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 213.45  E-value: 1.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  69 KETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLdmifnsigsfqa 148
Cdd:COG5059    54 KEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSL------------ 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 149 kRYVFKSNDRNSMDiqcevdallerqkreampnpktssskrqvdpefadmitvqefckaeevdedSVYGVFVSYIEIYNN 228
Cdd:COG5059   122 -KELFSKLEDLSMT---------------------------------------------------KDFAVSISYLEIYNE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 229 YIYDLLEevpfdpikpKPPQSKLLREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIK 308
Cdd:COG5059   150 KIYDLLS---------PNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIE 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 309 LVQApldadgDNVLQEKEQitiSQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENqmyGTNKMVPY 388
Cdd:COG5059   221 LASK------NKVSGTSET---SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDK---KKSGHIPY 288
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2217303428 389 RDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRFAEVTQEVE 437
Cdd:COG5059   289 RESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIK 337
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
25-430 5.63e-60

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: 205.04  E-value: 5.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  25 PVGVYCRVRPLGFPDQEC----CIEVINNTTVQLHTPEGYRLNRngdyketQYSFKQVFGTHTTQKELFDVVANPLVNDL 100
Cdd:cd01376     1 NVRVAVRVRPFVDGTAGAsdpsCVSGIDSCSVELADPRNHGETL-------KYQFDAFYGEESTQEDIYAREVQPIVPHL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 101 IHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCldmifnsigsfqakryvfksndrnsmdiqceVDALLERQKREAMP 180
Cdd:cd01376    74 LEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLT-------------------------------VMDLLQMTRKEAWA 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 181 npktssskrqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEevpfdpikpkPPQSKL-LREDKNHN 259
Cdd:cd01376   123 -----------------------------------LSFTMSYLEIYQEKILDLLE----------PASKELvIREDKDGN 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 260 MYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIklvqapldadgdNVLQEKEQITISQ----LSL 335
Cdd:cd01376   158 ILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLI------------KVDQRERLAPFRQrtgkLNL 225
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 336 VDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRENQmygtnKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNP 415
Cdd:cd01376   226 IDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNL-----PRIPYRDSKLTRLLQDSLGGGSRCIMVANIAP 300
                         410
                  ....*....|....*
gi 2217303428 416 KAEDYEENLQVMRFA 430
Cdd:cd01376   301 ERTFYQDTLSTLNFA 315
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
24-430 7.69e-60

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: 205.39  E-value: 7.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  24 DPVGVYCRVRPL-GFPDQECCIEVIN----NTTVQLHTPegyrlnrNGDYKET--QYSFKQVFGTHTTQKELFDVVANPL 96
Cdd:cd01371     1 ENVKVVVRCRPLnGKEKAAGALQIVDvdekRGQVSVRNP-------KATANEPpkTFTFDAVFDPNSKQLDVYDETARPL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  97 VNDLIHGKNGLLFTYGVTGSGKTHTMTG---SPGEGGLLPRCLDMIFNSIGsfqakryvfksndrnsmdiqcevdaller 173
Cdd:cd01371    74 VDSVLEGYNGTIFAYGQTGTGKTYTMEGkreDPELRGIIPNSFAHIFGHIA----------------------------- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 174 qkreampnpKTSSSKRqvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEevpfdpikpKPPQSKL-L 252
Cdd:cd01371   125 ---------RSQNNQQ--------------------------FLVRVSYLEIYNEEIRDLLG---------KDQTKRLeL 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 253 REDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDADGDNVlqekeqITISQ 332
Cdd:cd01371   161 KERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENH------IRVGK 234
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 333 LSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLREnqmyGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVC 412
Cdd:cd01371   235 LNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD----GKSTHIPYRDSKLTRLLQDSLGGNSKTVMCAN 310
                         410
                  ....*....|....*...
gi 2217303428 413 VNPKAEDYEENLQVMRFA 430
Cdd:cd01371   311 IGPADYNYDETLSTLRYA 328
MKLP1_Arf_bdg pfam16540
Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region ...
581-684 7.06e-59

Arf6-interacting domain of mitotic kinesin-like protein 1; This family is a C-terminal region of mitotic kinesin-like proteins that is necessary for the interaction with the small GTPase Arf6. MKLP1 is a Flemming body-localising protein essential for cytokinesis, so its interaction with Arf6 shows how Arf6 is involved in cytokinesis. The Arf6-MKLP1 complex plays a crucial role in cytokinesis by connecting the microtubule bundle and membranes at the cleavage plane.


