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Conserved domains on  [gi|308153656|sp|Q9HAQ2|]
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RecName: Full=Kinesin-like protein KIF9

Protein Classification

kinesin family protein( domain architecture ID 10103649)

kinesin family protein which contains an ATPase-containing motor domain found in kinesins that provides the driving force in kinesin-mediated processes; similar to mouse KIF9 which is essential for its localization in the sperm flagellum

Gene Symbol:  KIF9
Gene Ontology:  GO:0007018|GO:0003777|GO:0005524
PubMed:  32842864|1618910

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
6-338 0e+00

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: 654.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   6 KVHAFVRVKPTDDFAHEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLHDASQDLVYETVAKDVVSQALDGY 85
Cdd:cd01375    1 KVQAFVRVRPTDDFAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDWSFKFDGVLHNASQELVYETVAKDVVSSALAGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  86 NGTIMCYGQTGAGKTYTMMGATENYKHRGILPRALQQVFRMIEERPTHAITVRVSYLEIYNESLFDLLSTLPYVGPSVTP 165
Cdd:cd01375   81 NGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPSVTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 166 MTIVEN-PQGVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEEKYITSKINLV 244
Cdd:cd01375  161 MTILEDsPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLSSEKYITSKLNLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 245 DLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKRDHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQL 324
Cdd:cd01375  241 DLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQL 320
                        330
                 ....*....|....
gi 308153656 325 EETLSSLRFASRMK 338
Cdd:cd01375  321 EETLSTLRFASRVK 334
 
Name Accession Description Interval E-value
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
6-338 0e+00

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: 654.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   6 KVHAFVRVKPTDDFAHEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLHDASQDLVYETVAKDVVSQALDGY 85
Cdd:cd01375    1 KVQAFVRVRPTDDFAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDWSFKFDGVLHNASQELVYETVAKDVVSSALAGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  86 NGTIMCYGQTGAGKTYTMMGATENYKHRGILPRALQQVFRMIEERPTHAITVRVSYLEIYNESLFDLLSTLPYVGPSVTP 165
Cdd:cd01375   81 NGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPSVTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 166 MTIVEN-PQGVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEEKYITSKINLV 244
Cdd:cd01375  161 MTILEDsPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLSSEKYITSKLNLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 245 DLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKRDHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQL 324
Cdd:cd01375  241 DLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQL 320
                        330
                 ....*....|....
gi 308153656 325 EETLSSLRFASRMK 338
Cdd:cd01375  321 EETLSTLRFASRVK 334
Kinesin pfam00225
Kinesin motor domain;
12-340 5.30e-132

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 395.40  E-value: 5.30e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   12 RVKPTDDFahEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLH-DASQDLVYETVAKDVVSQALDGYNGTIM 90
Cdd:pfam00225   1 RVRPLNER--EKERGSSVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDpEATQEDVYEETAKPLVESVLEGYNVTIF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   91 CYGQTGAGKTYTMMGATEnykHRGILPRALQQVFRMIEERPTH-AITVRVSYLEIYNESLFDLLSTLPyvgPSVTPMTIV 169
Cdd:pfam00225  79 AYGQTGSGKTYTMEGSDE---QPGIIPRALEDLFDRIQKTKERsEFSVKVSYLEIYNEKIRDLLSPSN---KNKRKLRIR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  170 ENPQ-GVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEEKYI-TSKINLVDLA 247
Cdd:pfam00225 153 EDPKkGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVkTGKLNLVDLA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  248 GSERLGKSG-SEGQVLKEATYINKSLSFLEQAIIALGDQKRDHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQLEE 326
Cdd:pfam00225 233 GSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEE 312
                         330
                  ....*....|....
gi 308153656  327 TLSSLRFASRMKLV 340
Cdd:pfam00225 313 TLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
10-347 5.56e-115

