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Conserved domains on  [gi|659667948|ref|NP_001281078|]
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kinesin-like protein KIF1A isoform c [Mus musculus]

Protein Classification

Graphical summary

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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 ...
4-361 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: 677.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    4 ASVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVNPKQ-------PKETPKSFSFDYSYWSHTsPEDINYASQKQVYRD 76
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkaTREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   77 IGEEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEkdQQGIIPQLCEDLFSRINDTTNDNMSYSVEVSYMEIYCERVRD 156
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  157 LLNPK---NKGNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAE 233
Cdd:cd01365   158 LLNPKpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  234 TNITTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGPnknkKKKKTDFIPYRDSVLTW 313
Cdd:cd01365   238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGK----SKKKSSFIPYRDSVLTW 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 659667948  314 LLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIRCNAIIN 361
Cdd:cd01365   314 LLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
Kinesin_assoc pfam16183
Kinesin-associated;
358-515 8.83e-92

Kinesin-associated;


:

Pssm-ID: 435195 [Multi-domain]  Cd Length: 170  Bit Score: 294.42  E-value: 8.83e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   358 AIINEDPNNKLIRELKDEVTRLRDLLYAQGLGDITDM------------TNALVGMSPSSSLSALSSRAASVSSLHERIL 425
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLGDIIDArastpaanasaaTAAMAGASPSPSLSALSSRAASVSSLHERIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   426 FAPGSEEAIERLKETEKIIAELNETWEEKLRRTEAIRMEREALLAEMGVAMREDGGTLGVFSPKKTPHLVNLNEDPLMSE 505
Cdd:pfam16183   81 FTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSE 160
                          170
                   ....*....|
gi 659667948   506 CLLYYIKDGV 515
Cdd:pfam16183  161 CLLYYIKDGI 170
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
491-605 2.97e-82

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: 264.87  E-value: 2.97e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  491 TPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFRSDSRGGGEAVVTLEPCEGADTYVNGK 570
Cdd:cd22726     1 TPHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSGGEAVVTLEPCEGADTYVNGK 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 659667948  571 KVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 605
Cdd:cd22726    81 KVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
1148-1301 6.62e-56

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


:

Pssm-ID: 432581  Cd Length: 146  Bit Score: 190.88  E-value: 6.62e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  1148 DYIPAVVDHRGGMPcMGTFLLHQGIQRRITVTLLHETGSHIRWKEVRELVVGRIRNTPETDEALIDPN--ILSLNILSSG 1225
Cdd:pfam12473    1 EYVPVPVDQRSELD-PGTFQLHQGLQRRIVITLTHSSGDELPWERVREVRVGDVRLLDMKGRVPDSDStpDVSLKLLSKP 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 659667948  1226 YVHPAQDDRqfldsdiprTFYQFEAAWDSSMHNSLLLNRVTPYREKIYMTLSAYIEMENCTQPAVITKDFCMVFYS 1301
Cdd:pfam12473   80 VVRFNADGT---------SSYTIEAQWDSSLHNSLLLNRVTADGYRVYLTLAWDLVSEKCAEPVRFSMDTCVQIYP 146
PH_KIFIA_KIFIB cd01233
KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA ...
1579-1681 5.20e-54

KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA (Caenorhabditis elegans homolog unc-104) and KIFIB transport synaptic vesicle precursors that contain synaptic vesicle proteins, such as synaptophysin, synaptotagmin and the small GTPase RAB3A, but they do not transport organelles that contain plasma membrane proteins. They have a N-terminal motor domain, followed by a coiled-coil domain, and a C-terminal PH domain. KIF1A adopts a monomeric form in vitro, but acts as a processive dimer in vivo. KIF1B has alternatively spliced isoforms distinguished by the presence or absence of insertion sequences in the conserved amino-terminal region of the protein; this results in their different motor activities. KIF1A and KIF1B bind to RAB3 proteins through the adaptor protein mitogen-activated protein kinase (MAPK) -activating death domain (MADD; also calledDENN), which was first identified as a RAB3 guanine nucleotide exchange factor (GEF). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 269939  Cd Length: 103  Bit Score: 183.56  E-value: 5.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948 1579 RVSPIVSKKGYLHFLEPHTAGWAKRFVVVRRPYAYMYNSDKDTVERFVLNLSTAQVEYSEDQQAMLKTPNTFAVCTEHRG 1658
Cdd:cd01233     1 PKSPVVSKRGYLLFLEDATDGWVRRWVVLRRPYLHIYSSEKDGDERGVINLSTARVEYSPDQEALLGRPNVFAVYTPTNS 80
                          90       100
                  ....*....|....*....|...
gi 659667948 1659 ILLQANSDKDMHDWLYAFNPLLA 1681
Cdd:cd01233    81 YLLQARSEKEMQDWLYAIDPLLA 103
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
805-852 1.35e-14

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: 432544  Cd Length: 43  Bit Score: 69.17  E-value: 1.35e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 659667948   805 LRQRLDLMREMYDRAAEVPSSVVEDCDNvvtggDPFYDRFPWFRLVGR 852
Cdd:pfam12423    1 LRNRLIDMREMYQEYKEGEYSQHFEVEK-----DPFYEPPENHSLIGV 43
ERM super family cl38012
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
624-678 6.83e-03

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


The actual alignment was detected with superfamily member pfam00769:

Pssm-ID: 425860 [Multi-domain]  Cd Length: 247  Bit Score: 40.31  E-value: 6.83e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 659667948   624 RELLEKQgidmKQEMEQRLQELEDQYRR------EREEATYLLEQQRLDYESKLEALQKQM 678
Cdd:pfam00769    1 REEAERE----KQELEERLKQYEEETRKaqeeleESEETAELLEEKLRVAEEEAELLEQKA 57
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
4-361 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: 677.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    4 ASVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVNPKQ-------PKETPKSFSFDYSYWSHTsPEDINYASQKQVYRD 76
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkaTREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   77 IGEEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEkdQQGIIPQLCEDLFSRINDTTNDNMSYSVEVSYMEIYCERVRD 156
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  157 LLNPK---NKGNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAE 233
Cdd:cd01365   158 LLNPKpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  234 TNITTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGPnknkKKKKTDFIPYRDSVLTW 313
Cdd:cd01365   238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGK----SKKKSSFIPYRDSVLTW 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 659667948  314 LLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIRCNAIIN 361
Cdd:cd01365   314 LLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
5-361 4.25e-153

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: 471.29  E-value: 4.25e-153
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948      5 SVKVAVRVRPFNSREMSRDSKCIIQMSG--STTTIVNPKQPKETPKSFSFDYSYwshtsPEDinyASQKQVYRDIGEEML 82
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDkvGKTLTVRSPKNRQGEKKFTFDKVF-----DAT---ASQEDVFEETAAPLV 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948     83 QHAFEGYNVCIFAYGQTGAGKSYTMMGkqEKDQQGIIPQLCEDLFSRInDTTNDNMSYSVEVSYMEIYCERVRDLLNPkN 162
Cdd:smart00129   73 DSVLEGYNATIFAYGQTGSGKTYTMIG--TPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP-S 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    163 KGNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITteKVS 242
Cdd:smart00129  149 SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSG--KAS 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    243 KISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGPnknkkkkktdFIPYRDSVLTWLLRENLGGN 322
Cdd:smart00129  227 KLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSR----------HIPYRDSKLTRLLQDSLGGN 296
                           330       340       350
                    ....*....|....*....|....*....|....*....
gi 659667948    323 SRTAMVAALSPADINYDETLSTLRYADRAKQIRCNAIIN 361
Cdd:smart00129  297 SKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-354 1.85e-152

Kinesin motor domain;