Pssm-ID: 465166  Cd Length: 107  Bit Score: 194.45  E-value: 7.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 581 PPIRLRHRRSRSAGDRWVDHKPASNMQTETVMQPHVP---HAITVSVANEKALAKCEKYMLTHQELASDGEIETKLIKGD 657
Cdd:pfam16540   1 PVVNPRHRRSRSAGERWLDHKPPSNVPTGTILQPRIPnrkSVTKLTKPKDKALAKASKYCLTHQEQDSDGEIETKLYKGD 80
                          90       100
                  ....*....|....*....|....*..
gi 2217303428 658 IYKTRGGGQSVQFTDIETLKQESPNGS 684
Cdd:pfam16540  81 VIPTRGGGAQVQFNDIETLKQESPTGS 107
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
26-431 2.10e-51

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: 182.01  E-value: 2.10e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  26 VGVYCRVRPLGFPDQECCIEVINNTTVQLHTPEGYR---LNRngdyKETQYSFKQVFGTHTTQKEL-FDVVANPLVNDLI 101
Cdd:cd01375     2 VQAFVRVRPTDDFAHEMIKYGEDGKSISIHLKKDLRrgvVNN----QQEDWSFKFDGVLHNASQELvYETVAKDVVSSAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 102 HGKNGLLFTYGVTGSGKTHTMTGSpGEG----GLLPRCLDMIFnsigsfqakryvfksndrnsmdiqcevdallerqkre 177
Cdd:cd01375    78 AGYNGTIFAYGQTGAGKTFTMTGG-TENykhrGIIPRALQQVF------------------------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 178 ampnpktssskRQVdpefadmitvqefckaeEVDEDSVYGVFVSYIEIYNNYIYDLLEEVPFdpIKPKPPQSKLLrEDKN 257
Cdd:cd01375   120 -----------RMI-----------------EERPTKAYTVHVSYLEIYNEQLYDLLSTLPY--VGPSVTPMTIL-EDSP 168
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 258 HNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQAPLDAdgdnvlqEKEQITISQLSLVD 337
Cdd:cd01375   169 QNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTL-------SSEKYITSKLNLVD 241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 338 LAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVL-RENQMYgtnkmVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPK 416
Cdd:cd01375   242 LAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALsDKDRTH-----VPFRQSKLTHVLRDSLGGNCNTVMVANIYGE 316
                         410
                  ....*....|....*
gi 2217303428 417 AEDYEENLQVMRFAE 431
Cdd:cd01375   317 AAQLEETLSTLRFAS 331
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
25-430 1.77e-48

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: 174.02  E-value: 1.77e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  25 PVGVYCRVRPLgfPDQECC------IEVINNTTVQLHTPegyRLNRNGDYKETQYSFK--QVFGTHTTQKELFDVVANPL 96
Cdd:cd01367     1 KIKVCVRKRPL--NKKEVAkkeidvVSVPSKLTLIVHEP---KLKVDLTKYIENHTFRfdYVFDESSSNETVYRSTVKPL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  97 VNDLIHGKNGLLFTYGVTGSGKTHTMTGSPGEGGLLPRCLDMifnsigsfqAKRYVFksndrnsmdiqcevdalleRQKr 176
Cdd:cd01367    76 VPHIFEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYAL---------AARDVF-------------------RLL- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 177 eampnpKTSSSKRQvdpefadmitvqefckaeevdedsvYGVFVSYIEIYNNYIYDLLEEvpfdpikpkppQSKL-LRED 255
Cdd:cd01367   127 ------NKLPYKDN-------------------------LGVTVSFFEIYGGKVFDLLNR-----------KKRVrLRED 164
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 256 KNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFNIKLVQApldadgdnvlqeKEQITISQLSL 335
Cdd:cd01367   165 GKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDR------------GTNKLHGKLSF 232
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 336 VDLAGSERTNRTRAEG-NRLREAGNINQSLMTLRTCMDVLRENQMYgtnkmVPYRDSKLTHLFKNYFDGE-GKVRMIVCV 413
Cdd:cd01367   233 VDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKAH-----IPFRGSKLTQVLKDSFIGEnSKTCMIATI 307
                         410
                  ....*....|....*..
gi 2217303428 414 NPKAEDYEENLQVMRFA 430
Cdd:cd01367   308 SPGASSCEHTLNTLRYA 324
PLN03188 PLN03188
kinesin-12 family protein; Provisional
70-431 1.52e-41

