NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17554190|ref|NP_498069|]
View 

Kinesin-like protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 5-365 0e+00

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: 600.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   5 DSIIVAVRVRPFNDREKTRNCKLVIEMPDEETTVIRDPK--------TNDEKRFTYDHSYWSHDgfsekkngylePTDPH 76
Cdd:cd01365   1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkatREVPKSFSFDYSYWSHD-----------SEDPN 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  77 YADQRRVFEDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELFKQIADNKKKNMQFEVFVSMME 156
Cdd:cd01365  70 YASQEQVYEDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYME 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 157 IYCEKVRDLLSSTPP-PKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITF 235
Cdd:cd01365 150 IYNEKVRDLLNPKPKkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVL 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 236 NQKSSKQAGG-TSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDSQKAKSGKK-TQIPYRDS 313
Cdd:cd01365 230 TQKRHDAETNlTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSKKKsSFIPYRDS 309

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 17554190 314 VLTCLLKNALGGNSKTIMIAAISPADINFEETLSTLRFADRAKSIKTNAVVN 365
Cdd:cd01365 310 VLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
 450-552 2.10e-46

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


:

Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 161.23  E-value: 2.10e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 450 CHLWNLNEDPALTNVIVHFIPVGESVVGNKPTSSGNFIQMSGLSILPQHVTLKNDgNNQIHLSPCSEDLDIFINGKPVHG 529
Cdd:cd22709   1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNT-DGKVTIEPVSPGAKVIVNGVPVTG 79

                        90       100
                ....*....|....*....|...
gi 17554190 530 ETQLQQNDRVFFGGNHLYVFNNP 552
Cdd:cd22709  80 ETELHHLDRVILGSNHLYVFVGP 102
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
 659-699 6.33e-08

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


:

Pssm-ID: 463574  Cd Length: 43  Bit Score: 49.52  E-value: 6.33e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 17554190   659 FMNRYYGMQEMYEAKQDGSEDWNMPKERDPFYEPPDSPVFI 699
Cdd:pfam12423   1 LENRLVDMREMYQEYKEGEYSQHFEVDRDPFYEPPENHNLI 41
tolA super family cl35847
cell envelope integrity inner membrane protein TolA; Provisional
 366-446 2.21e-03

cell envelope integrity inner membrane protein TolA; Provisional


The actual alignment was detected with superfamily member PRK09510:

Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  366 ENQTERALRELREENLRLQSQIQggtagdasneEIEKLRRQLAENQKEMEEMEK--SWQQKIAEEAA-KHASGASEKVEM 442
Cdd:PRK09510  82 KKKEQQQAEELQQKQAAEQERLK----------QLEKERLAAQEQKKQAEEAAKqaALKQKQAEEAAaKAAAAAKAKAEA 151


                 ....
gi 17554190  443 EAKK 446
Cdd:PRK09510 152 EAKR 155
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 5-365 0e+00

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: 600.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   5 DSIIVAVRVRPFNDREKTRNCKLVIEMPDEETTVIRDPK--------TNDEKRFTYDHSYWSHDgfsekkngylePTDPH 76
Cdd:cd01365   1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkatREVPKSFSFDYSYWSHD-----------SEDPN 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  77 YADQRRVFEDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELFKQIADNKKKNMQFEVFVSMME 156
Cdd:cd01365  70 YASQEQVYEDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYME 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 157 IYCEKVRDLLSSTPP-PKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITF 235
Cdd:cd01365 150 IYNEKVRDLLNPKPKkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVL 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 236 NQKSSKQAGG-TSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDSQKAKSGKK-TQIPYRDS 313
Cdd:cd01365 230 TQKRHDAETNlTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSKKKsSFIPYRDS 309

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 17554190 314 VLTCLLKNALGGNSKTIMIAAISPADINFEETLSTLRFADRAKSIKTNAVVN 365
Cdd:cd01365 310 VLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 6-365 6.45e-154

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: 456.26  E-value: 6.45e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190      6 SIIVAVRVRPFNDREKTRNCKLVIEMPDE---ETTVIRDPKTNDEKRFTYDHSYwshdgfsekkngyleptdPHYADQRR 82
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKvgkTLTVRSPKNRQGEKKFTFDKVF------------------DATASQED 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190     83 VFEDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELFKQIaDNKKKNMQFEVFVSMMEIYCEKV 162
Cdd:smart00129  63 VFEETAAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKI 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190    163 RDLLSSTPPPkggLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQKSsKQ 242
Cdd:smart00129 142 RDLLNPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKI-KN 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190    243 AGGTSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALhdsqkAKSGKKTQIPYRDSVLTCLLKNA 322
Cdd:smart00129 218 SSSGSGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINAL-----AQHSKSRHIPYRDSKLTRLLQDS 292

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 17554190    323 LGGNSKTIMIAAISPADINFEETLSTLRFADRAKSIKTNAVVN 365
Cdd:smart00129 293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
12-358 1.70e-132

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 400.41  E-value: 1.70e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190    12 RVRPFNDREKTRNCKLVIEMPD---EETTVIRDPKTNDEKRFTYDHSYWSHdgfsekkngyleptdphyADQRRVFEDLG 88
Cdd:pfam00225   1 RVRPLNEREKERGSSVIVSVESvdsETVESSHLTNKNRTKTFTFDKVFDPE------------------ATQEDVYEETA 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190    89 RGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELFKQIaDNKKKNMQFEVFVSMMEIYCEKVRDLLSS 168
Cdd:pfam00225  63 KPLVESVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRI-QKTKERSEFSVKVSYLEIYNEKIRDLLSP 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   169 TPPPKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQKSSKQAGGTSM 248
Cdd:pfam00225 142 SNKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   249 KKSEINLVDLAGSERQSAAG-TEGDRLKEGIVINQSLTTLGRVIKALHDsqkaksGKKTQIPYRDSVLTCLLKNALGGNS 327
Cdd:pfam00225 222 KTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD------KKSKHIPYRDSKLTRLLQDSLGGNS 295

                         330       340       350
                  ....*....|....*....|....*....|.
gi 17554190   328 KTIMIAAISPADINFEETLSTLRFADRAKSI 358
Cdd:pfam00225 296 KTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
12-420 7.17e-78