Pssm-ID: 425537 [Multi-domain]  Cd Length: 326  Bit Score: 469.36  E-value: 1.85e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    11 RVRPFNSREMSRDSKCIIQMS--GSTTTIVNPKQPKETPKSFSFDYSYWSHtspedinyASQKQVYRDIGEEMLQHAFEG 88
Cdd:pfam00225    1 RVRPLNEREKSRGSSDIVSVEsvDSETVESSHLTNKNKTKTFTFDKVFDPE--------ATQEDVYEETAKPLVESVLEG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    89 YNVCIFAYGQTGAGKSYTMMGKQEkdQQGIIPQLCEDLFSRINDTTnDNMSYSVEVSYMEIYCERVRDLLNP--KNKGNL 166
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDE--DPGIIPRALEDLFDRIQKTK-ERDEFSVKVSYLEIYNEKIRDLLSPspKNKRPL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   167 RVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITTeKVSKISL 246
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAVFTITIEQRNRDTGGEESV-KTGKLNL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   247 VDLAGSERADSTG-AKGTRLKEGANINKSLTTLGKVISALAEMDSgpnknkkkkktDFIPYRDSVLTWLLRENLGGNSRT 325
Cdd:pfam00225  229 VDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS-----------KHIPYRDSKLTRLLQDSLGGNSKT 297
                          330       340
                   ....*....|....*....|....*....
gi 659667948   326 AMVAALSPADINYDETLSTLRYADRAKQI 354
Cdd:pfam00225  298 LMIANISPSSSNYEETLSTLRFASRAKNI 326
Kinesin_assoc pfam16183
Kinesin-associated;
358-515 8.83e-92

Kinesin-associated;


Pssm-ID: 435195 [Multi-domain]  Cd Length: 170  Bit Score: 294.42  E-value: 8.83e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   358 AIINEDPNNKLIRELKDEVTRLRDLLYAQGLGDITDM------------TNALVGMSPSSSLSALSSRAASVSSLHERIL 425
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLGDIIDArastpaanasaaTAAMAGASPSPSLSALSSRAASVSSLHERIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   426 FAPGSEEAIERLKETEKIIAELNETWEEKLRRTEAIRMEREALLAEMGVAMREDGGTLGVFSPKKTPHLVNLNEDPLMSE 505
Cdd:pfam16183   81 FTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSE 160
                          170
                   ....*....|
gi 659667948   506 CLLYYIKDGV 515
Cdd:pfam16183  161 CLLYYIKDGI 170
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
491-605 2.97e-82

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: 264.87  E-value: 2.97e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  491 TPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFRSDSRGGGEAVVTLEPCEGADTYVNGK 570
Cdd:cd22726     1 TPHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSGGEAVVTLEPCEGADTYVNGK 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 659667948  571 KVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 605
Cdd:cd22726    81 KVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
5-381 9.76e-81

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 278.16  E-value: 9.76e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    5 SVKVAVRVRPfnsREMSRDskcIIQMSGSTTTIVNpkqpKETPKSFSFDYSYWSHtspedinyASQKQVYRDIGEEMLQH 84
Cdd:COG5059    23 DIKSTIRIIP---GELGER---LINTSKKSHVSLE----KSKEGTYAFDKVFGPS--------ATQEDVYEETIKPLIDS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   85 AFEGYNVCIFAYGQTGAGKSYTMMGkqEKDQQGIIPQLCEDLFSRInDTTNDNMSYSVEVSYMEIYCERVRDLLNPKNKG 164
Cdd:COG5059    85 LLLGYNCTVFAYGQTGSGKTYTMSG--TEEEPGIIPLSLKELFSKL-EDLSMTKDFAVSISYLEIYNEKIYDLLSPNEES 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  165 nLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITtekvSKI 244
Cdd:COG5059   162 -LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET----SKL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  245 SLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALaeMDSGPNKNkkkkktdfIPYRDSVLTWLLRENLGGNSR 324
Cdd:COG5059   237 SLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINAL--GDKKKSGH--------IPYRESKLTRLLQDSLGGNCN 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 659667948  325 TAMVAALSPADINYDETLSTLRYADRAKQIRcNAIINEDPNNKLIR--ELKDEVTRLRD 381
Cdd:COG5059   307 TRVICTISPSSNSFEETINTLKFASRAKSIK-NKIQVNSSSDSSREieEIKFDLSEDRS 364
PLN03188 PLN03188
kinesin-12 family protein; Provisional
1-381 2.15e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 273.73  E-value: 2.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    1 MAGASVKVAVRVRPFNSREmsrDSKCIIQ-MSGSTTTIvnpkqpkeTPKSFSFDysywSHTSPEdinyASQKQVYRDIGE 79
Cdd:PLN03188   95 VSDSGVKVIVRMKPLNKGE---EGEMIVQkMSNDSLTI--------NGQTFTFD----SIADPE----STQEDIFQLVGA 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   80 EMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQ--------EKDQQGIIPQLCEDLFSRINDT----TNDNMSYSVEVSYM 147
Cdd:PLN03188  156 PLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlSGDQQGLTPRVFERLFARINEEqikhADRQLKYQCRCSFL 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  148 EIYCERVRDLLNPKNKgNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQ 227
Cdd:PLN03188  236 EIYNEQITDLLDPSQK-NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVES 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  228 KRHDAETNITTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSgpnknkkKKKTDFIPYR 307
Cdd:PLN03188  315 RCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQ-------TGKQRHIPYR 387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  308 DSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIRCNAIINE---DPNNKL---IRELKDEVTRLRD 381
Cdd:PLN03188  388 DSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqDDVNFLrevIRQLRDELQRVKA 467
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
1148-1301 6.62e-56

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 432581  Cd Length: 146  Bit Score: 190.88  E-value: 6.62e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  1148 DYIPAVVDHRGGMPcMGTFLLHQGIQRRITVTLLHETGSHIRWKEVRELVVGRIRNTPETDEALIDPN--ILSLNILSSG 1225
Cdd:pfam12473    1 EYVPVPVDQRSELD-PGTFQLHQGLQRRIVITLTHSSGDELPWERVREVRVGDVRLLDMKGRVPDSDStpDVSLKLLSKP 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 659667948  1226 YVHPAQDDRqfldsdiprTFYQFEAAWDSSMHNSLLLNRVTPYREKIYMTLSAYIEMENCTQPAVITKDFCMVFYS 1301
Cdd:pfam12473   80 VVRFNADGT---------SSYTIEAQWDSSLHNSLLLNRVTADGYRVYLTLAWDLVSEKCAEPVRFSMDTCVQIYP 146
PH_KIFIA_KIFIB cd01233
KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA ...
1579-1681 5.20e-54

KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA (Caenorhabditis elegans homolog unc-104) and KIFIB transport synaptic vesicle precursors that contain synaptic vesicle proteins, such as synaptophysin, synaptotagmin and the small GTPase RAB3A, but they do not transport organelles that contain plasma membrane proteins. They have a N-terminal motor domain, followed by a coiled-coil domain, and a C-terminal PH domain. KIF1A adopts a monomeric form in vitro, but acts as a processive dimer in vivo. KIF1B has alternatively spliced isoforms distinguished by the presence or absence of insertion sequences in the conserved amino-terminal region of the protein; this results in their different motor activities. KIF1A and KIF1B bind to RAB3 proteins through the adaptor protein mitogen-activated protein kinase (MAPK) -activating death domain (MADD; also calledDENN), which was first identified as a RAB3 guanine nucleotide exchange factor (GEF). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269939  Cd Length: 103  Bit Score: 183.56  E-value: 5.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948 1579 RVSPIVSKKGYLHFLEPHTAGWAKRFVVVRRPYAYMYNSDKDTVERFVLNLSTAQVEYSEDQQAMLKTPNTFAVCTEHRG 1658
Cdd:cd01233     1 PKSPVVSKRGYLLFLEDATDGWVRRWVVLRRPYLHIYSSEKDGDERGVINLSTARVEYSPDQEALLGRPNVFAVYTPTNS 80
                          90       100
                  ....*....|....*....|...
gi 659667948 1659 ILLQANSDKDMHDWLYAFNPLLA 1681
Cdd:cd01233    81 YLLQARSEKEMQDWLYAIDPLLA 103
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
805-852 1.35e-14

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: 432544  Cd Length: 43  Bit Score: 69.17  E-value: 1.35e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 659667948   805 LRQRLDLMREMYDRAAEVPSSVVEDCDNvvtggDPFYDRFPWFRLVGR 852
Cdd:pfam12423    1 LRNRLIDMREMYQEYKEGEYSQHFEVEK-----DPFYEPPENHSLIGV 43
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1584-1677 5.40e-12

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574  Cd Length: 102  Bit Score: 63.72  E-value: 5.40e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   1584 VSKKGYLHFLEP-HTAGWAKRFVVVRRPYAYMYNSDK---DTVERFVLNLSTAQVEYSEDQQAMlKTPNTFAVCTEHRG- 1658
Cdd:smart00233    1 VIKEGWLYKKSGgGKKSWKKRYFVLFNSTLLYYKSKKdkkSYKPKGSIDLSGCTVREAPDPDSS-KKPHCFEIKTSDRKt 79
                            90
                    ....*....|....*....
gi 659667948   1659 ILLQANSDKDMHDWLYAFN 1677
Cdd:smart00233   80 LLLQAESEEEREKWVEALR 98
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1584-1677 5.71e-11

