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Conserved domains on  [gi|688611584|ref|XP_009295087|]
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kinesin-like protein KIF1B isoform X2 [Danio rerio]

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 ...
4-360 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: 666.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    4 ASVKVAVRVRPFNSRETGKESKCIIQMQGNSTTILNPKN--------PKEPKTFSFDYSYWSHTSPDdPSFASQNQVYND 75
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkatREVPKSFSFDYSYWSHDSED-PNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   76 IGKEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEegQEGIIPQLCEELFEKINDNNNEEISYSVEVAYMEIYCERVRD 155
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  156 LLNPK---NKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYDSE 232
Cdd:cd01365   158 LLNPKpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  233 TDLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskSKKKKKTDFIPYRDSVLTW 312
Cdd:cd01365   238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSS----GKSKKKSSFIPYRDSVLTW 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 688611584  313 LLRENLGGNSRTAMVAALSPADINFDETLSTLRYADRAKQIKCNAVIN 360
Cdd:cd01365   314 LLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
Kinesin_assoc pfam16183
Kinesin-associated;
357-593 1.97e-89

Kinesin-associated;


:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 288.28  E-value: 1.97e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   357 AVINEDPNAKLVRELKDEVSRLKELLRAQGLGDILDIEPMGDdclgsgskcddindvkTLLSSQTEAMLYRRKAPMGCLT 436
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLGDIIDTIAHPT----------------KKRANTPAANASAATAAMAGAS 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   437 ASPSSGSLCSQAGlqSVSSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDG 516
Cdd:pfam16183   65 PSPSLSALSSRAA--SVSSLHERIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDG 142
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688611584   517 GTLgvfspkkfgpdrptslsiedfsvyssnqlfverpcevytdfnGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGI 593
Cdd:pfam16183  143 GTL------------------------------------------GVFSPKKTPHLVNLNEDPLMSECLLYYIKDGI 177
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
568-677 1.62e-77

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: 251.49  E-value: 1.62e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  568 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNANGHVIVTLEPCEGSETYVNG 647
Cdd:cd22727     1 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNNNGEVIVTLEPCERSETYVNG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 688611584  648 KRVNSAVQLRSGNRIIMGKNHVFRFNHPEQ 677
Cdd:cd22727    81 KRVVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
1370-1526 9.89e-60

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: 463599  Cd Length: 149  Bit Score: 202.04  E-value: 9.89e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  1370 EYIPAVVDHTGGLPcHGTYLLHQGIQRRITVTLIHEKGSELHWKDVRELVVGRIRN---KPEVDDSAADAVLSLNIISAK 1446
Cdd:pfam12473    1 EYVPVPVDQRSELD-PGTFQLHQGLQRRIVITLTHSSGDELPWERVRNVRVGDVRLldmKGRVPDSDSTPDVSLKLLSKP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  1447 NLKSSHNSsslcidsdisRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAIITKDICMVFYSRDA 1526
Cdd:pfam12473   80 VVRFNADG----------TSSYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
PH_KIFIA_KIFIB cd01233
KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA ...
1805-1907 1.32e-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: 185.49  E-value: 1.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584 1805 RPGSVVSKKGILNFMEPRSNTWVKHFVVVRRPYVFIYNNDKDPVERGVLNLSTAQVEYSEDQQAMLKTPHTFAMCTKHRG 1884
Cdd:cd01233     1 PKSPVVSKRGYLLFLEDATDGWVRRWVVLRRPYLHIYSSEKDGDERGVINLSTARVEYSPDQEALLGRPNVFAVYTPTNS 80
                          90       100
                  ....*....|....*....|...
gi 688611584 1885 ILLQANNDKDMNDWLYAFNPLLA 1907
Cdd:cd01233    81 YLLQARSEKEMQDWLYAIDPLLA 103
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
886-934 1.12e-13

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


:

Pssm-ID: 463574  Cd Length: 43  Bit Score: 66.86  E-value: 1.12e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 688611584   886 LKQRLDQMREMYDRAGEMASSNQGDDGEgaltgsDPFYDRFHWFKLVGS 934
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR------DPFYEPPENHNLIGV 43
GBP_C super family cl46256
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
677-751 7.37e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


The actual alignment was detected with superfamily member cd16269:

Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.72  E-value: 7.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688611584  677 QARAEREKTPSAEtpvepvdwtfAQRELLEKQGIDMKQEMEKR----LTEMEILYKKEKEEADQLLEQQRLVYESKLQE 751
Cdd:cd16269   199 EIEAERAKAEAAE----------QERKLLEEQQRELEQKLEDQersyEEHLRQLKEKMEEERENLLKEQERALESKLKE 267
KIF1B super family cl13810
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
996-1018 3.84e-03

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.