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 264.68  E-value: 7.17e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  12 RVRPFNDREKTRNCKLVIEMPDEETTVIR--------DPKTNDEKRFTYDHSYwshdgfsekkngyleptDPHyADQRRV 83
Cdd:COG5059  12 RLSSRNEKSVSDIKSTIRIIPGELGERLIntskkshvSLEKSKEGTYAFDKVF-----------------GPS-ATQEDV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  84 FEDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELFKQIaDNKKKNMQFEVFVSMMEIYCEKVR 163
Cdd:COG5059  74 YEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL-EDLSMTKDFAVSISYLEIYNEKIY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 164 DLLSSTPPpkgGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQKSSKqa 243
Cdd:COG5059 153 DLLSPNEE---SLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKV-- 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 244 GGTSmKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDSQKAKSgkktqIPYRDSVLTCLLKNAL 323
Cdd:COG5059 228 SGTS-ETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSGH-----IPYRESKLTRLLQDSL 301

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 324 GGNSKTIMIAAISPADINFEETLSTLRFADRAKSIKTNAVVNENQ--------TERALRELREENLRLQSQIQGGTagda 395
Cdd:COG5059 302 GGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSdssreieeIKFDLSEDRSEIEILVFREQSQL---- 377

                       410       420
                ....*....|....*....|....*
gi 17554190 396 SNEEIEKLRRQLAENQKEMEEMEKS 420
Cdd:COG5059 378 SQSSLSGIFAYMQSLKKETETLKSR 402
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 9-407 1.57e-68

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 249.47  E-value: 1.57e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190     9 VAVRVRPFNDrektrncklviempDEETTVIRDPKTND-----EKRFTYDhsywshdgfsekkngylEPTDPHyADQRRV 83
Cdd:PLN03188  102 VIVRMKPLNK--------------GEEGEMIVQKMSNDsltinGQTFTFD-----------------SIADPE-STQEDI 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190    84 FEDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKN----------NKGIVPIVCEELFKQIADNKKKN----MQFE 149
Cdd:PLN03188  150 FQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPANglleehlsgdQQGLTPRVFERLFARINEEQIKHadrqLKYQ 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   150 VFVSMMEIYCEKVRDLLSstpPPKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHT 229
Cdd:PLN03188  230 CRCSFLEIYNEQITDLLD---PSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHS 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   230 IVKITFNQKSSKQAGG-TSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALhdSQKAKSGKKTQI 308
Cdd:PLN03188  307 VFTCVVESRCKSVADGlSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINIL--AEISQTGKQRHI 384

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   309 PYRDSVLTCLLKNALGGNSKTIMIAAISPADINFEETLSTLRFADRAKSIKTNAVVNE------NQTERALRELREENLR 382
Cdd:PLN03188  385 PYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqddvNFLREVIRQLRDELQR 464

                         410       420
                  ....*....|....*....|....*
gi 17554190   383 LQSQIQGGTAGDASNEEIEKLRRQL 407
Cdd:PLN03188  465 VKANGNNPTNPNVAYSTAWNARRSL 489
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
 450-552 2.10e-46

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 161.23  E-value: 2.10e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 450 CHLWNLNEDPALTNVIVHFIPVGESVVGNKPTSSGNFIQMSGLSILPQHVTLKNDgNNQIHLSPCSEDLDIFINGKPVHG 529
Cdd:cd22709   1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNT-DGKVTIEPVSPGAKVIVNGVPVTG 79

                        90       100
                ....*....|....*....|...
gi 17554190 530 ETQLQQNDRVFFGGNHLYVFNNP 552
Cdd:cd22709  80 ETELHHLDRVILGSNHLYVFVGP 102
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
 659-699 6.33e-08

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


Pssm-ID: 463574  Cd Length: 43  Bit Score: 49.52  E-value: 6.33e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 17554190   659 FMNRYYGMQEMYEAKQDGSEDWNMPKERDPFYEPPDSPVFI 699
Cdd:pfam12423   1 LENRLVDMREMYQEYKEGEYSQHFEVDRDPFYEPPENHNLI 41
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 475-539 4.44e-04

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 39.48  E-value: 4.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17554190   475 VVGNKPTSSgnfIQMSGLSILPQHVTLKNDGNNQIHLSPCSEDLDIFINGKPVHGE-TQLQQNDRV 539
Cdd:pfam00498   2 TIGRSPDCD---IVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTNGTFVNGQRLGPEpVRLKDGDVI 64
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
482-548 1.04e-03

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 39.17  E-value: 1.04e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17554190 482 SSGNFIQMSGLSILPQHVTLKNDGNnQIHLspcsEDLD----IFINGKPVHGETQLQQNDRVFFGGNHLYV 548
Cdd:COG1716  28 APDNDIVLDDPTVSRRHARIRRDGG-GWVL----EDLGstngTFVNGQRVTEPAPLRDGDVIRLGKTELRF 93
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 366-446 2.21e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  366 ENQTERALRELREENLRLQSQIQggtagdasneEIEKLRRQLAENQKEMEEMEK--SWQQKIAEEAA-KHASGASEKVEM 442
Cdd:PRK09510  82 KKKEQQQAEELQQKQAAEQERLK----------QLEKERLAAQEQKKQAEEAAKqaALKQKQAEEAAaKAAAAAKAKAEA 151


                 ....
gi 17554190  443 EAKK 446
Cdd:PRK09510 152 EAKR 155
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 487-527 3.44e-03

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 36.39  E-value: 3.44e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 17554190    487 IQMSGLSILPQHVTLKNDGNNQIHLSPCSEDLDIFINGKPV 527
Cdd:smart00240  12 IQLDGPSISRRHAVIVYDGGGRFYLIDLGSTNGTFVNGKRI 52
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 338-448 4.01e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 4.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190    338 ADINFEETLSTLRFADRAKSIKTNAVVNENQTERALRELREENLRLQSQIQGGTAgdasneEIEKLRRQLAENQKEMEEM 417
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEA------EIASLERSIAEKERELEDA 320

                           90       100       110
                   ....*....|....*....|....*....|.
gi 17554190    418 EKSWQQKIAEEAAKHASGASEKVEMEAKKKK 448
Cdd:TIGR02169  321 EERLAKLEAEIDKLLAEIEELEREIEEERKR 351
Kinesin_assoc pfam16183
Kinesin-associated;
394-472 6.17e-03

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 38.67  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   394 DASNEEIEKLRrqlaENQKEMEEMEKSWQQKIAEEAAKH----ASGASEKVEMEA--------KKKKMCHLWNLNEDPAL 461
Cdd:pfam16183  90 PGSEEAIERLK----ETEKIIAELNETWEEKLRKTEAIRmereALLAEMGVAIREdggtlgvfSPKKTPHLVNLNEDPLM 165

                          90
                  ....*....|.
gi 17554190   462 TNVIVHFIPVG 472
Cdd:pfam16183 166 SECLLYYIKDG 176
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 5-365 0e+00