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 395117 [Multi-domain]  Cd Length: 105  Bit Score: 61.04  E-value: 5.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  1584 VSKKGYLHFLEPHTA-GWAKRFVVVRRPYAYMYNSD---KDTVERFVLNLSTAQVEYSEDQqAMLKTPNTFAVCT----E 1655
Cdd:pfam00169    1 VVKEGWLLKKGGGKKkSWKKRYFVLFDGSLLYYKDDkskKSKEPKGSISLSGCEVVEVVAS-DSPKRKFCFELRTgertG 79
                           90       100
                   ....*....|....*....|..
gi 659667948  1656 HRGILLQANSDKDMHDWLYAFN 1677
Cdd:pfam00169   80 KRTYLLQAESEEERKDWIKAIQ 101
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
516-584 1.99e-07

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


Pssm-ID: 425720 [Multi-domain]  Cd Length: 66  Bit Score: 49.50  E-value: 1.99e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 659667948   516 TRVGREDaerRQDIVLSGHFIKEEHCIFRSDsrggGEAVVTLEPC-EGADTYVNGKKVT-EPSILRSGNRI 584
Cdd:pfam00498    1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYD----GGGRFYLEDLgSTNGTFVNGQRLGpEPVRLKDGDVI 64
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
516-572 4.02e-06

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 45.25  E-value: 4.02e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 659667948    516 TRVGRedAERRQDIVLSGHFIKEEHCIFRSDsrggGEAVVTLEPC-EGADTYVNGKKV 572
Cdd:smart00240    1 VTIGR--SSEDCDIQLDGPSISRRHAVIVYD----GGGRFYLIDLgSTNGTFVNGKRI 52
ERM pfam00769
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
624-678 6.83e-03

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


Pssm-ID: 425860 [Multi-domain]  Cd Length: 247  Bit Score: 40.31  E-value: 6.83e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 659667948   624 RELLEKQgidmKQEMEQRLQELEDQYRR------EREEATYLLEQQRLDYESKLEALQKQM 678
Cdd:pfam00769    1 REEAERE----KQELEERLKQYEEETRKaqeeleESEETAELLEEKLRVAEEEAELLEQKA 57
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
4-361 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: 677.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    4 ASVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVNPKQ-------PKETPKSFSFDYSYWSHTsPEDINYASQKQVYRD 76
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkaTREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   77 IGEEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEkdQQGIIPQLCEDLFSRINDTTNDNMSYSVEVSYMEIYCERVRD 156
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  157 LLNPK---NKGNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAE 233
Cdd:cd01365   158 LLNPKpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  234 TNITTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGPnknkKKKKTDFIPYRDSVLTW 313
Cdd:cd01365   238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGK----SKKKSSFIPYRDSVLTW 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 659667948  314 LLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIRCNAIIN 361
Cdd:cd01365   314 LLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
5-352 1.16e-154

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: 475.21  E-value: 1.16e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    5 SVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVNPKQPKETPKSFSFDYSYWSHtspedinyASQKQVYRDIGEEMLQH 84
Cdd:cd00106     1 NVRVAVRVRPLNGREARSAKSVISVDGGKSVVLDPPKNRVAPPKTFAFDAVFDST--------STQEEVYEGTAKPLVDS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   85 AFEGYNVCIFAYGQTGAGKSYTMMGKQEkDQQGIIPQLCEDLFSRINDTTNDNMSYSVEVSYMEIYCERVRDLLNPKNKG 164
Cdd:cd00106    73 ALEGYNGTIFAYGQTGSGKTYTMLGPDP-EQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLLSPVPKK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  165 NLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITTekVSKI 244
Cdd:cd00106   152 PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVT--SSKL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  245 SLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDsgpnknkkkkkTDFIPYRDSVLTWLLRENLGGNSR 324
Cdd:cd00106   230 NLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQ-----------NKHIPYRDSKLTRLLQDSLGGNSK 298
                         330       340
                  ....*....|....*....|....*...
gi 659667948  325 TAMVAALSPADINYDETLSTLRYADRAK 352
Cdd:cd00106   299 TIMIACISPSSENFEETLSTLRFASRAK 326
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
5-361 4.25e-153

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: 471.29  E-value: 4.25e-153
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948      5 SVKVAVRVRPFNSREMSRDSKCIIQMSG--STTTIVNPKQPKETPKSFSFDYSYwshtsPEDinyASQKQVYRDIGEEML 82
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDkvGKTLTVRSPKNRQGEKKFTFDKVF-----DAT---ASQEDVFEETAAPLV 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948     83 QHAFEGYNVCIFAYGQTGAGKSYTMMGkqEKDQQGIIPQLCEDLFSRInDTTNDNMSYSVEVSYMEIYCERVRDLLNPkN 162
Cdd:smart00129   73 DSVLEGYNATIFAYGQTGSGKTYTMIG--TPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP-S 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    163 KGNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITteKVS 242
Cdd:smart00129  149 SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSG--KAS 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    243 KISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGPnknkkkkktdFIPYRDSVLTWLLRENLGGN 322
Cdd:smart00129  227 KLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSR----------HIPYRDSKLTRLLQDSLGGN 296
                           330       340       350
                    ....*....|....*....|....*....|....*....
gi 659667948    323 SRTAMVAALSPADINYDETLSTLRYADRAKQIRCNAIIN 361
Cdd:smart00129  297 SKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-354 1.85e-152

Kinesin motor domain;


Pssm-ID: 425537 [Multi-domain]  Cd Length: 326  Bit Score: 469.36  E-value: 1.85e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    11 RVRPFNSREMSRDSKCIIQMS--GSTTTIVNPKQPKETPKSFSFDYSYWSHtspedinyASQKQVYRDIGEEMLQHAFEG 88
Cdd:pfam00225    1 RVRPLNEREKSRGSSDIVSVEsvDSETVESSHLTNKNKTKTFTFDKVFDPE--------ATQEDVYEETAKPLVESVLEG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    89 YNVCIFAYGQTGAGKSYTMMGKQEkdQQGIIPQLCEDLFSRINDTTnDNMSYSVEVSYMEIYCERVRDLLNP--KNKGNL 166
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDE--DPGIIPRALEDLFDRIQKTK-ERDEFSVKVSYLEIYNEKIRDLLSPspKNKRPL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   167 RVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITTeKVSKISL 246
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAVFTITIEQRNRDTGGEESV-KTGKLNL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   247 VDLAGSERADSTG-AKGTRLKEGANINKSLTTLGKVISALAEMDSgpnknkkkkktDFIPYRDSVLTWLLRENLGGNSRT 325
Cdd:pfam00225  229 VDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS-----------KHIPYRDSKLTRLLQDSLGGNSKT 297
                          330       340
                   ....*....|....*....|....*....
gi 659667948   326 AMVAALSPADINYDETLSTLRYADRAKQI 354
Cdd:pfam00225  298 LMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
5-354 6.59e-114

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: 364.09  E-value: 6.59e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    5 SVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIV--NPKQ-PKETPKSFSFDYSYwshtSPEdinyASQKQVYRDIGEEM 81
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSvrNPKAtANEPPKTFTFDAVF----DPN----SKQLDVYDETARPL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   82 LQHAFEGYNVCIFAYGQTGAGKSYTMMGKQE-KDQQGIIPQLCEDLFSRINdTTNDNMSYSVEVSYMEIYCERVRDLLNP 160
Cdd:cd01371    74 VDSVLEGYNGTIFAYGQTGTGKTYTMEGKREdPELRGIIPNSFAHIFGHIA-RSQNNQQFLVRVSYLEIYNEEIRDLLGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  161 KNKGNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIF--TQKRHDAETNITt 238
Cdd:cd01371   153 DQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIecSEKGEDGENHIR- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  239 ekVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGpnknkkkkktdFIPYRDSVLTWLLREN 318
Cdd:cd01371   232 --VGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKST-----------HIPYRDSKLTRLLQDS 298
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 659667948  319 LGGNSRTAMVAALSPADINYDETLSTLRYADRAKQI 354
Cdd:cd01371   299 LGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
5-354 2.03e-109