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: 351.49  E-value: 5.56e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656    10 FVRVKPTDDF-----AHEMIRYgDDKRSIDIHLKKDirrgvvNNQQTDWSFKLDGVL-HDASQDLVYETVAKDVVSQALD 83
Cdd:smart00129   5 VVRVRPLNKReksrkSPSVVPF-PDKVGKTLTVRSP------KNRQGEKKFTFDKVFdATASQEDVFEETAAPLVDSVLE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656    84 GYNGTIMCYGQTGAGKTYTMMGATEnykHRGILPRALQQVFRMIEER-PTHAITVRVSYLEIYNESLFDLLSTLPyvgps 162
Cdd:smart00129  78 GYNATIFAYGQTGSGKTYTMIGTPD---SPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLLNPSS----- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   163 vTPMTIVENPQ-GVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEEKYITSKI 241
Cdd:smart00129 150 -KKLEIREDEKgGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   242 NLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGD-QKRDHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGE 320
Cdd:smart00129 229 NLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPS 308
                          330       340
                   ....*....|....*....|....*..
gi 308153656   321 AAQLEETLSSLRFASRMKLVTTEPAIN 347
Cdd:smart00129 309 SSNLEETLSTLRFASRAKEIKNKPIVN 335
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
5-401 7.23e-70

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 240.41  E-value: 7.23e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   5 KKVHAFVRVKPTDdfahEMIRYGDDKRSIDIHLKKDIRrgvvnnqqtdwsFKLDGVLH-DASQDLVYETVAKDVVSQALD 83
Cdd:COG5059   24 IKSTIRIIPGELG----ERLINTSKKSHVSLEKSKEGT------------YAFDKVFGpSATQEDVYEETIKPLIDSLLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  84 GYNGTIMCYGQTGAGKTYTMMGateNYKHRGILPRALQQVFRMIEERP-THAITVRVSYLEIYNESLFDLLStlpyvgPS 162
Cdd:COG5059   88 GYNCTVFAYGQTGSGKTYTMSG---TEEEPGIIPLSLKELFSKLEDLSmTKDFAVSISYLEIYNEKIYDLLS------PN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 163 VTPMTIVENPQ-GVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEahSRTLSEEKYITSKI 241
Cdd:COG5059  159 EESLNIREDSLlGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELA--SKNKVSGTSETSKL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 242 NLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKR-DHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGE 320
Cdd:COG5059  237 SLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKsGHIPYRESKLTRLLQDSLGGNCNTRVICTISPS 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 321 AAQLEETLSSLRFASRMKLVTTEPAINekydaerMVKNLEKELALLKQELAIHDSLTNRtfvtydpmDEIQIAEINSQVR 400
Cdd:COG5059  317 SNSFEETINTLKFASRAKSIKNKIQVN-------SSSDSSREIEEIKFDLSEDRSEIEI--------LVFREQSQLSQSS 381

                 .
gi 308153656 401 R 401
Cdd:COG5059  382 L 382
PLN03188 PLN03188
kinesin-12 family protein; Provisional
7-348 6.86e-53

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 199.39  E-value: 6.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656    7 VHAFVRVKP-TDDFAHEMIRYGDDKRSIDIhlkkdirrgvvnNQQTdwsFKLDGVLH-DASQDLVYETVAKDVVSQALDG 84
Cdd:PLN03188  100 VKVIVRMKPlNKGEEGEMIVQKMSNDSLTI------------NGQT---FTFDSIADpESTQEDIFQLVGAPLVENCLAG 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   85 YNGTIMCYGQTGAGKTYTMMGAT-----ENYK--HRGILPRALQQVF-RMIEERPTHA-----ITVRVSYLEIYNESLFD 151
Cdd:PLN03188  165 FNSSVFAYGQTGSGKTYTMWGPAnglleEHLSgdQQGLTPRVFERLFaRINEEQIKHAdrqlkYQCRCSFLEIYNEQITD 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  152 LLStlpyvgPSVTPMTIVENPQ-GVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRT 230
Cdd:PLN03188  245 LLD------PSQKNLQIREDVKsGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKS 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  231 LSE--EKYITSKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGD----QKRDHIPFRQCKLTHALKDS 304
Cdd:PLN03188  319 VADglSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQES 398
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 308153656  305 LGGNCNMVLVTNIYGEAAQLEETLSSLRFASRMKLVTTEPAINE 348
Cdd:PLN03188  399 LGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNE 442
 
Name Accession Description Interval E-value
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
6-338 0e+00