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: 600.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   5 DSIIVAVRVRPFNDREKTRNCKLVIEMPDEETTVIRDPK--------TNDEKRFTYDHSYWSHDgfsekkngylePTDPH 76
Cdd:cd01365   1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkatREVPKSFSFDYSYWSHD-----------SEDPN 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  77 YADQRRVFEDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELFKQIADNKKKNMQFEVFVSMME 156
Cdd:cd01365  70 YASQEQVYEDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYME 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 157 IYCEKVRDLLSSTPP-PKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITF 235
Cdd:cd01365 150 IYNEKVRDLLNPKPKkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVL 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 236 NQKSSKQAGG-TSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDSQKAKSGKK-TQIPYRDS 313
Cdd:cd01365 230 TQKRHDAETNlTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSKKKsSFIPYRDS 309

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 17554190 314 VLTCLLKNALGGNSKTIMIAAISPADINFEETLSTLRFADRAKSIKTNAVVN 365
Cdd:cd01365 310 VLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 6-365 6.45e-154

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: 456.26  E-value: 6.45e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190      6 SIIVAVRVRPFNDREKTRNCKLVIEMPDE---ETTVIRDPKTNDEKRFTYDHSYwshdgfsekkngyleptdPHYADQRR 82
Cdd:smart00129   1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKvgkTLTVRSPKNRQGEKKFTFDKVF------------------DATASQED 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190     83 VFEDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELFKQIaDNKKKNMQFEVFVSMMEIYCEKV 162
Cdd:smart00129  63 VFEETAAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKI 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190    163 RDLLSSTPPPkggLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQKSsKQ 242
Cdd:smart00129 142 RDLLNPSSKK---LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKI-KN 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190    243 AGGTSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALhdsqkAKSGKKTQIPYRDSVLTCLLKNA 322
Cdd:smart00129 218 SSSGSGKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINAL-----AQHSKSRHIPYRDSKLTRLLQDS 292

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 17554190    323 LGGNSKTIMIAAISPADINFEETLSTLRFADRAKSIKTNAVVN 365
Cdd:smart00129 293 LGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
12-358 1.70e-132

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 400.41  E-value: 1.70e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190    12 RVRPFNDREKTRNCKLVIEMPD---EETTVIRDPKTNDEKRFTYDHSYWSHdgfsekkngyleptdphyADQRRVFEDLG 88
Cdd:pfam00225   1 RVRPLNEREKERGSSVIVSVESvdsETVESSHLTNKNRTKTFTFDKVFDPE------------------ATQEDVYEETA 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190    89 RGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELFKQIaDNKKKNMQFEVFVSMMEIYCEKVRDLLSS 168
Cdd:pfam00225  63 KPLVESVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRI-QKTKERSEFSVKVSYLEIYNEKIRDLLSP 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   169 TPPPKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQKSSKQAGGTSM 248
Cdd:pfam00225 142 SNKNKRKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   249 KKSEINLVDLAGSERQSAAG-TEGDRLKEGIVINQSLTTLGRVIKALHDsqkaksGKKTQIPYRDSVLTCLLKNALGGNS 327
Cdd:pfam00225 222 KTGKLNLVDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD------KKSKHIPYRDSKLTRLLQDSLGGNS 295

                         330       340       350
                  ....*....|....*....|....*....|.
gi 17554190   328 KTIMIAAISPADINFEETLSTLRFADRAKSI 358
Cdd:pfam00225 296 KTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 6-356 5.81e-126

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: 383.53  E-value: 5.81e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   6 SIIVAVRVRPFNDREKTRnCKLVIEMPDEETTVIRDPKTND--EKRFTYDHSYWSHdgfsekkngyleptdphyADQRRV 83
Cdd:cd00106   1 NVRVAVRVRPLNGREARS-AKSVISVDGGKSVVLDPPKNRVapPKTFAFDAVFDST------------------STQEEV 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  84 FEDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVG-FKNNKGIVPIVCEELFKQIADNKKKNMQFEVFVSMMEIYCEKV 162
Cdd:cd00106  62 YEGTAKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGpDPEQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKI 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 163 RDLLSstPPPKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQKSSKQ 242
Cdd:cd00106 142 YDLLS--PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREK 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 243 AGGTSmKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDsqkaksGKKTQIPYRDSVLTCLLKNA 322
Cdd:cd00106 220 SGESV-TSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD------GQNKHIPYRDSKLTRLLQDS 292

                       330       340       350
                ....*....|....*....|....*....|....
gi 17554190 323 LGGNSKTIMIAAISPADINFEETLSTLRFADRAK 356
Cdd:cd00106 293 LGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 6-359 1.64e-103

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: 325.44  E-value: 1.64e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   6 SIIVAVRVRPFNDREKTRNCKLVIEMPDEETTVIrdpkTNDEKRFTYDHSYwshdgfsekkngyleptDPHyADQRRVFE 85
Cdd:cd01372   2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVT----VGTDKSFTFDYVF-----------------DPS-TEQEEVYN 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  86 DLGRGVLANAWAGYNCSLFAYGQTGSGKSYSI-VGFKNN-----KGIVPIVCEELFKQIaDNKKKNMQFEVFVSMMEIYC 159
Cdd:cd01372  60 TCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMgTAYTAEedeeqVGIIPRAIQHIFKKI-EKKKDTFEFQLKVSFLEIYN 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 160 EKVRDLLSSTPPPKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQK- 238
Cdd:cd01372 139 EEIRDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTk 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 239 ------SSKQAGGTSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDSQKaksgKKTQIPYRD 312
Cdd:cd01372 219 kngpiaPMSADDKNSTFTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESK----KGAHVPYRD 294

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 17554190 313 SVLTCLLKNALGGNSKTIMIAAISPADINFEETLSTLRFADRAKSIK 359
Cdd:cd01372 295 SKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 6-358 1.23e-99

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: 315.44  E-value: 1.23e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   6 SIIVAVRVRPFNDREKTRNCKLVIEMPDEETTVIrDPKTNDEKRFTYDHSYWSHDGFSEKKNGYL--EPTDPhYADQRRV 83
Cdd:cd01370   1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVF-DPKDEEDGFFHGGSNNRDRRKRRNKELKYVfdRVFDE-TSTQEEV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  84 FEDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELFKQIaDNKKKNMQFEVFVSMMEIYCEKVR 163
Cdd:cd01370  79 YEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRI-ESLKDEKEFEVSMSYLEIYNETIR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 164 DLLSstpPPKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQKSSKQA 243
Cdd:cd01370 158 DLLN---PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTAS 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 244 GGTSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDSqkakSGKKTQIPYRDSVLTCLLKNAL 323
Cdd:cd01370 235 INQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADP----GKKNKHIPYRDSKLTRLLKDSL 310