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: 351.25  E-value: 2.03e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    5 SVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVnpkQPKETPKSFSFDYSYwshtsPEDinyASQKQVYRDIGEEMLQH 84
Cdd:cd01369     3 NIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVI---ATSETGKTFSFDRVF-----DPN---TTQEDVYNFAAKPIVDD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   85 AFEGYNVCIFAYGQTGAGKSYTMMGKQEKDQ-QGIIPQLCEDLFSRINDTTnDNMSYSVEVSYMEIYCERVRDLLNPKNK 163
Cdd:cd01369    72 VLNGYNGTIFAYGQTSSGKTYTMEGKLGDPEsMGIIPRIVQDIFETIYSMD-ENLEFHVKVSYFEIYMEKIRDLLDVSKT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  164 gNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKrhDAETNITteKVSK 243
Cdd:cd01369   151 -NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE--NVETEKK--KSGK 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  244 ISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSgpnknkkkkktDFIPYRDSVLTWLLRENLGGNS 323
Cdd:cd01369   226 LYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK-----------THIPYRDSKLTRILQDSLGGNS 294
                         330       340       350
                  ....*....|....*....|....*....|.
gi 659667948  324 RTAMVAALSPADINYDETLSTLRYADRAKQI 354
Cdd:cd01369   295 RTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
5-355 3.21e-104

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: 337.00  E-value: 3.21e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    5 SVKVAVRVRPFNSREMSRDSK-CIIQMSGSTTTIVNPKqpketpKSFSFDYSYwshtSPEDinyaSQKQVYRDIGEEMLQ 83
Cdd:cd01372     2 SVRVAVRVRPLLPKEIIEGCRiCVSFVPGEPQVTVGTD------KSFTFDYVF----DPST----EQEEVYNTCVAPLVD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   84 HAFEGYNVCIFAYGQTGAGKSYTMMG----KQEKDQQGIIPQLCEDLFSRInDTTNDNMSYSVEVSYMEIYCERVRDLLN 159
Cdd:cd01372    68 GLFEGYNATVLAYGQTGSGKTYTMGTaytaEEDEEQVGIIPRAIQHIFKKI-EKKKDTFEFQLKVSFLEIYNEEIRDLLD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  160 PKN--KGNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHD--AETN 235
Cdd:cd01372   147 PETdkKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNgpIAPM 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  236 ITTEK----VSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGPNknkkkkktdFIPYRDSVL 311
Cdd:cd01372   227 SADDKnstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGA---------HVPYRDSKL 297
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 659667948  312 TWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIR 355
Cdd:cd01372   298 TRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
5-354 2.83e-103

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: 333.53  E-value: 2.83e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    5 SVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVNPKqpketPKSFSFDYSYWSHTSpediNYasqkQVYRDIGEEMLQH 84
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIYLVEPP-----STSFTFDHVFGGDST----NR----EVYELIAKPVVKS 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   85 AFEGYNVCIFAYGQTGAGKSYTMMGKQEKDqqGIIPQLCEDLFSRINDTTNDNmsYSVEVSYMEIYCERVRDLLNPKNKg 164
Cdd:cd01374    68 ALEGYNGTIFAYGQTSSGKTFTMSGDEDEP--GIIPLAIRDIFSKIQDTPDRE--FLLRVSYLEIYNEKINDLLSPTSQ- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  165 NLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNiTTEKVSKI 244
Cdd:cd01374   143 NLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEE-GTVRVSTL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  245 SLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEmdsgpnknkkKKKTDFIPYRDSVLTWLLRENLGGNSR 324
Cdd:cd01374   222 NLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQPSLGGNSR 291
                         330       340       350
                  ....*....|....*....|....*....|
gi 659667948  325 TAMVAALSPADINYDETLSTLRYADRAKQI 354
Cdd:cd01374   292 TAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
5-354 6.06e-102

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: 330.85  E-value: 6.06e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    5 SVKVAVRVRPFNSREMSR-DSKCIIQMSG----------------STTTIVNPKQPKETPKSFSFDYSYwshtspeDINy 67
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEgFRRIVKVMDNhmlvfdpkdeedgffhGGSNNRDRRKRRNKELKYVFDRVF-------DET- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   68 ASQKQVYRDIGEEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKqeKDQQGIIPQLCEDLFSRInDTTNDNMSYSVEVSYM 147
Cdd:cd01370    73 STQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGT--PQEPGLMVLTMKELFKRI-ESLKDEKEFEVSMSYL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  148 EIYCERVRDLLNPKNKGnLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQ 227
Cdd:cd01370   150 EIYNETIRDLLNPSSGP-LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQ 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  228 KRHDAETNITTeKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGPNknkkkkktdFIPYR 307
Cdd:cd01370   229 QDKTASINQQV-RQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNK---------HIPYR 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 659667948  308 DSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQI 354
Cdd:cd01370   299 DSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
11-356 4.38e-100

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: 324.93  E-value: 4.38e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   11 RVRPFNSREMSRDSKCI-IQMSGSTTTIVNPKQPKEtpKSFSFDYSYwshtSPEdinyASQKQVYRDIgEEMLQHAFEGY 89
Cdd:cd01366     9 RVRPLLPSEENEDTSHItFPDEDGQTIELTSIGAKQ--KEFSFDKVF----DPE----ASQEDVFEEV-SPLVQSALDGY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   90 NVCIFAYGQTGAGKSYTMMGKqeKDQQGIIPQLCEDLFSRINDTTNDNMSYSVEVSYMEIYCERVRDLLNPKNKGNLR-- 167
Cdd:cd01366    78 NVCIFAYGQTGSGKTYTMEGP--PESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLLAPGNAPQKKle 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  168 VREHPLLGP-YVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQkrhdaeTNITTEK--VSKI 244
Cdd:cd01366   156 IRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISG------RNLQTGEisVGKL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  245 SLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSgpnknkkkkktdFIPYRDSVLTWLLRENLGGNSR 324
Cdd:cd01366   230 NLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQS------------HIPYRNSKLTYLLQDSLGGNSK 297
                         330       340       350
                  ....*....|....*....|....*....|..
gi 659667948  325 TAMVAALSPADINYDETLSTLRYADRAKQIRC 356
Cdd:cd01366   298 TLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
6-363 1.91e-95

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: 312.52  E-value: 1.91e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    6 VKVAVRVRPFNSREMSRD-SKCIIQMSgsTTTIVNPKQPketPKSFSFDysywsHTSPEDINyasQKQVYRDIGEEMLQH 84
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEyGQCLKKLS--SDTLVLHSKP---PKTFTFD-----HVADSNTN---QESVFQSVGKPIVES 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   85 AFEGYNVCIFAYGQTGAGKSYTMMGKQEKDQ------QGIIPQLCEDLFSRIN---DTTNDNMSYSVEVSYMEIYCERVR 155
Cdd:cd01373    70 CLSGYNGTIFAYGQTGSGKTYTMWGPSESDNesphglRGVIPRIFEYLFSLIQrekEKAGEGKSFLCKCSFLEIYNEQIY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  156 DLLNPKNKgNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAEtn 235
Cdd:cd01373   150 DLLDPASR-NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKAC-- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  236 ITTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGpnknkkkkKTDFIPYRDSVLTWLL 315
Cdd:cd01373   227 FVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHG--------KQRHVCYRDSKLTFLL 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 659667948  316 RENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIRCNAIINED 363
Cdd:cd01373   299 RDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
3-363 1.03e-92

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: 304.63  E-value: 1.03e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    3 GASVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIV---NPKQPKETPKSFSFDYSYwshtSPEdinyASQKQVYRDIGE 79
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSvrtGGLADKSSTKTYTFDMVF----GPE----AKQIDVYRSVVC 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   80 EMLQHAFEGYNVCIFAYGQTGAGKSYTMMGK---------QEKDQQGIIPQLCEDLFSRINDTTNDnmsYSVEVSYMEIY 150
Cdd:cd01364    73 PILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwELDPLAGIIPRTLHQLFEKLEDNGTE---YSVKVSYLEIY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  151 CERVRDLLNPKNKGNLRVREHPLL----GPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFT 226
Cdd:cd01364   150 NEELFDLLSPSSDVSERLRMFDDPrnkrGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIH 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  227 QKrhdaETNITTE---KVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSgpnknkkkkktdF 303
Cdd:cd01364   230 IK----ETTIDGEelvKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAP------------H 293
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  304 IPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIRCNAIINED 363
Cdd:cd01364   294 VPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
Kinesin_assoc pfam16183
Kinesin-associated;
358-515 8.83e-92