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: 654.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   6 KVHAFVRVKPTDDFAHEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLHDASQDLVYETVAKDVVSQALDGY 85
Cdd:cd01375    1 KVQAFVRVRPTDDFAHEMIKYGEDGKSISIHLKKDLRRGVVNNQQEDWSFKFDGVLHNASQELVYETVAKDVVSSALAGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  86 NGTIMCYGQTGAGKTYTMMGATENYKHRGILPRALQQVFRMIEERPTHAITVRVSYLEIYNESLFDLLSTLPYVGPSVTP 165
Cdd:cd01375   81 NGTIFAYGQTGAGKTFTMTGGTENYKHRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPSVTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 166 MTIVEN-PQGVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEEKYITSKINLV 244
Cdd:cd01375  161 MTILEDsPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLSSEKYITSKLNLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 245 DLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKRDHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQL 324
Cdd:cd01375  241 DLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQL 320
                        330
                 ....*....|....
gi 308153656 325 EETLSSLRFASRMK 338
Cdd:cd01375  321 EETLSTLRFASRVK 334
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
6-338 1.29e-140

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: 417.43  E-value: 1.29e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   6 KVHAFVRVKPT----DDFAHEMIRYgDDKRSIDIHLKKdirrgvvNNQQTDWSFKLDGVLHD-ASQDLVYETVAKDVVSQ 80
Cdd:cd00106    1 NVRVAVRVRPLngreARSAKSVISV-DGGKSVVLDPPK-------NRVAPPKTFAFDAVFDStSTQEEVYEGTAKPLVDS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  81 ALDGYNGTIMCYGQTGAGKTYTMMGatENYKHRGILPRALQQVFRMIEERPT--HAITVRVSYLEIYNESLFDLLSTlpy 158
Cdd:cd00106   73 ALEGYNGTIFAYGQTGSGKTYTMLG--PDPEQRGIIPRALEDIFERIDKRKEtkSSFSVSASYLEIYNEKIYDLLSP--- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 159 vgPSVTPMTIVENP-QGVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEEKYI 237
Cdd:cd00106  148 --VPKKPLSLREDPkRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVT 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 238 TSKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKRDHIPFRQCKLTHALKDSLGGNCNMVLVTNI 317
Cdd:cd00106  226 SSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
                        330       340
                 ....*....|....*....|.
gi 308153656 318 YGEAAQLEETLSSLRFASRMK 338
Cdd:cd00106  306 SPSSENFEETLSTLRFASRAK 326
Kinesin pfam00225
Kinesin motor domain;
12-340 5.30e-132

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 395.40  E-value: 5.30e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   12 RVKPTDDFahEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLH-DASQDLVYETVAKDVVSQALDGYNGTIM 90
Cdd:pfam00225   1 RVRPLNER--EKERGSSVIVSVESVDSETVESSHLTNKNRTKTFTFDKVFDpEATQEDVYEETAKPLVESVLEGYNVTIF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   91 CYGQTGAGKTYTMMGATEnykHRGILPRALQQVFRMIEERPTH-AITVRVSYLEIYNESLFDLLSTLPyvgPSVTPMTIV 169
Cdd:pfam00225  79 AYGQTGSGKTYTMEGSDE---QPGIIPRALEDLFDRIQKTKERsEFSVKVSYLEIYNEKIRDLLSPSN---KNKRKLRIR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  170 ENPQ-GVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEEKYI-TSKINLVDLA 247
Cdd:pfam00225 153 EDPKkGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVkTGKLNLVDLA 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  248 GSERLGKSG-SEGQVLKEATYINKSLSFLEQAIIALGDQKRDHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQLEE 326
Cdd:pfam00225 233 GSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEE 312
                         330
                  ....*....|....
gi 308153656  327 TLSSLRFASRMKLV 340
Cdd:pfam00225 313 TLSTLRFASRAKNI 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
10-347 5.56e-115

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: 351.49  E-value: 5.56e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656    10 FVRVKPTDDF-----AHEMIRYgDDKRSIDIHLKKDirrgvvNNQQTDWSFKLDGVL-HDASQDLVYETVAKDVVSQALD 83
Cdd:smart00129   5 VVRVRPLNKReksrkSPSVVPF-PDKVGKTLTVRSP------KNRQGEKKFTFDKVFdATASQEDVFEETAAPLVDSVLE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656    84 GYNGTIMCYGQTGAGKTYTMMGATEnykHRGILPRALQQVFRMIEER-PTHAITVRVSYLEIYNESLFDLLSTLPyvgps 162
Cdd:smart00129  78 GYNATIFAYGQTGSGKTYTMIGTPD---SPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLLNPSS----- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   163 vTPMTIVENPQ-GVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEEKYITSKI 241
Cdd:smart00129 150 -KKLEIREDEKgGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   242 NLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGD-QKRDHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGE 320
Cdd:smart00129 229 NLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPS 308
                          330       340
                   ....*....|....*....|....*..
gi 308153656   321 AAQLEETLSSLRFASRMKLVTTEPAIN 347
Cdd:smart00129 309 SSNLEETLSTLRFASRAKEIKNKPIVN 335
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
10-341 2.69e-92