The actual alignment was detected with superfamily member pfam12423:

Pssm-ID: 463574  Cd Length: 43  Bit Score: 36.81  E-value: 3.84e-03
                           10        20
                   ....*....|....*....|...
gi 688611584   996 SDIFSDGQDPFYDRSPWFILVGR 1018
Cdd:pfam12423   21 SQHFEVDRDPFYEPPENHNLIGV 43
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
4-360 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: 666.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    4 ASVKVAVRVRPFNSRETGKESKCIIQMQGNSTTILNPKN--------PKEPKTFSFDYSYWSHTSPDdPSFASQNQVYND 75
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkatREVPKSFSFDYSYWSHDSED-PNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   76 IGKEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEegQEGIIPQLCEELFEKINDNNNEEISYSVEVAYMEIYCERVRD 155
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  156 LLNPK---NKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYDSE 232
Cdd:cd01365   158 LLNPKpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  233 TDLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskSKKKKKTDFIPYRDSVLTW 312
Cdd:cd01365   238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSS----GKSKKKSSFIPYRDSVLTW 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 688611584  313 LLRENLGGNSRTAMVAALSPADINFDETLSTLRYADRAKQIKCNAVIN 360
Cdd:cd01365   314 LLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
5-360 2.10e-152

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: 472.44  E-value: 2.10e-152
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584      5 SVKVAVRVRPFNSRETGKESKCIIQMQGN---STTILNPKNPKEPKTFSFDYSYwshtspddPSFASQNQVYNDIGKEML 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKvgkTLTVRSPKNRQGEKKFTFDKVF--------DATASQEDVFEETAAPLV 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584     82 QHAFEGYNVCIFAYGQTGAGKSYTMMGKQEEgqEGIIPQLCEELFEKInDNNNEEISYSVEVAYMEIYCERVRDLLNPkN 161
Cdd:smart00129   73 DSVLEGYNATIFAYGQTGSGKTYTMIGTPDS--PGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP-S 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    162 KGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYDSETDlsTEKVS 241
Cdd:smart00129  149 SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSG--SGKAS 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    242 KISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkkTDFIPYRDSVLTWLLRENLGGN 321
Cdd:smart00129  227 KLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK----------SRHIPYRDSKLTRLLQDSLGGN 296
                           330       340       350
                    ....*....|....*....|....*....|....*....
gi 688611584    322 SRTAMVAALSPADINFDETLSTLRYADRAKQIKCNAVIN 360
Cdd:smart00129  297 SKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-353 1.58e-143

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 447.79  E-value: 1.58e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    11 RVRPFNSRETGKESKCIIQM--QGNSTTILNPKNPK-EPKTFSFDYSYWSHtspddpsfASQNQVYNDIGKEMLQHAFEG 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVesVDSETVESSHLTNKnRTKTFTFDKVFDPE--------ATQEDVYEETAKPLVESVLEG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    88 YNVCIFAYGQTGAGKSYTMMGKQEegQEGIIPQLCEELFEKINDNNnEEISYSVEVAYMEIYCERVRDLLNP--KNKGNL 165
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDE--QPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPsnKNKRKL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   166 RVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYDSETDLSTeKVSKISL 245
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKLNL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   246 VDLAGSERADSTG-AKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkktDFIPYRDSVLTWLLRENLGGNSRT 324
Cdd:pfam00225  229 VDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS-----------KHIPYRDSKLTRLLQDSLGGNSKT 297
                          330       340
                   ....*....|....*....|....*....
gi 688611584   325 AMVAALSPADINFDETLSTLRYADRAKQI 353
Cdd:pfam00225  298 LMIANISPSSSNYEETLSTLRFASRAKNI 326
Kinesin_assoc pfam16183
Kinesin-associated;
357-593 1.97e-89

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 288.28  E-value: 1.97e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   357 AVINEDPNAKLVRELKDEVSRLKELLRAQGLGDILDIEPMGDdclgsgskcddindvkTLLSSQTEAMLYRRKAPMGCLT 436
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLGDIIDTIAHPT----------------KKRANTPAANASAATAAMAGAS 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   437 ASPSSGSLCSQAGlqSVSSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDG 516
Cdd:pfam16183   65 PSPSLSALSSRAA--SVSSLHERIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDG 142
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688611584   517 GTLgvfspkkfgpdrptslsiedfsvyssnqlfverpcevytdfnGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGI 593
Cdd:pfam16183  143 GTL------------------------------------------GVFSPKKTPHLVNLNEDPLMSECLLYYIKDGI 177
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
1-380 7.51e-83