                       330       340       350
                ....*....|....*....|....*....|....*
gi 17554190 324 GGNSKTIMIAAISPADINFEETLSTLRFADRAKSI 358
Cdd:cd01370 311 GGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 5-358 2.84e-99

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: 314.01  E-value: 2.84e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   5 DSIIVAVRVRPFNDREKTRNCKLVIEM-PDEETTVIRDPK-TNDE--KRFTYDHSYwshdgfsekkngyleptDPHyADQ 80
Cdd:cd01371   1 ENVKVVVRCRPLNGKEKAAGALQIVDVdEKRGQVSVRNPKaTANEppKTFTFDAVF-----------------DPN-SKQ 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  81 RRVFEDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNN---KGIVPIVCEELFKQIAdNKKKNMQFEVFVSMMEI 157
Cdd:cd01371  63 LDVYDETARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDpelRGIIPNSFAHIFGHIA-RSQNNQQFLVRVSYLEI 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 158 YCEKVRDLLSSTPPPKggLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQ 237
Cdd:cd01371 142 YNEEIRDLLGKDQTKR--LELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIEC 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 238 KSSKQAGGTSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDsqkaksGKKTQIPYRDSVLTC 317
Cdd:cd01371 220 SEKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD------GKSTHIPYRDSKLTR 293

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 17554190 318 LLKNALGGNSKTIMIAAISPADINFEETLSTLRFADRAKSI 358
Cdd:cd01371 294 LLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 3-359 1.52e-96

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: 306.44  E-value: 1.52e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   3 KGdSIIVAVRVRPFNDREKTRNCKlVIEMPDEETTVIRDPKTND-EKRFTYDHSYwshdgfsekkngyleptdPHYADQR 81
Cdd:cd01366   1 KG-NIRVFCRVRPLLPSEENEDTS-HITFPDEDGQTIELTSIGAkQKEFSFDKVF------------------DPEASQE 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  82 RVFEDLGRGVLAnAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELFKQIADNKKKNMQFEVFVSMMEIYCEK 161
Cdd:cd01366  61 DVFEEVSPLVQS-ALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNET 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 162 VRDLLSSTPPPKGGLKVR-EHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKIT---FNQ 237
Cdd:cd01366 140 IRDLLAPGNAPQKKLEIRhDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHisgRNL 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 238 KSSKQAGGTsmkkseINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALhdsqkakSGKKTQIPYRDSVLTC 317
Cdd:cd01366 220 QTGEISVGK------LNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL-------RQKQSHIPYRNSKLTY 286

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 17554190 318 LLKNALGGNSKTIMIAAISPADINFEETLSTLRFADRAKSIK 359
Cdd:cd01366 287 LLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCE 328
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 6-358 2.16e-94

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: 300.79  E-value: 2.16e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   6 SIIVAVRVRPFNDREKTRNCKlVIEMPDEETTVIRDPKTNdekRFTYDHSYWSHdgfsekkngyleptdphyADQRRVFE 85
Cdd:cd01374   1 KITVTVRVRPLNSREIGINEQ-VAWEIDNDTIYLVEPPST---SFTFDHVFGGD------------------STNREVYE 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  86 DLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELFKQIADNKKKNmqFEVFVSMMEIYCEKVRDL 165
Cdd:cd01374  59 LIAKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDRE--FLLRVSYLEIYNEKINDL 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 166 LSSTPPPkggLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQKSSKQAGG 245
Cdd:cd01374 137 LSPTSQN---LKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEE 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 246 TSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDSQKAKsgkktQIPYRDSVLTCLLKNALGG 325
Cdd:cd01374 214 GTVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGG-----HIPYRDSKLTRILQPSLGG 288

                       330       340       350
                ....*....|....*....|....*....|...
gi 17554190 326 NSKTIMIAAISPADINFEETLSTLRFADRAKSI 358
Cdd:cd01374 289 NSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 5-358 3.19e-93

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: 297.70  E-value: 3.19e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   5 DSIIVAVRVRPFNDREKTRNCKLVIEMPDEETTVIRDpkTNDEKRFTYDHSYwshdgfsekkngylePTDphyADQRRVF 84
Cdd:cd01369   2 CNIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIAT--SETGKTFSFDRVF---------------DPN---TTQEDVY 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  85 EDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNN---KGIVPIVCEELFKQIADNKKkNMQFEVFVSMMEIYCEK 161
Cdd:cd01369  62 NFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDpesMGIIPRIVQDIFETIYSMDE-NLEFHVKVSYFEIYMEK 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 162 VRDLLSstpPPKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQKSSK 241
Cdd:cd01369 141 IRDLLD---VSKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVE 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 242 QAggtSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDsqkaksGKKTQIPYRDSVLTCLLKN 321
Cdd:cd01369 218 TE---KKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD------GKKTHIPYRDSKLTRILQD 288

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 17554190 322 ALGGNSKTIMIAAISPADINFEETLSTLRFADRAKSI 358
Cdd:cd01369 289 SLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 7-366 1.53e-88

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: 286.14  E-value: 1.53e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   7 IIVAVRVRPFNDREKTRNCKLVIEMPD------EETTVIRDpkTNDEKRFTYDHSYWSHdgfsekkngyleptdphyADQ 80
Cdd:cd01364   4 IQVVVRCRPFNLRERKASSHSVVEVDPvrkevsVRTGGLAD--KSSTKTYTFDMVFGPE------------------AKQ 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  81 RRVFEDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNK-----------GIVPIVCEELFKQIADNKKknmQFE 149
Cdd:cd01364  64 IDVYRSVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDRSPNeeytweldplaGIIPRTLHQLFEKLEDNGT---EYS 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 150 VFVSMMEIYCEKVRDLLSSTPPPKGGLKVREHP--KNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRA 227
Cdd:cd01364 141 VKVSYLEIYNEELFDLLSPSSDVSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRS 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 228 HTIVKITFNQKSSKQAGGTSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDsqkaksgKKTQ 307
Cdd:cd01364 221 HSVFSITIHIKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE-------RAPH 293

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17554190 308 IPYRDSVLTCLLKNALGGNSKTIMIAAISPADINFEETLSTLRFADRAKSIKTNAVVNE 366
Cdd:cd01364 294 VPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQ 352
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 5-367 4.27e-86