Kinesin-associated;


Pssm-ID: 435195 [Multi-domain]  Cd Length: 170  Bit Score: 294.42  E-value: 8.83e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   358 AIINEDPNNKLIRELKDEVTRLRDLLYAQGLGDITDM------------TNALVGMSPSSSLSALSSRAASVSSLHERIL 425
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLGDIIDArastpaanasaaTAAMAGASPSPSLSALSSRAASVSSLHERIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   426 FAPGSEEAIERLKETEKIIAELNETWEEKLRRTEAIRMEREALLAEMGVAMREDGGTLGVFSPKKTPHLVNLNEDPLMSE 505
Cdd:pfam16183   81 FTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSE 160
                          170
                   ....*....|
gi 659667948   506 CLLYYIKDGV 515
Cdd:pfam16183  161 CLLYYIKDGI 170
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
491-605 2.97e-82

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: 264.87  E-value: 2.97e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  491 TPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFRSDSRGGGEAVVTLEPCEGADTYVNGK 570
Cdd:cd22726     1 TPHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSGGEAVVTLEPCEGADTYVNGK 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 659667948  571 KVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 605
Cdd:cd22726    81 KVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
5-381 9.76e-81

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 278.16  E-value: 9.76e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    5 SVKVAVRVRPfnsREMSRDskcIIQMSGSTTTIVNpkqpKETPKSFSFDYSYWSHtspedinyASQKQVYRDIGEEMLQH 84
Cdd:COG5059    23 DIKSTIRIIP---GELGER---LINTSKKSHVSLE----KSKEGTYAFDKVFGPS--------ATQEDVYEETIKPLIDS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   85 AFEGYNVCIFAYGQTGAGKSYTMMGkqEKDQQGIIPQLCEDLFSRInDTTNDNMSYSVEVSYMEIYCERVRDLLNPKNKG 164
Cdd:COG5059    85 LLLGYNCTVFAYGQTGSGKTYTMSG--TEEEPGIIPLSLKELFSKL-EDLSMTKDFAVSISYLEIYNEKIYDLLSPNEES 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  165 nLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITtekvSKI 244
Cdd:COG5059   162 -LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET----SKL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  245 SLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALaeMDSGPNKNkkkkktdfIPYRDSVLTWLLRENLGGNSR 324
Cdd:COG5059   237 SLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINAL--GDKKKSGH--------IPYRESKLTRLLQDSLGGNCN 306
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 659667948  325 TAMVAALSPADINYDETLSTLRYADRAKQIRcNAIINEDPNNKLIR--ELKDEVTRLRD 381
Cdd:COG5059   307 TRVICTISPSSNSFEETINTLKFASRAKSIK-NKIQVNSSSDSSREieEIKFDLSEDRS 364
PLN03188 PLN03188
kinesin-12 family protein; Provisional
1-381 2.15e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 273.73  E-value: 2.15e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    1 MAGASVKVAVRVRPFNSREmsrDSKCIIQ-MSGSTTTIvnpkqpkeTPKSFSFDysywSHTSPEdinyASQKQVYRDIGE 79
Cdd:PLN03188   95 VSDSGVKVIVRMKPLNKGE---EGEMIVQkMSNDSLTI--------NGQTFTFD----SIADPE----STQEDIFQLVGA 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   80 EMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQ--------EKDQQGIIPQLCEDLFSRINDT----TNDNMSYSVEVSYM 147
Cdd:PLN03188  156 PLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlSGDQQGLTPRVFERLFARINEEqikhADRQLKYQCRCSFL 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  148 EIYCERVRDLLNPKNKgNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQ 227
Cdd:PLN03188  236 EIYNEQITDLLDPSQK-NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVES 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  228 KRHDAETNITTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSgpnknkkKKKTDFIPYR 307
Cdd:PLN03188  315 RCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQ-------TGKQRHIPYR 387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  308 DSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIRCNAIINE---DPNNKL---IRELKDEVTRLRD 381
Cdd:PLN03188  388 DSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqDDVNFLrevIRQLRDELQRVKA 467
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
6-352 4.75e-74

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: 250.29  E-value: 4.75e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    6 VKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVN-PKQ-----PKETPKSFSFDYSYwshtsPEDinyASQKQVYRDIGE 79
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHePKLkvdltKYIENHTFRFDYVF-----DES---SSNETVYRSTVK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   80 EMLQHAFEGYNVCIFAYGQTGAGKSYTMMGK--QEKDQQGIIPQLCEDLFSRINdTTNDNMSYSVEVSYMEIYCERVRDL 157
Cdd:cd01367    74 PLVPHIFEGGKATCFAYGQTGSGKTYTMGGDfsGQEESKGIYALAARDVFRLLN-KLPYKDNLGVTVSFFEIYGGKVFDL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  158 LNPKNKgnLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFtqkrHDAETNIT 237
Cdd:cd01367   153 LNRKKR--VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL----RDRGTNKL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  238 tekVSKISLVDLAGSER-ADSTGAKGTRLKEGANINKSLTTLGKVISALAemdsgpnknkkkKKTDFIPYRDSVLTWLLR 316
Cdd:cd01367   227 ---HGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHIPFRGSKLTQVLK 291
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 659667948  317 ENL-GGNSRTAMVAALSPADINYDETLSTLRYADRAK 352
Cdd:cd01367   292 DSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
6-352 6.02e-72

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: 244.61  E-value: 6.02e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    6 VKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVN-PKQP-----------KETPKSFSFDYSywshtsPEdinyASQKQV 73
Cdd:cd01368     3 VKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHpPKGSaanksernggqKETKFSFSKVFG------PN----TTQKEF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   74 YRDIGEEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEkdQQGIIPQLCEDLFSRINDttndnmsYSVEVSYMEIYCER 153
Cdd:cd01368    73 FQGTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPG--DGGILPRSLDVIFNSIGG-------YSVFVSYIEIYNEY 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  154 VRDLLNP------KNKGNLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQ 227
Cdd:cd01368   144 IYDLLEPspssptKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQ 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  228 KRHDAETNITTEK----VSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEmdsgpnkNKKKKKTDF 303
Cdd:cd01368   224 APGDSDGDVDQDKdqitVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE-------NQLQGTNKM 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 659667948  304 IPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAK 352
Cdd:cd01368   297 VPFRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
6-352 1.91e-70

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: 239.33  E-value: 1.91e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    6 VKVAVRVRPFNSREMSRDSK-CIIQMSGSTTTIVNPKQPKEtPKSFSFDYSYwshtSPEDinyaSQKQVYRDIGEEMLQH 84
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPsCVSGIDSCSVELADPRNHGE-TLKYQFDAFY----GEES----TQEDIYAREVQPIVPH 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   85 AFEGYNVCIFAYGQTGAGKSYTMMGKQEkdQQGIIPQLCEDLFsRINDTTNDnmSYSVEVSYMEIYCERVRDLLNPKNKg 164
Cdd:cd01376    73 LLEGQNATVFAYGSTGAGKTFTMLGSPE--QPGLMPLTVMDLL-QMTRKEAW--ALSFTMSYLEIYQEKILDLLEPASK- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  165 NLRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITTekvSKI 244
Cdd:cd01376   147 ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRT---GKL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  245 SLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGpnknkkkkktdfIPYRDSVLTWLLRENLGGNSR 324
Cdd:cd01376   224 NLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR------------IPYRDSKLTRLLQDSLGGGSR 291
                         330       340
                  ....*....|....*....|....*...
gi 659667948  325 TAMVAALSPADINYDETLSTLRYADRAK 352
Cdd:cd01376   292 CIMVANIAPERTFYQDTLSTLNFAARSR 319
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
490-599 2.37e-68

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: 224.91  E-value: 2.37e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  490 KTPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFRSDSRGGGEAVVTLEPCEGADTYVNG 569
Cdd:cd22727     1 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNNNGEVIVTLEPCERSETYVNG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 659667948  570 KKVTEPSILRSGNRIIMGKSHVFRFNHPEQ 599
Cdd:cd22727    81 KRVVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
491-596 1.52e-63