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 284.71  E-value: 7.51e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    1 MSGASVKVAVRVRPFNSRETGKESKCIIQMQGNSTTILNPKNPKepkTFSFDYSYwshtspdDPSfASQNQVYNDIGKEM 80
Cdd:COG5059    13 LSSRNEKSVSDIKSTIRIIPGELGERLINTSKKSHVSLEKSKEG---TYAFDKVF-------GPS-ATQEDVYEETIKPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   81 LQHAFEGYNVCIFAYGQTGAGKSYTMMGkqEEGQEGIIPQLCEELFEKInDNNNEEISYSVEVAYMEIYCERVRDLLNPK 160
Cdd:COG5059    82 IDSLLLGYNCTVFAYGQTGSGKTYTMSG--TEEEPGIIPLSLKELFSKL-EDLSMTKDFAVSISYLEIYNEKIYDLLSPN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  161 NKGnLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYDSETDLStekv 240
Cdd:COG5059   159 EES-LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET---- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  241 SKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkkTDFIPYRDSVLTWLLRENLGG 320
Cdd:COG5059   234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKK----------SGHIPYRESKLTRLLQDSLGG 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688611584  321 NSRTAMVAALSPADINFDETLSTLRYADRAKQIK-----CNAVINEDPNAKLVREL---KDEVSRLKE 380
Cdd:COG5059   304 NCNTRVICTISPSSNSFEETINTLKFASRAKSIKnkiqvNSSSDSSREIEEIKFDLsedRSEIEILVF 371
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
568-677 1.62e-77

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: 251.49  E-value: 1.62e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  568 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNANGHVIVTLEPCEGSETYVNG 647
Cdd:cd22727     1 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNNNGEVIVTLEPCERSETYVNG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 688611584  648 KRVNSAVQLRSGNRIIMGKNHVFRFNHPEQ 677
Cdd:cd22727    81 KRVVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
PLN03188 PLN03188
kinesin-12 family protein; Provisional
1-379 5.73e-77

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 282.21  E-value: 5.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    1 MSGASVKVAVRVRPFNSretGKESKCIIQ-MQGNSTTILNpknpkepKTFSFDysywshtSPDDPSfASQNQVYNDIGKE 79
Cdd:PLN03188   95 VSDSGVKVIVRMKPLNK---GEEGEMIVQkMSNDSLTING-------QTFTFD-------SIADPE-STQEDIFQLVGAP 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   80 MLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQ----EEG----QEGIIPQLCEELFEKINDNN----NEEISYSVEVAYME 147
Cdd:PLN03188  157 LVENCLAGFNSSVFAYGQTGSGKTYTMWGPAngllEEHlsgdQQGLTPRVFERLFARINEEQikhaDRQLKYQCRCSFLE 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  148 IYCERVRDLLNPKNKgNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQR 227
Cdd:PLN03188  237 IYNEQITDLLDPSQK-NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESR 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  228 KYDSETDLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKkkkktdfIPYRD 307
Cdd:PLN03188  316 CKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRH-------IPYRD 388
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688611584  308 SVLTWLLRENLGGNSRTAMVAALSPADINFDETLSTLRYADRAKQIKCNAVINE----DPN--AKLVRELKDEVSRLK 379
Cdd:PLN03188  389 SRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
1370-1526 9.89e-60

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: 463599  Cd Length: 149  Bit Score: 202.04  E-value: 9.89e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  1370 EYIPAVVDHTGGLPcHGTYLLHQGIQRRITVTLIHEKGSELHWKDVRELVVGRIRN---KPEVDDSAADAVLSLNIISAK 1446
Cdd:pfam12473    1 EYVPVPVDQRSELD-PGTFQLHQGLQRRIVITLTHSSGDELPWERVRNVRVGDVRLldmKGRVPDSDSTPDVSLKLLSKP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  1447 NLKSSHNSsslcidsdisRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAIITKDICMVFYSRDA 1526
Cdd:pfam12473   80 VVRFNADG----------TSSYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
PH_KIFIA_KIFIB cd01233
KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA ...
1805-1907 1.32e-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: 185.49  E-value: 1.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584 1805 RPGSVVSKKGILNFMEPRSNTWVKHFVVVRRPYVFIYNNDKDPVERGVLNLSTAQVEYSEDQQAMLKTPHTFAMCTKHRG 1884
Cdd:cd01233     1 PKSPVVSKRGYLLFLEDATDGWVRRWVVLRRPYLHIYSSEKDGDERGVINLSTARVEYSPDQEALLGRPNVFAVYTPTNS 80
                          90       100
                  ....*....|....*....|...
gi 688611584 1885 ILLQANNDKDMNDWLYAFNPLLA 1907
Cdd:cd01233    81 YLLQARSEKEMQDWLYAIDPLLA 103
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
886-934 1.12e-13