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: 279.39  E-value: 4.27e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   5 DSIIVAVRVRPFNDREKTRNCKLVIEMPDEETTVIRdpkTNDEKRFTYDHSywshdgFSEKKNgyleptdphyadQRRVF 84
Cdd:cd01373   1 DAVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLH---SKPPKTFTFDHV------ADSNTN------------QESVF 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  85 EDLGRGVLANAWAGYNCSLFAYGQTGSGKSY-------SIVGFKNN-KGIVPIVCEELFKQI---ADNKKKNMQFEVFVS 153
Cdd:cd01373  60 QSVGKPIVESCLSGYNGTIFAYGQTGSGKTYtmwgpseSDNESPHGlRGVIPRIFEYLFSLIqreKEKAGEGKSFLCKCS 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 154 MMEIYCEKVRDLLSSTpppKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKI 233
Cdd:cd01373 140 FLEIYNEQIYDLLDPA---SRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTC 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 234 TFNQKSsKQAGGTSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDSQKaksGKKTQIPYRDS 313
Cdd:cd01373 217 TIESWE-KKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAH---GKQRHVCYRDS 292

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 17554190 314 VLTCLLKNALGGNSKTIMIAAISPADINFEETLSTLRFADRAKSIKTNAVVNEN 367
Cdd:cd01373 293 KLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
12-420 7.17e-78

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 264.68  E-value: 7.17e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  12 RVRPFNDREKTRNCKLVIEMPDEETTVIR--------DPKTNDEKRFTYDHSYwshdgfsekkngyleptDPHyADQRRV 83
Cdd:COG5059  12 RLSSRNEKSVSDIKSTIRIIPGELGERLIntskkshvSLEKSKEGTYAFDKVF-----------------GPS-ATQEDV 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  84 FEDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELFKQIaDNKKKNMQFEVFVSMMEIYCEKVR 163
Cdd:COG5059  74 YEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKL-EDLSMTKDFAVSISYLEIYNEKIY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 164 DLLSSTPPpkgGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQKSSKqa 243
Cdd:COG5059 153 DLLSPNEE---SLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKV-- 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 244 GGTSmKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDSQKAKSgkktqIPYRDSVLTCLLKNAL 323
Cdd:COG5059 228 SGTS-ETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSGH-----IPYRESKLTRLLQDSL 301

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 324 GGNSKTIMIAAISPADINFEETLSTLRFADRAKSIKTNAVVNENQ--------TERALRELREENLRLQSQIQGGTagda 395
Cdd:COG5059 302 GGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSdssreieeIKFDLSEDRSEIEILVFREQSQL---- 377

                       410       420
                ....*....|....*....|....*
gi 17554190 396 SNEEIEKLRRQLAENQKEMEEMEKS 420
Cdd:COG5059 378 SQSSLSGIFAYMQSLKKETETLKSR 402
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 7-356 1.94e-70

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: 236.42  E-value: 1.94e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   7 IIVAVRVRPFNDREKTRNCKLVIEMPDEETTVIRDPKTN-DEKRFTYDHSYwSHDG-FSEKkngyleptdphyADQRRVF 84
Cdd:cd01367   2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKvDLTKYIENHTF-RFDYvFDES------------SSNETVY 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  85 EDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKN----NKGIVPIVCEELFKQIADNKKKNmQFEVFVSMMEIYCE 160
Cdd:cd01367  69 RSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDFSgqeeSKGIYALAARDVFRLLNKLPYKD-NLGVTVSFFEIYGG 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 161 KVRDLLSSTPPpkggLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQKSS 240
Cdd:cd01367 148 KVFDLLNRKKR----VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGT 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 241 KQAGGtsmkksEINLVDLAGSER---QSAAGTEgdRLKEGIVINQSLTTLGRVIKALHDsqkaksgKKTQIPYRDSVLTC 317
Cdd:cd01367 224 NKLHG------KLSFVDLAGSERgadTSSADRQ--TRMEGAEINKSLLALKECIRALGQ-------NKAHIPFRGSKLTQ 288

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 17554190 318 LLKNAL-GGNSKTIMIAAISPADINFEETLSTLRFADRAK 356
Cdd:cd01367 289 VLKDSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 9-407 1.57e-68

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 249.47  E-value: 1.57e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190     9 VAVRVRPFNDrektrncklviempDEETTVIRDPKTND-----EKRFTYDhsywshdgfsekkngylEPTDPHyADQRRV 83
Cdd:PLN03188  102 VIVRMKPLNK--------------GEEGEMIVQKMSNDsltinGQTFTFD-----------------SIADPE-STQEDI 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190    84 FEDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKN----------NKGIVPIVCEELFKQIADNKKKN----MQFE 149
Cdd:PLN03188  150 FQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPANglleehlsgdQQGLTPRVFERLFARINEEQIKHadrqLKYQ 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   150 VFVSMMEIYCEKVRDLLSstpPPKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHT 229
Cdd:PLN03188  230 CRCSFLEIYNEQITDLLD---PSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHS 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   230 IVKITFNQKSSKQAGG-TSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALhdSQKAKSGKKTQI 308
Cdd:PLN03188  307 VFTCVVESRCKSVADGlSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINIL--AEISQTGKQRHI 384

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   309 PYRDSVLTCLLKNALGGNSKTIMIAAISPADINFEETLSTLRFADRAKSIKTNAVVNE------NQTERALRELREENLR 382
Cdd:PLN03188  385 PYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqddvNFLREVIRQLRDELQR 464

                         410       420
                  ....*....|....*....|....*
gi 17554190   383 LQSQIQGGTAGDASNEEIEKLRRQL 407
Cdd:PLN03188  465 VKANGNNPTNPNVAYSTAWNARRSL 489
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 6-356 7.45e-66

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: 224.38  E-value: 7.45e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   6 SIIVAVRVRPfNDREKTRNCKLvieMPDEETTVIRDPKtnDEKRFTYDHSywsHDGFSEKKNGYLeptdpHYADQRRVFE 85
Cdd:cd01375   1 KVQAFVRVRP-TDDFAHEMIKY---GEDGKSISIHLKK--DLRRGVVNNQ---QEDWSFKFDGVL-----HNASQELVYE 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  86 DLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNN---KGIVPIVCEELFKQIadNKKKNMQFEVFVSMMEIYCEKV 162
Cdd:cd01375  67 TVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMI--EERPTKAYTVHVSYLEIYNEQL 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 163 RDLLSSTP---PPKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQKS 239
Cdd:cd01375 145 YDLLSTLPyvgPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHS 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 240 SkQAGGTSMKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDSqkaksgKKTQIPYRDSVLTCLL 319
Cdd:cd01375 225 R-TLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDK------DRTHVPFRQSKLTHVL 297

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 17554190 320 KNALGGNSKTIMIAAISPADINFEETLSTLRFADRAK 356
Cdd:cd01375 298 RDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 9-356 2.06e-62