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: 210.94  E-value: 1.52e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  491 TPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFRSDsrgggEAVVTLEPCEGADTYVNGK 570
Cdd:cd22705     1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENE-----DGVVTLEPCEGALTYVNGK 75
                          90       100
                  ....*....|....*....|....*.
gi 659667948  571 KVTEPSILRSGNRIIMGKSHVFRFNH 596
Cdd:cd22705    76 RVTEPTRLKTGSRVILGKNHVFRFNH 101
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
5-352 1.53e-63

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: 220.14  E-value: 1.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    5 SVKVAVRVRP----------FNSREMSRDSKCIIQMSGStttIVNPKQpkeTPKSFSFDYSywshtspedINYASQKQVY 74
Cdd:cd01375     1 KVQAFVRVRPtddfahemikYGEDGKSISIHLKKDLRRG---VVNNQQ---EDWSFKFDGV---------LHNASQELVY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   75 RDIGEEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEK-DQQGIIPQLCEDLFSRInDTTNDNMsYSVEVSYMEIYCER 153
Cdd:cd01375    66 ETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENyKHRGIIPRALQQVFRMI-EERPTKA-YTVHVSYLEIYNEQ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  154 VRDLLNPKNKGN-----LRVREHPLLGPYVEDLSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQK 228
Cdd:cd01375   144 LYDLLSTLPYVGpsvtpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAH 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  229 RHDA--ETNITtekvSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSgpnknkkkkktDFIPY 306
Cdd:cd01375   224 SRTLssEKYIT----SKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDR-----------THVPF 288
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 659667948  307 RDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAK 352
Cdd:cd01375   289 RQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
491-596 3.97e-58

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: 195.47  E-value: 3.97e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  491 TPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAerrqDIVLSGHFIKEEHCIFRSDSRGGGEAVVTLEPCEGADTYVNGK 570
Cdd:cd22728     1 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFRSIPNPSGEVVVTLEPCEGAETYVNGK 76
                          90       100
                  ....*....|....*....|....*.
gi 659667948  571 KVTEPSILRSGNRIIMGKSHVFRFNH 596
Cdd:cd22728    77 QVTEPLVLKSGNRIVMGKNHVFRFNH 102
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
1148-1301 6.62e-56

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 432581  Cd Length: 146  Bit Score: 190.88  E-value: 6.62e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  1148 DYIPAVVDHRGGMPcMGTFLLHQGIQRRITVTLLHETGSHIRWKEVRELVVGRIRNTPETDEALIDPN--ILSLNILSSG 1225
Cdd:pfam12473    1 EYVPVPVDQRSELD-PGTFQLHQGLQRRIVITLTHSSGDELPWERVREVRVGDVRLLDMKGRVPDSDStpDVSLKLLSKP 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 659667948  1226 YVHPAQDDRqfldsdiprTFYQFEAAWDSSMHNSLLLNRVTPYREKIYMTLSAYIEMENCTQPAVITKDFCMVFYS 1301
Cdd:pfam12473   80 VVRFNADGT---------SSYTIEAQWDSSLHNSLLLNRVTADGYRVYLTLAWDLVSEKCAEPVRFSMDTCVQIYP 146
PH_KIFIA_KIFIB cd01233
KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA ...
1579-1681 5.20e-54

KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA (Caenorhabditis elegans homolog unc-104) and KIFIB transport synaptic vesicle precursors that contain synaptic vesicle proteins, such as synaptophysin, synaptotagmin and the small GTPase RAB3A, but they do not transport organelles that contain plasma membrane proteins. They have a N-terminal motor domain, followed by a coiled-coil domain, and a C-terminal PH domain. KIF1A adopts a monomeric form in vitro, but acts as a processive dimer in vivo. KIF1B has alternatively spliced isoforms distinguished by the presence or absence of insertion sequences in the conserved amino-terminal region of the protein; this results in their different motor activities. KIF1A and KIF1B bind to RAB3 proteins through the adaptor protein mitogen-activated protein kinase (MAPK) -activating death domain (MADD; also calledDENN), which was first identified as a RAB3 guanine nucleotide exchange factor (GEF). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269939  Cd Length: 103  Bit Score: 183.56  E-value: 5.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948 1579 RVSPIVSKKGYLHFLEPHTAGWAKRFVVVRRPYAYMYNSDKDTVERFVLNLSTAQVEYSEDQQAMLKTPNTFAVCTEHRG 1658
Cdd:cd01233     1 PKSPVVSKRGYLLFLEDATDGWVRRWVVLRRPYLHIYSSEKDGDERGVINLSTARVEYSPDQEALLGRPNVFAVYTPTNS 80
                          90       100
                  ....*....|....*....|...
gi 659667948 1659 ILLQANSDKDMHDWLYAFNPLLA 1681
Cdd:cd01233    81 YLLQARSEKEMQDWLYAIDPLLA 103
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
8-284 1.93e-45

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: 161.74  E-value: 1.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948    8 VAVRVRPFNSREMSRDSKCIIqmsgstttivnpkqpketpksfsfdysywshTSPEDINYASQKQVYRDIGeEMLQHAFE 87
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKIIV-------------------------------FYRGFRRSESQPHVFAIAD-PAYQSMLD 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   88 GYNV-CIFAYGQTGAGKSYTMMgkqekdqqGIIPQLCEDLFSRINDTTNDNMSYsvevsymeiycervrdllnpknkgnl 166
Cdd:cd01363    49 GYNNqSIFAYGESGAGKTETMK--------GVIPYLASVAFNGINKGETEGWVY-------------------------- 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  167 rvrehpllgpyvedLSKLAVTSYNDIQDLMDSGNKARTvAATNMNETSSRSHAVFNIiftqkrhdaetnittekvskisL 246
Cdd:cd01363    95 --------------LTEITVTLEDQILQANPILEAFGN-AKTTRNENSSRFGKFIEI----------------------L 137
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 659667948  247 VDLAGSERadstgakgtrlkeganINKSLTTLGKVISA 284
Cdd:cd01363   138 LDIAGFEI----------------INESLNTLMNVLRA 159
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
490-597 4.53e-37

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: 135.48  E-value: 4.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  490 KTPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFrsDSRGGgeaVVTLEPCEGADTYVNG 569
Cdd:cd22708     7 ELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCII--ENVGG---VVTLHPLPGALCAVNG 81
                          90       100
                  ....*....|....*....|....*...
gi 659667948  570 KKVTEPSILRSGNRIIMGKSHVFRFNHP 597
Cdd:cd22708    82 QVITQPTRLTQGDVILLGKTNMFRFNHP 109
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
490-597 1.48e-36

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: 133.93  E-value: 1.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  490 KTPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFRsdSRGGgeaVVTLEPCEGADTYVNG 569
Cdd:cd22707     6 KLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIE--NNGG---KVTIIPVGDAETYVNG 80
                          90       100
                  ....*....|....*....|....*...
gi 659667948  570 KKVTEPSILRSGNRIIMGKSHVFRFNHP 597
Cdd:cd22707    81 ELISEPTVLHHGDRVILGGDHYFRFNHP 108
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
492-597 2.53e-36

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: 133.11  E-value: 2.53e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  492 PHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFrsdSRGGGEavVTLEPC-EGADTYVNGK 570
Cdd:cd22709     1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVI---TNTDGK--VTIEPVsPGAKVIVNGV 75
                          90       100
                  ....*....|....*....|....*..
gi 659667948  571 KVTEPSILRSGNRIIMGKSHVFRFNHP 597
Cdd:cd22709    76 PVTGETELHHLDRVILGSNHLYVFVGP 102
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
484-606 2.73e-33

forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); 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). 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: 438783 [Multi-domain]  Cd Length: 119  Bit Score: 125.27  E-value: 2.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  484 GVFSPKKTPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFRSDSrgggeAVVTLEPCEGA 563
Cdd:cd22731     1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNEC-----GVVTLRPAQGA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 659667948  564 DTYVNGKKVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERER 606
Cdd:cd22731    76 QCTVNGREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQR 118
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
494-597 7.21e-33

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: 123.17  E-value: 7.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  494 LVNLNEDPLMSECLLYYIKDgVTRVGREDAERRQDIVLSGHFIKEEHCIFRSDSRGggeavVTLEPCEGADTYVNGKKVT 573
Cdd:cd22706     4 LVNLNADPSLNELLVYYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIENED-----VYLTPLEGARTCVNGSIVT 77
                          90       100
                  ....*....|....*....|....
gi 659667948  574 EPSILRSGNRIIMGKSHVFRFNHP 597
Cdd:cd22706    78 EKTQLRHGDRILWGNNHFFRLNCP 101
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
484-605 2.73e-28