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: 292.19  E-value: 2.69e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  10 FVRVKP------TDDFAHemIRYGDDKRSIDIHLKKDIRRgvvnnqqtdWSFKLDGVLH-DASQDLVYETVAKDVVSqAL 82
Cdd:cd01366    7 FCRVRPllpseeNEDTSH--ITFPDEDGQTIELTSIGAKQ---------KEFSFDKVFDpEASQEDVFEEVSPLVQS-AL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  83 DGYNGTIMCYGQTGAGKTYTMMGATENykhRGILPRALQQVFRMIEERPTHAI--TVRVSYLEIYNESLFDLLSTLPYVG 160
Cdd:cd01366   75 DGYNVCIFAYGQTGSGKTYTMEGPPES---PGIIPRALQELFNTIKELKEKGWsyTIKASMLEIYNETIRDLLAPGNAPQ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 161 PsvtPMTIVENP--QGVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAhsRTLSEEKYIT 238
Cdd:cd01366  152 K---KLEIRHDSekGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISG--RNLQTGEISV 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 239 SKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGdQKRDHIPFRQCKLTHALKDSLGGNCNMVLVTNIY 318
Cdd:cd01366  227 GKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR-QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNIS 305
                        330       340
                 ....*....|....*....|...
gi 308153656 319 GEAAQLEETLSSLRFASRMKLVT 341
Cdd:cd01366  306 PAESNLNETLNSLRFASKVNSCE 328
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
54-338 2.42e-88

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: 281.91  E-value: 2.42e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  54 SFKLDGVLH-DASQDLVYETVAKDVVSQALDGYNGTIMCYGQTGAGKTYTMMGATENYKHRGILPRALQQVFRMIEERPT 132
Cdd:cd01369   44 TFSFDRVFDpNTTQEDVYNFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPESMGIIPRIVQDIFETIYSMDE 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 133 HA-ITVRVSYLEIYNESLFDLLstlpyvGPSVTPMTIVENP-QGVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMN 210
Cdd:cd01369  124 NLeFHVKVSYFEIYMEKIRDLL------DVSKTNLSVHEDKnRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMN 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 211 KNSSRSHCIFTIYLEahSRTLSEEKYITSKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKRDHI 290
Cdd:cd01369  198 EESSRSHSIFLINVK--QENVETEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKTHI 275
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 308153656 291 PFRQCKLTHALKDSLGGNCNMVLVTN----IYGEAaqleETLSSLRFASRMK 338
Cdd:cd01369  276 PYRDSKLTRILQDSLGGNSRTTLIICcspsSYNES----ETLSTLRFGQRAK 323
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
54-340 5.78e-88

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: 280.76  E-value: 5.78e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  54 SFKLDGVLHDASQDL-VYETVAKDVVSQALDGYNGTIMCYGQTGAGKTYTMMGateNYKHRGILPRALQQVFRMIEERPT 132
Cdd:cd01374   40 SFTFDHVFGGDSTNReVYELIAKPVVKSALEGYNGTIFAYGQTSSGKTFTMSG---DEDEPGIIPLAIRDIFSKIQDTPD 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 133 HAITVRVSYLEIYNESLFDLLStlpyvgPSVTPMTIVENP-QGVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNK 211
Cdd:cd01374  117 REFLLRVSYLEIYNEKINDLLS------PTSQNLKIRDDVeKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNE 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 212 NSSRSHCIFTIYLEAHSR-TLSEEKYITSKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKRD-H 289
Cdd:cd01374  191 RSSRSHTIFRITIESSERgELEEGTVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGgH 270
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 308153656 290 IPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQLEETLSSLRFASRMKLV 340
Cdd:cd01374  271 IPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
54-338 2.97e-82