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: 214.29  E-value: 2.06e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   9 VAVRVRPFNDREKTRNCKLVIEMPDEETTVIRDPKTNDE-KRFTYDHSYWSHDgfsekkngyleptdphyaDQRRVFEDL 87
Cdd:cd01376   4 VAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPRNHGEtLKYQFDAFYGEES------------------TQEDIYARE 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  88 GRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELfkqIADNKKKNMQFEVFVSMMEIYCEKVRDLLS 167
Cdd:cd01376  66 VQPIVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDL---LQMTRKEAWALSFTMSYLEIYQEKILDLLE 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 168 stpPPKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKItfNQKSSKQAGGTS 247
Cdd:cd01376 143 ---PASKELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLI--KVDQRERLAPFR 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 248 MKKSEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDSQKaksgkktQIPYRDSVLTCLLKNALGGNS 327
Cdd:cd01376 218 QRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLP-------RIPYRDSKLTRLLQDSLGGGS 290

                       330       340
                ....*....|....*....|....*....
gi 17554190 328 KTIMIAAISPADINFEETLSTLRFADRAK 356
Cdd:cd01376 291 RCIMVANIAPERTFYQDTLSTLNFAARSR 319
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 5-356 6.10e-62

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: 213.79  E-value: 6.10e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   5 DSIIVAVRVRPFNDREKTRNCKLVIEMPDEETTVIRDPKTndekrfTYDHSYWSHDGFSEKKNGYLEPTDPHYAdQRRVF 84
Cdd:cd01368   1 DPVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKG------SAANKSERNGGQKETKFSFSKVFGPNTT-QKEFF 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  85 EDLGRGVLANAWAGYNCSLFAYGQTGSGKSYSIVGFKNNKGIVPIVCEELFKQIADnkkknmqFEVFVSMMEIYCEKVRD 164
Cdd:cd01368  74 QGTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG-------YSVFVSYIEIYNEYIYD 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 165 LL----SSTPPPKGGLKVREHPKNGFYVENLTTVPVNSFKEIEAKIEEGTKSRTIAATQMNATSSRAHTIVKITFNQKSS 240
Cdd:cd01368 147 LLepspSSPTKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPG 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 241 KQAGGTSMKK-----SEINLVDLAGSERQSAAGTEGDRLKEGIVINQSLTTLGRVIKALHDSQKAKSGKKtqIPYRDSVL 315
Cdd:cd01368 227 DSDGDVDQDKdqitvSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKM--VPFRDSKL 304

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 17554190 316 TCLLKNALGGNSKTIMIAAISPADINFEETLSTLRFADRAK 356
Cdd:cd01368 305 THLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
 450-552 2.10e-46

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 161.23  E-value: 2.10e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 450 CHLWNLNEDPALTNVIVHFIPVGESVVGNKPTSSGNFIQMSGLSILPQHVTLKNDgNNQIHLSPCSEDLDIFINGKPVHG 529
Cdd:cd22709   1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVITNT-DGKVTIEPVSPGAKVIVNGVPVTG 79

                        90       100
                ....*....|....*....|...
gi 17554190 530 ETQLQQNDRVFFGGNHLYVFNNP 552
Cdd:cd22709  80 ETELHHLDRVILGSNHLYVFVGP 102
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
 448-552 5.10e-20

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 86.17  E-value: 5.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 448 KMCHLWNLNEDPALTNVIVHFIPVGESVVGNKPTSSGNFIQMSGLSILPQHVTLKNDgNNQIHLSPcSEDLDIFINGKPV 527
Cdd:cd22707   6 KLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENN-GGKVTIIP-VGDAETYVNGELI 83

                        90       100
                ....*....|....*....|....*
gi 17554190 528 HGETQLQQNDRVFFGGNHLYVFNNP 552
Cdd:cd22707  84 SEPTVLHHGDRVILGGDHYFRFNHP 108
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
 451-551 6.61e-20

forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438757 [Multi-domain]  Cd Length: 101  Bit Score: 85.36  E-value: 6.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 451 HLWNLNEDPALTNVIVHFIPVGESVVGNKPTSSGNFIQMSGLSILPQHVTLKNDgNNQIHLSPCsEDLDIFINGKPVHGE 530
Cdd:cd22705   3 HLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENE-DGVVTLEPC-EGALTYVNGKRVTEP 80

                        90       100
                ....*....|....*....|.
gi 17554190 531 TQLQQNDRVFFGGNHLYVFNN 551
Cdd:cd22705  81 TRLKTGSRVILGKNHVFRFNH 101
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
 450-552 2.98e-19

forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438758 [Multi-domain]  Cd Length: 101  Bit Score: 83.50  E-value: 2.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 450 CHLWNLNEDPALTNVIVHFIPvGESVVGNKPTSSGNFIQMSGLSILPQH--VTLKNDgnnQIHLSPCsEDLDIFINGKPV 527
Cdd:cd22706   2 YYLVNLNADPSLNELLVYYLK-EHTLIGRSDAPTQQDIQLSGLGIQPEHciITIENE---DVYLTPL-EGARTCVNGSIV 76

                        90       100
                ....*....|....*....|....*
gi 17554190 528 HGETQLQQNDRVFFGGNHLYVFNNP 552
Cdd:cd22706  77 TEKTQLRHGDRILWGNNHFFRLNCP 101
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 9-295 6.43e-16

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: 76.23  E-value: 6.43e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   9 VAVRVRPFNDREKTRNCKLVIempdeettvirdpktndekrftydhsywshdGFSEKKNGylePTDPHyadqrrVFEDLG 88
Cdd:cd01363   1 VLVRVNPFKELPIYRDSKIIV-------------------------------FYRGFRRS---ESQPH------VFAIAD 40

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  89 RgVLANAWAGYNC-SLFAYGQTGSGKSYsivgfkNNKGIVPIVCEELFKQIADNKKKNMQFevfvsmmeiycekvrdlls 167
Cdd:cd01363  41 P-AYQSMLDGYNNqSIFAYGESGAGKTE------TMKGVIPYLASVAFNGINKGETEGWVY------------------- 94

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 168 stpppkgglkvrehpkngfyvenLTTVPVNSFKEIEAKIEEGTKSRTiAATQMNATSSRAHTIVKItfnqksskqaggts 247
Cdd:cd01363  95 -----------------------LTEITVTLEDQILQANPILEAFGN-AKTTRNENSSRFGKFIEI-------------- 136