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: 110.79  E-value: 2.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  484 GVFSPKKTPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFrsDSRGGgeaVVTLEPCEGA 563
Cdd:cd22732     1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIF--ENLNG---TVTLIPLNGA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 659667948  564 DTYVNGKKVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 605
Cdd:cd22732    76 QCSVNGVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
494-604 1.40e-20

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: 88.41  E-value: 1.40e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  494 LVNLNEDPLMSECLLYYIKDGvTRVGredAERRQDIVLSGHFIKEEHCIFRSDSRGGgeavVTLEPCEGADTYVNGKKVT 573
Cdd:cd22729     4 LVNLNADPALNELLVYYLKDH-TRVG---ADTSQDIQLFGIGIQPEHCVIDIAADGD----VTLTPKENARTCVNGTLVC 75
                          90       100       110
                  ....*....|....*....|....*....|.
gi 659667948  574 EPSILRSGNRIIMGKSHVFRFNHPEQARQER 604
Cdd:cd22729    76 SVTQLWHGDRILWGNNHFFRINLPKRKRRDW 106
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
494-597 1.05e-19

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: 85.74  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  494 LVNLNEDPLMSECLLYYIKDGvTRVGREDAerrQDIVLSGHFIKEEHCIFRSDSrgggEAVVTLEPCEGADTYVNGKKVT 573
Cdd:cd22730     4 LVNLNADPALNELLVYYLKEH-TLIGSADS---QDIQLCGMGILPEHCIIDITP----EGQVMLTPQKNTRTFVNGSAVT 75
                          90       100
                  ....*....|....*....|....
gi 659667948  574 EPSILRSGNRIIMGKSHVFRFNHP 597
Cdd:cd22730    76 SPIQLHHGDRILWGNNHFFRINLP 99
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
478-602 6.54e-17

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: 78.14  E-value: 6.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  478 EDGGTLGVFSPKktPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAErrqDIVLSGHFIKEEHCIFrsDSRGGgeaVVTL 557
Cdd:cd22713     5 ETGKALKVQTEK--PHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASD---IISLQGPGVEPEHCYI--ENING---TVTL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 659667948  558 EPCEGADTyVNGKKVTEPSILRSGNRIIMGKSHVFRFNHPEQARQ 602
Cdd:cd22713    75 YPCGNLCS-VDGLPITEPTRLTQGCMICLGRSNYFRFNHPAEAKR 118
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
492-597 7.03e-17

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: 77.75  E-value: 7.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  492 PHLVNLNEDPLMSECL-LYYIKDGVTRVG--REDAERRQDIVLSGHFIKEEHCIFRSDsrgggEAVVTLEPCEG-ADTYV 567
Cdd:cd22711     2 PYLLELSPDGSDRDKPrRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVITHM-----EGVVTVTPASQdAETYV 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 659667948  568 NGKKVTEPSILRSGNRIIMGKSHVFRFNHP 597
Cdd:cd22711    77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
6-158 2.22e-15

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


Pssm-ID: 435586 [Multi-domain]  Cd Length: 144  Bit Score: 74.56  E-value: 2.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948     6 VKVAVRVRPFNSREmsrdskCIIQMSGSTTTIvnpKQPKETPKSFSFDYSYwshtSPEdinyASQKQVYRDIgeEML-QH 84
Cdd:pfam16796   22 IRVFARVRPELLSE------AQIDYPDETISD---GKIGSKNKSFSFDRVF----PPE----SEQEDVFQEI--SQLvQS 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 659667948    85 AFEGYNVCIFAYGQTGAGKSYTMmgkqekdqqgiIPQLCEDLFSRINDTTNdNMSYSVEVSYMEIYCERVRDLL 158
Cdd:pfam16796   83 CLDGYNVCIFAYGQTGSGSNPGM-----------IPRARKEIFKFISELKK-GWKYTIELQFVEIYNESSQDLL 144
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
805-852 1.35e-14

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: 432544  Cd Length: 43  Bit Score: 69.17  E-value: 1.35e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 659667948   805 LRQRLDLMREMYDRAAEVPSSVVEDCDNvvtggDPFYDRFPWFRLVGR 852
Cdd:pfam12423    1 LRNRLIDMREMYQEYKEGEYSQHFEVEK-----DPFYEPPENHSLIGV 43
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1584-1677 5.40e-12

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574  Cd Length: 102  Bit Score: 63.72  E-value: 5.40e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948   1584 VSKKGYLHFLEP-HTAGWAKRFVVVRRPYAYMYNSDK---DTVERFVLNLSTAQVEYSEDQQAMlKTPNTFAVCTEHRG- 1658
Cdd:smart00233    1 VIKEGWLYKKSGgGKKSWKKRYFVLFNSTLLYYKSKKdkkSYKPKGSIDLSGCTVREAPDPDSS-KKPHCFEIKTSDRKt 79
                            90
                    ....*....|....*....
gi 659667948   1659 ILLQANSDKDMHDWLYAFN 1677
Cdd:smart00233   80 LLLQAESEEEREKWVEALR 98
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1584-1677 5.71e-11

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 395117 [Multi-domain]  Cd Length: 105  Bit Score: 61.04  E-value: 5.71e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  1584 VSKKGYLHFLEPHTA-GWAKRFVVVRRPYAYMYNSD---KDTVERFVLNLSTAQVEYSEDQqAMLKTPNTFAVCT----E 1655
Cdd:pfam00169    1 VVKEGWLLKKGGGKKkSWKKRYFVLFDGSLLYYKDDkskKSKEPKGSISLSGCEVVEVVAS-DSPKRKFCFELRTgertG 79
                           90       100
                   ....*....|....*....|..
gi 659667948  1656 HRGILLQANSDKDMHDWLYAFN 1677
Cdd:pfam00169   80 KRTYLLQAESEEERKDWIKAIQ 101
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
493-594 1.32e-10

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: 59.21  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  493 HLVNLNEDPLMSEcllYYIKDGVTRVGREDAerrQDIVLSGHFIKEEHCIFRSDSRGggeavVTLEPCEGAD-TYVNGKK 571
Cdd:cd00060     1 RLIVLDGDGGGRE---FPLTKGVVTIGRSPD---CDIVLDDPSVSRRHARIEVDGGG-----VYLEDLGSTNgTFVNGKR 69
                          90       100
                  ....*....|....*....|...
gi 659667948  572 VTEPSILRSGNRIIMGKsHVFRF 594
Cdd:cd00060    70 ITPPVPLQDGDVIRLGD-TTFRF 91
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
490-597 1.07e-08

forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. 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: 438785  Cd Length: 113  Bit Score: 54.80  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  490 KTPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQDIVLSGHFIKEEHCIFR--SDSRGGGEAVVTLEPCEGADTYV 567
Cdd:cd22733     4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRrvRLPKHRSEEKLVLEPIPGAHVSV 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 659667948  568 NGKKVTEPSILRSGNRIIMGKSHVFRFNHP 597
Cdd:cd22733    84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
1584-1677 2.88e-08

Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal proteins are unknown, but they all contain 2 PH domains. This cd represents the first PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270110  Cd Length: 106  Bit Score: 53.01  E-value: 2.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948 1584 VSKKGYLHFLEPHTAGWAKRFVVVRRPYAYMYNSDKDTVERFVLNLS--TAqVEYSEDQqamlKTPNTFAVCTEHRGILL 1661
Cdd:cd13298     6 VLKSGYLLKRSRKTKNWKKRWVVLRPCQLSYYKDEKEYKLRRVINLSelLA-VAPLKDK----KRKNVFGIYTPSKNLHF 80
                          90
                  ....*....|....*.
gi 659667948 1662 QANSDKDMHDWLYAFN 1677
Cdd:cd13298    81 RATSEKDANEWVEALR 96
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
491-597 5.17e-08

forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. 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: 438764 [Multi-domain]  Cd Length: 120  Bit Score: 53.07  E-value: 5.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948  491 TPHLVNLNEDPLMSECLLYYIKDGVTRVGREDAERRQ-DIVLSGHFIKEEHC-IFRSDSRGGGEA---------VVTLEP 559
Cdd:cd22712     3 YPYLLTLRGFSPKQDLLVYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCwIRRKPEPLSDDEdsdkesadyRVVLSP 82
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 659667948  560 CEGADTYVNGKKVTEPSILRSGNRIIMGKSHVFRFNHP 597
Cdd:cd22712    83 LRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
516-584 1.99e-07