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: 266.25  E-value: 2.97e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  54 SFKLDGVLH-DASQDLVYETVAKDVVSQALDGYNGTIMCYGQTGAGKTYTMMGATENYKHRGILPRALQQVFRMIEERP- 131
Cdd:cd01371   49 TFTFDAVFDpNSKQLDVYDETARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPELRGIIPNSFAHIFGHIARSQn 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 132 THAITVRVSYLEIYNESLFDLLSTLPyvgpsVTPMTIVENPQ-GVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMN 210
Cdd:cd01371  129 NQQFLVRVSYLEIYNEEIRDLLGKDQ-----TKRLELKERPDtGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMN 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 211 KNSSRSHCIFTIYLEAHSRTLSEEKYIT-SKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKRDH 289
Cdd:cd01371  204 EDSSRSHAIFTITIECSEKGEDGENHIRvGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKSTH 283
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 308153656 290 IPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQLEETLSSLRFASRMK 338
Cdd:cd01371  284 IPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAK 332
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
5-349 1.54e-80

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: 262.26  E-value: 1.54e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   5 KKVHAFVRVKPTDDF-----AHEMIRYGDDKRSIDIhlkkdiRRGVVNNQQTDWSFKLDGVL-HDASQDLVYETVAKDVV 78
Cdd:cd01364    2 KNIQVVVRCRPFNLRerkasSHSVVEVDPVRKEVSV------RTGGLADKSSTKTYTFDMVFgPEAKQIDVYRSVVCPIL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  79 SQALDGYNGTIMCYGQTGAGKTYTMMGATENYK--------HRGILPRALQQVFRMIEERPTHaITVRVSYLEIYNESLF 150
Cdd:cd01364   76 DEVLMGYNCTIFAYGQTGTGKTYTMEGDRSPNEeytweldpLAGIIPRTLHQLFEKLEDNGTE-YSVKVSYLEIYNEELF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 151 DLLSTLPYVGpsvTPMTIVENPQ---GVFIKGLS-VHLTSQEEdAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEA 226
Cdd:cd01364  155 DLLSPSSDVS---ERLRMFDDPRnkrGVIIKGLEeITVHNKDE-VYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHI 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 227 HSRTLSEEKYI-TSKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDqKRDHIPFRQCKLTHALKDSL 305
Cdd:cd01364  231 KETTIDGEELVkIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE-RAPHVPYRESKLTRLLQDSL 309
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 308153656 306 GGNCNMVLVTNIYGEAAQLEETLSSLRFASRMKLVTTEPAINEK 349
Cdd:cd01364  310 GGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
7-348 7.13e-79

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: 257.44  E-value: 7.13e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   7 VHAFVRVKPTDDfahemiryGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLH-DASQDLVYETVAKDVVSQALDGY 85
Cdd:cd01373    3 VKVFVRIRPPAE--------REGDGEYGQCLKKLSSDTLVLHSKPPKTFTFDHVADsNTNQESVFQSVGKPIVESCLSGY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  86 NGTIMCYGQTGAGKTYTMMGATE---NYKH--RGILPRALQQVFRMIE-ERPTH----AITVRVSYLEIYNESLFDLLSt 155
Cdd:cd01373   75 NGTIFAYGQTGSGKTYTMWGPSEsdnESPHglRGVIPRIFEYLFSLIQrEKEKAgegkSFLCKCSFLEIYNEQIYDLLD- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 156 lpyvgPSVTPMTIVENPQ-GVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEE 234
Cdd:cd01373  154 -----PASRNLKLREDIKkGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFV 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 235 KYITSKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQ---KRDHIPFRQCKLTHALKDSLGGNCNM 311
Cdd:cd01373  229 NIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVahgKQRHVCYRDSKLTFLLRDSLGGNAKT 308
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 308153656 312 VLVTNIYGEAAQLEETLSSLRFASRMKLVTTEPAINE 348
Cdd:cd01373  309 AIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNE 345
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
51-336 6.73e-78

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: 254.95  E-value: 6.73e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  51 TDWSFKLDGV-LHDASQDLVYETVAKDVVSQALDGYNGTIMCYGQTGAGKTYTMMGA---TENYKHRGILPRALQQVFRM 126
Cdd:cd01372   38 TDKSFTFDYVfDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAytaEEDEEQVGIIPRAIQHIFKK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 127 IEERP-THAITVRVSYLEIYNESLFDLLSTLPyvgPSVTPMTIVENPQG-VFIKGLS-VHLTSQEeDAFSLLFEGETNRI 203
Cdd:cd01372  118 IEKKKdTFEFQLKVSFLEIYNEEIRDLLDPET---DKKPTISIREDSKGgITIVGLTeVTVLSAE-DMMSCLEQGSLSRT 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 204 IASHTMNKNSSRSHCIFTIYLE--------AHSRTLSEEKYITSKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFL 275
Cdd:cd01372  194 TASTAMNSQSSRSHAIFTITLEqtkkngpiAPMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLAL 273
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308153656 276 EQAIIALGDQKRD--HIPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQLEETLSSLRFASR 336
Cdd:cd01372  274 GNVISALGDESKKgaHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANR 336
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
53-347 7.00e-78