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 17554190 248 mkkseinLVDLAGSERqsaagtegdrlkegivINQSLTTLGRVIKALH 295
Cdd:cd01363 137 -------LLDIAGFEI----------------INESLNTLMNVLRATR 161
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
 448-554 2.85e-15

forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438779 [Multi-domain]  Cd Length: 110  Bit Score: 72.76  E-value: 2.85e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 448 KMCHLWNLNEDPALTNVIVHFIPVGESVVGNKPTSSGNFIQMSGLSILPQHVTLKNDGNNQ----IHLSPCsEDLDIFIN 523
Cdd:cd22727   1 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNNNgeviVTLEPC-ERSETYVN 79

                        90       100       110
                ....*....|....*....|....*....|.
gi 17554190 524 GKPVHGETQLQQNDRVFFGGNHLYVFNNPTK 554
Cdd:cd22727  80 GKRVVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
 450-552 2.44e-14

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 69.56  E-value: 2.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 450 CHLWNLNEDPALTNVIVHFIPvGESVVGNKPTSSgnfIQMSGLSILPQHVTLKNDGNNQIHLSPcSEDLDIFINGKPVHG 529
Cdd:cd22730   2 CFLVNLNADPALNELLVYYLK-EHTLIGSADSQD---IQLCGMGILPEHCIIDITPEGQVMLTP-QKNTRTFVNGSAVTS 76

                        90       100
                ....*....|....*....|...
gi 17554190 530 ETQLQQNDRVFFGGNHLYVFNNP 552
Cdd:cd22730  77 PIQLHHGDRILWGNNHFFRINLP 99
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
 451-552 7.66e-14

forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438778 [Multi-domain]  Cd Length: 115  Bit Score: 68.80  E-value: 7.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 451 HLWNLNEDPALTNVIVHFIPVGESVVGNKPTSSGNFIQMSGLSILPQHVTLKND----GNNQIHLSPCsEDLDIFINGKP 526
Cdd:cd22726   3 HLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDtrsgGEAVVTLEPC-EGADTYVNGKK 81

                        90       100
                ....*....|....*....|....*.
gi 17554190 527 VHGETQLQQNDRVFFGGNHLYVFNNP 552
Cdd:cd22726  82 VTEPSILRSGNRIIMGKSHVFRFNHP 107
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
 449-552 2.69e-13

forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438763 [Multi-domain]  Cd Length: 106  Bit Score: 66.96  E-value: 2.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 449 MCHLWNLNEDPALT-NVIVHFIPVGESVVGNK--PTSSGNFIQMSGLSILPQHVTLKN-DGnnQIHLSPCSEDLDIFING 524
Cdd:cd22711   1 LPYLLELSPDGSDRdKPRRHRLQPNVTEVGSErsPANSGQFIQLFGPDILPRHCVITHmEG--VVTVTPASQDAETYVNG 78

                        90       100
                ....*....|....*....|....*...
gi 17554190 525 KPVHGETQLQQNDRVFFGGNHLYVFNNP 552
Cdd:cd22711  79 QRIYETTMLQHGMVVQFGRSHTFRFCDP 106
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
 450-555 1.52e-12

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438781 [Multi-domain]  Cd Length: 109  Bit Score: 64.91  E-value: 1.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 450 CHLWNLNEDPALTNVIVHFIPvGESVVGNKPTSSgnfIQMSGLSILPQHVTLKNDGNNQIHLSPcSEDLDIFINGKPVHG 529
Cdd:cd22729   2 CYLVNLNADPALNELLVYYLK-DHTRVGADTSQD---IQLFGIGIQPEHCVIDIAADGDVTLTP-KENARTCVNGTLVCS 76

                        90       100
                ....*....|....*....|....*.
gi 17554190 530 ETQLQQNDRVFFGGNHLYVFNNPTKK 555
Cdd:cd22729  77 VTQLWHGDRILWGNNHFFRINLPKRK 102
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 3-166 2.18e-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: 62.62  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190     3 KGdSIIVAVRVRPFNDREktrnckLVIEMPDEETTVIRDPKTNdeKRFTYDHSYwshdgfsekkngyleptdPHYADQRR 82
Cdd:pfam16796  19 KG-NIRVFARVRPELLSE------AQIDYPDETSSDGKIGSKN--KSFSFDRVF------------------PPESEQED 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190    83 VFEDLGrgVLAN-AWAGYNCSLFAYGQTGSGksysivgfkNNKGIVPIVCEELFKQIAdNKKKNMQFEVFVSMMEIYCEK 161
Cdd:pfam16796  72 VFQEIS--QLVQsCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFIS-SLKKGWKYTIELQFVEIYNES 139


                  ....*
gi 17554190   162 VRDLL 166
Cdd:pfam16796 140 SQDLL 144
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
 451-551 6.10e-10

forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438780 [Multi-domain]  Cd Length: 102  Bit Score: 57.19  E-value: 6.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 451 HLWNLNEDPALTNVIVHFIPVGESVVGNKPTSsgnfIQMSGLSILPQHVTLKNDGNNQ----IHLSPCsEDLDIFINGKP 526
Cdd:cd22728   3 HLVNLNEDPLMSECLLYHIKDGVTRVGQVDVD----IKLSGQFIREQHCLFRSIPNPSgevvVTLEPC-EGAETYVNGKQ 77

                        90       100
                ....*....|....*....|....*
gi 17554190 527 VHGETQLQQNDRVFFGGNHLYVFNN 551
Cdd:cd22728  78 VTEPLVLKSGNRIVMGKNHVFRFNH 102
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
 448-552 4.08e-08

forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438760 [Multi-domain]  Cd Length: 109  Bit Score: 52.27  E-value: 4.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 448 KMCHLWNLNEDPALTNVIVHFIPVGESVVGNKPTSSGNFIQMSGLSILPQHVTLKNDgNNQIHLSPCSEDLdIFINGKPV 527
Cdd:cd22708   7 ELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENV-GGVVTLHPLPGAL-CAVNGQVI 84

                        90       100
                ....*....|....*....|....*
gi 17554190 528 HGETQLQQNDRVFFGGNHLYVFNNP 552
Cdd:cd22708  85 TQPTRLTQGDVILLGKTNMFRFNHP 109
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
 659-699 6.33e-08

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


Pssm-ID: 463574  Cd Length: 43  Bit Score: 49.52  E-value: 6.33e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 17554190   659 FMNRYYGMQEMYEAKQDGSEDWNMPKERDPFYEPPDSPVFI 699
Cdd:pfam12423   1 LENRLVDMREMYQEYKEGEYSQHFEVDRDPFYEPPENHNLI 41
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 451-549 2.16e-07