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


Pssm-ID: 425720 [Multi-domain]  Cd Length: 66  Bit Score: 49.50  E-value: 1.99e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 659667948   516 TRVGREDaerRQDIVLSGHFIKEEHCIFRSDsrggGEAVVTLEPC-EGADTYVNGKKVT-EPSILRSGNRI 584
Cdd:pfam00498    1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYD----GGGRFYLEDLgSTNGTFVNGQRLGpEPVRLKDGDVI 64
PH_TBC1D2A cd01265
TBC1 domain family member 2A pleckstrin homology (PH) domain; TBC1D2A (also called PARIS-1 ...
1588-1673 2.21e-07

TBC1 domain family member 2A pleckstrin homology (PH) domain; TBC1D2A (also called PARIS-1/Prostate antigen recognized and identified by SEREX 1 and ARMUS) contains a PH domain and a TBC-type GTPase catalytic domain. TBC1D2A integrates signaling between Arf6, Rac1, and Rab7 during junction disassembly. Activated Rac1 recruits TBC1D2A to locally inactivate Rab7 via its C-terminal TBC/RabGAP domain and facilitate E-cadherin degradation in lysosomes. The TBC1D2A PH domain mediates localization at cell-cell contacts and coprecipitates with cadherin complexes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269966  Cd Length: 102  Bit Score: 50.40  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948 1588 GYLHFLEPHTA---GWAKRFVVV--RRPYAYMYNSDKDTVERFVLNLSTAQVEYSEDQQamlktPNTFAVCTEHRGILLQ 1662
Cdd:cd01265     4 GYLNKLETRGLglkGWKRRWFVLdeSKCQLYYYRSPQDATPLGSIDLSGAAFSYDPEAE-----PGQFEIHTPGRVHILK 78
                          90
                  ....*....|.
gi 659667948 1663 ANSDKDMHDWL 1673
Cdd:cd01265    79 ASTRQAMLYWL 89
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
1586-1676 3.65e-06

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 46.77  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948 1586 KKGYLHFLEPHT-AGWAKRFVVVRRPYAYMYNSDKD--TVERFVLNLStAQVEYSEDQQamLKTPNTFAVCT-EHRGILL 1661
Cdd:cd00821     1 KEGYLLKRGGGGlKSWKKRWFVLFEGVLLYYKSKKDssYKPKGSIPLS-GILEVEEVSP--KERPHCFELVTpDGRTYYL 77
                          90
                  ....*....|....*
gi 659667948 1662 QANSDKDMHDWLYAF 1676
Cdd:cd00821    78 QADSEEERQEWLKAL 92
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
1581-1677 3.82e-06

Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 (also called PLEKHA2) adaptors to PtdIns(3,4)P(2), but not PI(3,4, 5)P3, function as negative regulators of insulin and PI3K signalling pathways (i.e. TAPP/utrophin/syntrophin complex). TAPP2 contains two sequential PH domains in which the C-terminal PH domain specifically binds PtdIns(3,4)P2 with high affinity. The N-terminal PH domain does not interact with any phosphoinositide tested. They also contain a C-terminal PDZ-binding motif that interacts with several PDZ-binding proteins, including PTPN13 (known previously as PTPL1 or FAP-1) as well as the scaffolding proteins MUPP1 (multiple PDZ-domain-containing protein 1), syntrophin and utrophin. The members here are most sequence similar to TAPP2 proteins, but may not be actual TAPP2 proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270075  Cd Length: 110  Bit Score: 47.41  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948 1581 SPIVSKKGYLHFLEPHTAGWAKRFVVVRRPYAYMYNSDKdtvERFVLNL-------STAQVEysedqqaMLKTPNTFAVC 1653
Cdd:cd13255     3 SEAVLKAGYLEKKGERRKTWKKRWFVLRPTKLAYYKNDK---EYRLLRLidltdihTCTEVQ-------LKKHDNTFGIV 72
                          90       100
                  ....*....|....*....|....
gi 659667948 1654 TEHRGILLQANSDKDMHDWLYAFN 1677
Cdd:cd13255    73 TPARTFYVQADSKAEMESWISAIN 96
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
516-572 4.02e-06

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


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 45.25  E-value: 4.02e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 659667948    516 TRVGRedAERRQDIVLSGHFIKEEHCIFRSDsrggGEAVVTLEPC-EGADTYVNGKKV 572
Cdd:smart00240    1 VTIGR--SSEDCDIQLDGPSISRRHAVIVYD----GGGRFYLIDLgSTNGTFVNGKRI 52
PH_DAPP1 cd10573
Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; ...
1582-1672 3.67e-05

Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; DAPP1 (also known as PHISH/3' phosphoinositide-interacting SH2 domain-containing protein or Bam32) plays a role in B-cell activation and has potential roles in T-cell and mast cell function. DAPP1 promotes B cell receptor (BCR) induced activation of Rho GTPases Rac1 and Cdc42, which feed into mitogen-activated protein kinases (MAPK) activation pathways and affect cytoskeletal rearrangement. DAPP1can also regulate BCR-induced activation of extracellular signal-regulated kinase (ERK), and c-jun NH2-terminal kinase (JNK). DAPP1 contains an N-terminal SH2 domain and a C-terminal pleckstrin homology (PH) domain with a single tyrosine phosphorylation site located centrally. DAPP1 binds strongly to both PtdIns(3,4,5)P3 and PtdIns(3,4)P2. The PH domain is essential for plasma membrane recruitment of PI3K upon cell activation. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269977 [Multi-domain]  Cd Length: 96  Bit Score: 44.24  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948 1582 PIVSKKGYLHFLEPHTAGWAKRFVVVRRPYAYMYNSDKDTVERFVLNLSTAQ-VEYSEDQQamlkTPNTFAVCTEHRGIL 1660
Cdd:cd10573     1 SLGSKEGYLTKLGGIVKNWKTRWFVLRRNELKYFKTRGDTKPIRVLDLRECSsVQRDYSQG----KVNCFCLVFPERTFY 76
                          90
                  ....*....|..
gi 659667948 1661 LQANSDKDMHDW 1672
Cdd:cd10573    77 MYANTEEEADEW 88
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
1586-1675 1.17e-03

ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho/Rac/Cdc42-like GTPase activating proteins with a RhoGAP domain. These proteins functions as a GTPase-activating protein (GAP) for RHOA and CDC42. ARHGAP21 controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. It is recruited to the Golgi by to GTPase, ARF1, through its PH domain and its helical motif. It is also required for CTNNA1 recruitment to adherens junctions. ARHGAP21 and it related proteins all contains a PH domain and a RhoGAP domain. Some of the members have additional N-terminal domains including PDZ, SH3, and SPEC. The ARHGAP21 PH domain interacts with the GTPbound forms of both ARF1 and ARF6 ARF-binding domain/ArfBD. The members here include: ARHGAP15, ARHGAP21, and ARHGAP23. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269955  Cd Length: 113  Bit Score: 40.43  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 659667948 1586 KKGYLHFLEPHTAG--------WAKRFVVVRRPYAYMYNsDKDTVE-----------RFVLNLSTAQVEYSEdqqamLKT 1646
Cdd:cd01253     2 REGWLHYKQIVTDKgkrvsdrsWKQAWAVLRGHSLYLYK-DKREQTpalsielgseqRISIRGCIVDIAYSY-----TKR 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 659667948 1647 PNTFAVCT----EHrgiLLQANSDKDMHDWLYA 1675
Cdd:cd01253    76 KHVFRLTTsdfsEY---LFQAEDRDDMLGWIKA 105
ERM pfam00769
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ...
624-678 6.83e-03

Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.


Pssm-ID: 425860 [Multi-domain]  Cd Length: 247  Bit Score: 40.31  E-value: 6.83e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 659667948   624 RELLEKQgidmKQEMEQRLQELEDQYRR------EREEATYLLEQQRLDYESKLEALQKQM 678
Cdd:pfam00769    1 REEAERE----KQELEERLKQYEEETRKaqeeleESEETAELLEEKLRVAEEEAELLEQKA 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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