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: 255.36  E-value: 7.00e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  53 WSFKLDGVlHDASQDLVYETVAKDVVSQALDGYNGTIMCYGQTGAGKTYTMMGATENykhRGILPRALQQVFRMIEERPT 132
Cdd:cd01365   61 WSHDSEDP-NYASQEQVYEDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQ---PGIIPRLCEDLFSRIADTTN 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 133 HAIT--VRVSYLEIYNESLFDLLStlPYVGPSVTPMTIVENP-QGVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTM 209
Cdd:cd01365  137 QNMSysVEVSYMEIYNEKVRDLLN--PKPKKNKGNLKVREHPvLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNM 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 210 NKNSSRSHCIFTIYL--EAHSRTLSEEKYITSKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQ-- 285
Cdd:cd01365  215 NDTSSRSHAVFTIVLtqKRHDAETNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMss 294
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 308153656 286 -----KRDHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQLEETLSSLRFASRMKLVTTEPAIN 347
Cdd:cd01365  295 gkskkKSSFIPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
13-338 6.02e-72

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: 239.17  E-value: 6.02e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  13 VKPTDDfahEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVL-HDASQDLVYETVAKDVVSQALDGYNGTIMC 91
Cdd:cd01370   24 VKVMDN---HMLVFDPKDEEDGFFHGGSNNRDRRKRRNKELKYVFDRVFdETSTQEEVYEETTKPLVDGVLNGYNATVFA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  92 YGQTGAGKTYTMMGaTENykHRGILPRALQQVFRMIEE-RPTHAITVRVSYLEIYNESLFDLLStlpyvgPSVTPMTIVE 170
Cdd:cd01370  101 YGATGAGKTHTMLG-TPQ--EPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNETIRDLLN------PSSGPLELRE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 171 NPQ-GVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEEKYITS-KINLVDLAG 248
Cdd:cd01370  172 DAQnGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTASINQQVRQgKLSLIDLAG 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 249 SERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKRD--HIPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQLEE 326
Cdd:cd01370  252 SERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKnkHIPYRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEE 331
                        330
                 ....*....|..
gi 308153656 327 TLSSLRFASRMK 338
Cdd:cd01370  332 THNTLKYANRAK 343
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
5-401 7.23e-70

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 240.41  E-value: 7.23e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   5 KKVHAFVRVKPTDdfahEMIRYGDDKRSIDIHLKKDIRrgvvnnqqtdwsFKLDGVLH-DASQDLVYETVAKDVVSQALD 83
Cdd:COG5059   24 IKSTIRIIPGELG----ERLINTSKKSHVSLEKSKEGT------------YAFDKVFGpSATQEDVYEETIKPLIDSLLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  84 GYNGTIMCYGQTGAGKTYTMMGateNYKHRGILPRALQQVFRMIEERP-THAITVRVSYLEIYNESLFDLLStlpyvgPS 162
Cdd:COG5059   88 GYNCTVFAYGQTGSGKTYTMSG---TEEEPGIIPLSLKELFSKLEDLSmTKDFAVSISYLEIYNEKIYDLLS------PN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 163 VTPMTIVENPQ-GVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEahSRTLSEEKYITSKI 241
Cdd:COG5059  159 EESLNIREDSLlGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELA--SKNKVSGTSETSKL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 242 NLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKR-DHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGE 320
Cdd:COG5059  237 SLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKsGHIPYRESKLTRLLQDSLGGNCNTRVICTISPS 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 321 AAQLEETLSSLRFASRMKLVTTEPAINekydaerMVKNLEKELALLKQELAIHDSLTNRtfvtydpmDEIQIAEINSQVR 400
Cdd:COG5059  317 SNSFEETINTLKFASRAKSIKNKIQVN-------SSSDSSREIEEIKFDLSEDRSEIEI--------LVFREQSQLSQSS 381

                 .
gi 308153656 401 R 401
Cdd:COG5059  382 L 382
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
6-334 1.31e-58