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 49.58  E-value: 2.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 451 HLWNLNEDPAltnVIVHFIPVGESVVGnkpTSSGNFIQMSGLSILPQHVTLKNDGNnQIHLSPCSEDLDIFINGKPVHGE 530
Cdd:cd00060   1 RLIVLDGDGG---GREFPLTKGVVTIG---RSPDCDIVLDDPSVSRRHARIEVDGG-GVYLEDLGSTNGTFVNGKRITPP 73

                        90
                ....*....|....*....
gi 17554190 531 TQLQQNDRVFFgGNHLYVF 549
Cdd:cd00060  74 VPLQDGDVIRL-GDTTFRF 91
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
 462-552 4.57e-07

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438765  Cd Length: 120  Bit Score: 49.63  E-value: 4.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 462 TNVIVHFIPVGESVVGnkpTSSGNFIQMSGLSILPQHVTLKNDgNNQIHLSPCSEDldIFINGKPVHGETQLQQNDRVFF 541
Cdd:cd22713  29 TAVTLLPLPEGKTTIG---TAASDIISLQGPGVEPEHCYIENI-NGTVTLYPCGNL--CSVDGLPITEPTRLTQGCMICL 102

                        90
                ....*....|.
gi 17554190 542 GGNHLYVFNNP 552
Cdd:cd22713 103 GRSNYFRFNHP 113
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
 451-552 4.40e-05

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 43.77  E-value: 4.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 451 HLWNLNEDPALTNVIVHFIPVGESVVGNKPTSSGNFIQMSGLSILPQHVTLKNDgNNQIHLSPCSeDLDIFINGKPVHGE 530
Cdd:cd22732  10 HLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIFENL-NGTVTLIPLN-GAQCSVNGVQITEA 87

                        90       100
                ....*....|....*....|..
gi 17554190 531 TQLQQNDRVFFGGNHLYVFNNP 552
Cdd:cd22732  88 TQLNQGAVILLGRTNMFRFNHP 109
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
249-423 2.36e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 249 KKSEINLVDLAG-SERQSAAGTEGDRLKegivinqSLTTLGRVIKALHDSQKAKSGKKTqipyRDSVLTCLLKN---ALG 324
Cdd:COG3206  64 QSSDVLLSGLSSlSASDSPLETQIEILK-------SRPVLERVVDKLNLDEDPLGEEAS----REAAIERLRKNltvEPV 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190 325 GNSKTIMIAAISP--------------------ADINFEETLSTLRF-ADRAKSIKTNAvvneNQTERALRELREENlrl 383
Cdd:COG3206 133 KGSNVIEISYTSPdpelaaavanalaeayleqnLELRREEARKALEFlEEQLPELRKEL----EEAEAALEEFRQKN--- 205

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17554190 384 qSQIQGGTAGDASNEEIEKLRRQLAENQKEMEEMEKSWQQ 423
Cdd:COG3206 206 -GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 487-544 2.78e-04

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 40.66  E-value: 2.78e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17554190 487 IQMSGLSilPQHVTLKNDGNNQIHLSPCSEDLDIFINGKPVHGETQLQQNDRVFFGGN 544
Cdd:cd22673  35 IQLPGVS--REHCRIEVDENGKAYLENLSTTNPTLVNGKAIEKSAELKDGDVITIGGR 90
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 475-539 4.44e-04

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 39.48  E-value: 4.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17554190   475 VVGNKPTSSgnfIQMSGLSILPQHVTLKNDGNNQIHLSPCSEDLDIFINGKPVHGE-TQLQQNDRV 539
Cdd:pfam00498   2 TIGRSPDCD---IVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTNGTFVNGQRLGPEpVRLKDGDVI 64
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
482-548 1.04e-03

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 39.17  E-value: 1.04e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17554190 482 SSGNFIQMSGLSILPQHVTLKNDGNnQIHLspcsEDLD----IFINGKPVHGETQLQQNDRVFFGGNHLYV 548
Cdd:COG1716  28 APDNDIVLDDPTVSRRHARIRRDGG-GWVL----EDLGstngTFVNGQRVTEPAPLRDGDVIRLGKTELRF 93
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 366-446 2.21e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  366 ENQTERALRELREENLRLQSQIQggtagdasneEIEKLRRQLAENQKEMEEMEK--SWQQKIAEEAA-KHASGASEKVEM 442
Cdd:PRK09510  82 KKKEQQQAEELQQKQAAEQERLK----------QLEKERLAAQEQKKQAEEAAKqaALKQKQAEEAAaKAAAAAKAKAEA 151


                 ....
gi 17554190  443 EAKK 446
Cdd:PRK09510 152 EAKR 155
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 365-447 2.41e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.33  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190  365 NENQTERALRELREENLRLQSQIQggtagdasNEEIEKLRRQLAENQKEMEEMEKSWQ---QKIAEEAAKHASGASEKVE 441
Cdd:PRK09510  93 QQKQAAEQERLKQLEKERLAAQEQ--------KKQAEEAAKQAALKQKQAEEAAAKAAaaaKAKAEAEAKRAAAAAKKAA 164


                 ....*.
gi 17554190  442 MEAKKK 447
Cdd:PRK09510 165 AEAKKK 170
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 487-527 3.44e-03

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 36.39  E-value: 3.44e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 17554190    487 IQMSGLSILPQHVTLKNDGNNQIHLSPCSEDLDIFINGKPV 527
Cdd:smart00240  12 IQLDGPSISRRHAVIVYDGGGRFYLIDLGSTNGTFVNGKRI 52
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 338-448 4.01e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.21  E-value: 4.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190    338 ADINFEETLSTLRFADRAKSIKTNAVVNENQTERALRELREENLRLQSQIQGGTAgdasneEIEKLRRQLAENQKEMEEM 417
Cdd:TIGR02169  247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEA------EIASLERSIAEKERELEDA 320

                           90       100       110
                   ....*....|....*....|....*....|.
gi 17554190    418 EKSWQQKIAEEAAKHASGASEKVEMEAKKKK 448
Cdd:TIGR02169  321 EERLAKLEAEIDKLLAEIEELEREIEEERKR 351
Kinesin_assoc pfam16183
Kinesin-associated;
394-472 6.17e-03

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 38.67  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17554190   394 DASNEEIEKLRrqlaENQKEMEEMEKSWQQKIAEEAAKH----ASGASEKVEMEA--------KKKKMCHLWNLNEDPAL 461
Cdd:pfam16183  90 PGSEEAIERLK----ETEKIIAELNETWEEKLRKTEAIRmereALLAEMGVAIREdggtlgvfSPKKTPHLVNLNEDPLM 165

                          90
                  ....*....|.
gi 17554190   462 TNVIVHFIPVG 472
Cdd:pfam16183 166 SECLLYYIKDG 176
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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