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 163.95  E-value: 1.52e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428   70 ETQYSFKQVFGTHTTQKELFDVVANPLVNDLIHGKNGLLFTYGVTGSGKTHTMTG----------SPGEGGLLPRCLDMI 139
Cdd:PLN03188   131 GQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglleehlSGDQQGLTPRVFERL 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  140 FNSIGSFQAKRyvfksndrnsmdiqcevdalLERQKReampnpktssskrqvdpefadmitvqefckaeevdedsvYGVF 219
Cdd:PLN03188   211 FARINEEQIKH--------------------ADRQLK---------------------------------------YQCR 231
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  220 VSYIEIYNNYIYDLLEevpfdpikpkPPQSKL-LREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRES 298
Cdd:PLN03188   232 CSFLEIYNEQITDLLD----------PSQKNLqIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAES 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  299 SRSHSVFNIkLVQAPLD--ADGDNVLQekeqitISQLSLVDLAGSERTNRTRAEGNRLREAGNINQSLMTLRTCMDVLRE 376
Cdd:PLN03188   302 SRSHSVFTC-VVESRCKsvADGLSSFK------TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAE 374
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2217303428  377 NQMYGTNKMVPYRDSKLTHLFKNYFDGEGKVRMIVCVNPKAEDYEENLQVMRFAE 431
Cdd:PLN03188   375 ISQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQ 429
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
28-180 1.95e-08

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: 54.27  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  28 VYCRVRPLgfpdqeccievinnttvqlhtpegyrlNRNGDYKETQY-SFKQVFGTHTTQKELFDVvANPLVNDLIHGKNG 106
Cdd:cd01363     1 VLVRVNPF---------------------------KELPIYRDSKIiVFYRGFRRSESQPHVFAI-ADPAYQSMLDGYNN 52
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217303428 107 L-LFTYGVTGSGKTHTMTgspgegGLLPRCLDMIFNSIgsfqakryvfKSNDRNSMDIQCEVDALLERQKREAMP 180
Cdd:cd01363    53 QsIFAYGESGAGKTETMK------GVIPYLASVAFNGI----------NKGETEGWVYLTEITVTLEDQILQANP 111
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
28-157 5.65e-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: 49.53  E-value: 5.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428  28 VYCRVRPLGfpDQECCIEVINNTTvqlHTPEGYRLNRngdyketQYSFKQVFGTHTTQKELFDVVANpLVNDLIHGKNGL 107
Cdd:pfam16796  24 VFARVRPEL--LSEAQIDYPDETS---SDGKIGSKNK-------SFSFDRVFPPESEQEDVFQEISQ-LVQSCLDGYNVC 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217303428 108 LFTYGVTGSGKThtmtgspgeGGLLPRCLDMIFNSIGSFQAK-------RYVFKSND 157
Cdd:pfam16796  91 IFAYGQTGSGSN---------DGMIPRAREQIFRFISSLKKGwkytielQFVEIYNE 138
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
142-364 1.98e-03

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 41.65  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 142 SIGSFQAKRYVFKSNDR--NSMDIQCEVDALLERQKREAmpnpKTSSSKRQVDPEFADMITVQEFCKAEEV-----DEDS 214
Cdd:COG5059   351 EIEEIKFDLSEDRSEIEilVFREQSQLSQSSLSGIFAYM----QSLKKETETLKSRIDLIMKSIISGTFERkkllkEEGW 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217303428 215 VYGVFVSYIEIYNNYIYDLLEEvpfdpIKPKPPQSKL----LREDKNHNMyvagctevEVKSTEEAFEVFWRGQKKRRIA 290
Cdd:COG5059   427 KYKSTLQFLRIEIDRLLLLREE-----ELSKKKTKIHklnkLRHDLSSLL--------SSIPEETSDRVESEKASKLRSS 493
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217303428 291 NTH-LNRESSRSHSVFNIKLVQApldadgdnVLQEKEQITIsqlsLVDLAGSERtNRTRAEGNRLREAGNINQSL 364
Cdd:COG5059   494 ASTkLNLRSSRSHSKFRDHLNGS--------NSSTKELSLN----QVDLAGSER-KVSQSVGELLRETQSLNKSL 555
 
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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