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: 203.01  E-value: 1.31e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   6 KVHAFVRVKPtddFAHEMIRYGD-------DKRSIDIHLKKDIR----RGVVNNQQTDWSFKldGVLH-DASQDLVYETV 73
Cdd:cd01368    2 PVKVYLRVRP---LSKDELESEDegcieviNSTTVVLHPPKGSAanksERNGGQKETKFSFS--KVFGpNTTQKEFFQGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  74 AKDVVSQALDGYNGTIMCYGQTGAGKTYTMMGateNYKHRGILPRALQQVFRMIEErpthaITVRVSYLEIYNESLFDLL 153
Cdd:cd01368   77 ALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQG---SPGDGGILPRSLDVIFNSIGG-----YSVFVSYIEIYNEYIYDLL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 154 STLPYVGPSVTPMTIVENPQ--GVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTL 231
Cdd:cd01368  149 EPSPSSPTKKRQSLRLREDHngNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDS 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 232 SEEKYI------TSKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIAL----GDQKRDHIPFRQCKLTHAL 301
Cdd:cd01368  229 DGDVDQdkdqitVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLrenqLQGTNKMVPFRDSKLTHLF 308
                        330       340       350
                 ....*....|....*....|....*....|...
gi 308153656 302 KDSLGGNCNMVLVTNIYGEAAQLEETLSSLRFA 334
Cdd:cd01368  309 QNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
7-338 4.17e-53

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: 186.94  E-value: 4.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   7 VHAFVRVKPTDDFAHEmiryGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLHD-ASQDLVYETVAKDVVSQALDGY 85
Cdd:cd01376    2 VRVAVRVRPFVDGTAG----ASDPSCVSGIDSCSVELADPRNHGETLKYQFDAFYGEeSTQEDIYAREVQPIVPHLLEGQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  86 NGTIMCYGQTGAGKTYTMMGATENYkhrGILPRALQQVFRMIEERpTHAITVRVSYLEIYNESLFDLLStlpyvgPSVTP 165
Cdd:cd01376   78 NATVFAYGSTGAGKTFTMLGSPEQP---GLMPLTVMDLLQMTRKE-AWALSFTMSYLEIYQEKILDLLE------PASKE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 166 MTIVENPQG-VFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRtLSEEKYITSKINLV 244
Cdd:cd01376  148 LVIREDKDGnILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRER-LAPFRQRTGKLNLI 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 245 DLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALgDQKRDHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQL 324
Cdd:cd01376  227 DLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL-NKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFY 305
                        330
                 ....*....|....
gi 308153656 325 EETLSSLRFASRMK 338
Cdd:cd01376  306 QDTLSTLNFAARSR 319
PLN03188 PLN03188
kinesin-12 family protein; Provisional
7-348 6.86e-53

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 199.39  E-value: 6.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656    7 VHAFVRVKP-TDDFAHEMIRYGDDKRSIDIhlkkdirrgvvnNQQTdwsFKLDGVLH-DASQDLVYETVAKDVVSQALDG 84
Cdd:PLN03188  100 VKVIVRMKPlNKGEEGEMIVQKMSNDSLTI------------NGQT---FTFDSIADpESTQEDIFQLVGAPLVENCLAG 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   85 YNGTIMCYGQTGAGKTYTMMGAT-----ENYK--HRGILPRALQQVF-RMIEERPTHA-----ITVRVSYLEIYNESLFD 151
Cdd:PLN03188  165 FNSSVFAYGQTGSGKTYTMWGPAnglleEHLSgdQQGLTPRVFERLFaRINEEQIKHAdrqlkYQCRCSFLEIYNEQITD 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  152 LLStlpyvgPSVTPMTIVENPQ-GVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRT 230
Cdd:PLN03188  245 LLD------PSQKNLQIREDVKsGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKS 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  231 LSE--EKYITSKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGD----QKRDHIPFRQCKLTHALKDS 304
Cdd:PLN03188  319 VADglSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqtGKQRHIPYRDSRLTFLLQES 398
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 308153656  305 LGGNCNMVLVTNIYGEAAQLEETLSSLRFASRMKLVTTEPAINE 348
Cdd:PLN03188  399 LGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNE 442
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
6-338 4.65e-52

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: 184.42  E-value: 4.65e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   6 KVHAFVRVKPTDDFAHEMIRYG----DDKRSIDIHLKK---DIRRGVVNNqqtdwSFKLDGVLHD-ASQDLVYETVAKDV 77
Cdd:cd01367    1 KIKVCVRKRPLNKKEVAKKEIDvvsvPSKLTLIVHEPKlkvDLTKYIENH-----TFRFDYVFDEsSSNETVYRSTVKPL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  78 VSQALDGYNGTIMCYGQTGAGKTYTMMGA-TENYKHRGILPRALQQVFRMIEERPTH-AITVRVSYLEIYNESLFDLLSt 155
Cdd:cd01367   76 VPHIFEGGKATCFAYGQTGSGKTYTMGGDfSGQEESKGIYALAARDVFRLLNKLPYKdNLGVTVSFFEIYGGKVFDLLN- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 156 lpyvgpSVTPMTIVENPQG-VFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHsrtlseE 234
Cdd:cd01367  155 ------RKKRVRLREDGKGeVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDR------G 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 235 KYITS-KINLVDLAGSER-LGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKRdHIPFRQCKLTHALKDSL-GGNCNM 311
Cdd:cd01367  223 TNKLHgKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQNKA-HIPFRGSKLTQVLKDSFiGENSKT 301
                        330       340
                 ....*....|....*....|....*..
gi 308153656 312 VLVTNIYGEAAQLEETLSSLRFASRMK 338
Cdd:cd01367  302 CMIATISPGASSCEHTLNTLRYADRVK 328
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
64-255 5.73e-13

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: 67.76  E-value: 5.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  64 ASQDLVYEtVAKDVVSQALDGYNG-TIMCYGQTGAGKTYTMMgatenykhrGILPRALQQVFrmieerpthaitvrvSYL 142
Cdd:cd01363   30 ESQPHVFA-IADPAYQSMLDGYNNqSIFAYGESGAGKTETMK---------GVIPYLASVAF---------------NGI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 143 EIYNESLFDLLStlpyvgpsvtpmtivenpqgvFIKGLSvhltsqEEDAFSLLFEGETNRiIASHTMNKNSSRSHCIFTI 222
Cdd:cd01363   85 NKGETEGWVYLT---------------------EITVTL------EDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI 136
                        170       180       190
                 ....*....|....*....|....*....|...
gi 308153656 223 yleahsrtlseekyitskinLVDLAGSERLGKS 255
Cdd:cd01363  137 --------------------LLDIAGFEIINES 149
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
54-153 4.06e-11

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 61.47  E-value: 4.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656   54 SFKLDGVL-HDASQDLVYETVAKDVVSqALDGYNGTIMCYGQTGAGKTytmmgatenykhRGILPRALQQVFRMIEERPT 132
Cdd:pfam16796  56 SFSFDRVFpPESEQEDVFQEISQLVQS-CLDGYNVCIFAYGQTGSGSN------------DGMIPRAREQIFRFISSLKK 122
                          90       100
                  ....*....|....*....|..
gi 308153656  133 HA-ITVRVSYLEIYNESLFDLL 153
Cdd:pfam16796 123 GWkYTIELQFVEIYNESSQDLL 144
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
21-284 8.32e-04

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 42.80  E-value: 8.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656  21 HEMIRYGDDKRSIDIHLkkdIRRGVVNNQQTDWSFKLDGVLHDASQDLVYETVAKDVVSQALDGYNGtimcYGQTGAGKT 100
Cdd:COG5059  324 INTLKFASRAKSIKNKI---QVNSSSDSSREIEEIKFDLSEDRSEIEILVFREQSQLSQSSLSGIFA----YMQSLKKET 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 101 YTMmgatenyKHRGILprALQQVFRMIEERPTHAITVRVSYLEIyNESLFDLLSTLPYVGPSVTPMTIVENPQGVFIKGL 180
Cdd:COG5059  397 ETL-------KSRIDL--IMKSIISGTFERKKLLKEEGWKYKST-LQFLRIEIDRLLLLREEELSKKKTKIHKLNKLRHD 466
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308153656 181 SVHLTSQEEDAFSLLFEGETN---RIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEEkyitsKINLVDLAGSERLgKSGS 257
Cdd:COG5059  467 LSSLLSSIPEETSDRVESEKAsklRSSASTKLNLRSSRSHSKFRDHLNGSNSSTKEL-----SLNQVDLAGSERK-VSQS 540
                        250       260
                 ....*....|....*....|....*..
gi 308153656 258 EGQVLKEATYINKSLSFLEQAIIALGD 284
Cdd:COG5059  541 VGELLRETQSLNKSLSSLGDVIHALGS 567
 
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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