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


Pssm-ID: 463574  Cd Length: 43  Bit Score: 66.86  E-value: 1.12e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 688611584   886 LKQRLDQMREMYDRAGEMASSNQGDDGEgaltgsDPFYDRFHWFKLVGS 934
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR------DPFYEPPENHNLIGV 43
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1810-1903 2.18e-11

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 [Multi-domain]  Cd Length: 102  Bit Score: 62.18  E-value: 2.18e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   1810 VSKKGILNFMEPRSN-TWVKHFVVVRRPYVFIYNNDK---DPVERGVLNLSTAQVEYSEDQQAMlKTPHTFAMCTKHRG- 1884
Cdd:smart00233    1 VIKEGWLYKKSGGGKkSWKKRYFVLFNSTLLYYKSKKdkkSYKPKGSIDLSGCTVREAPDPDSS-KKPHCFEIKTSDRKt 79
                            90
                    ....*....|....*....
gi 688611584   1885 ILLQANNDKDMNDWLYAFN 1903
Cdd:smart00233   80 LLLQAESEEEREKWVEALR 98
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1810-1903 1.79e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 59.88  E-value: 1.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  1810 VSKKGILNFMEP-RSNTWVKHFVVVRRPYVFIYNNDKDPVE---RGVLNLSTAQVEYSEDQqAMLKTPHTFAMCTKH--- 1882
Cdd:pfam00169    1 VVKEGWLLKKGGgKKKSWKKRYFVLFDGSLLYYKDDKSGKSkepKGSISLSGCEVVEVVAS-DSPKRKFCFELRTGErtg 79
                           90       100
                   ....*....|....*....|..
gi 688611584  1883 -RGILLQANNDKDMNDWLYAFN 1903
Cdd:pfam00169   80 kRTYLLQAESEEERKDWIKAIQ 101
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
589-672 2.21e-07

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 50.73  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  589 IKDGITRVGQADaerRQDIVLSGAHIKEEHCIFRseRNANGHVIVTLepceGSE--TYVNGKRVNSAVQLRSGNRIIMGK 666
Cdd:COG1716    18 LDGGPLTIGRAP---DNDIVLDDPTVSRRHARIR--RDGGGWVLEDL----GSTngTFVNGQRVTEPAPLRDGDVIRLGK 88

                  ....*.
gi 688611584  667 nHVFRF 672
Cdd:COG1716    89 -TELRF 93
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
594-662 2.84e-06

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 46.42  E-value: 2.84e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688611584   594 TRVGQADaerRQDIVLSGAHIKEEHCIFRSERNANghviVTLEPCeGSE--TYVNGKRVNS-AVQLRSGNRI 662
Cdd:pfam00498    1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYDGGGR----FYLEDL-GSTngTFVNGQRLGPePVRLKDGDVI 64
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
677-751 7.37e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.72  E-value: 7.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688611584  677 QARAEREKTPSAEtpvepvdwtfAQRELLEKQGIDMKQEMEKR----LTEMEILYKKEKEEADQLLEQQRLVYESKLQE 751
Cdd:cd16269   199 EIEAERAKAEAAE----------QERKLLEEQQRELEQKLEDQersyEEHLRQLKEKMEEERENLLKEQERALESKLKE 267
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
700-757 2.37e-03

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 39.87  E-value: 2.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688611584  700 AQRELLEKQGIDMK-QEMEKRLTEME--------------ILYKKEKEEADQLLEQQRLVYESKLQELQKQVE 757
Cdd:COG1382    23 LQAVAAQKQQVESElKEAEKALEELEklpddaevyksvgnLLVKTDKEEVIKELEEKKETLELRLKTLEKQEE 95
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
996-1018 3.84e-03

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


Pssm-ID: 463574  Cd Length: 43  Bit Score: 36.81  E-value: 3.84e-03
                           10        20
                   ....*....|....*....|...
gi 688611584   996 SDIFSDGQDPFYDRSPWFILVGR 1018
Cdd:pfam12423   21 SQHFEVDRDPFYEPPENHNLIGV 43
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
4-360 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: 666.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    4 ASVKVAVRVRPFNSRETGKESKCIIQMQGNSTTILNPKN--------PKEPKTFSFDYSYWSHTSPDdPSFASQNQVYND 75
Cdd:cd01365     1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQadknnkatREVPKSFSFDYSYWSHDSED-PNYASQEQVYED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   76 IGKEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEegQEGIIPQLCEELFEKINDNNNEEISYSVEVAYMEIYCERVRD 155
Cdd:cd01365    80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQE--QPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  156 LLNPK---NKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYDSE 232
Cdd:cd01365   158 LLNPKpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  233 TDLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskSKKKKKTDFIPYRDSVLTW 312
Cdd:cd01365   238 TNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSS----GKSKKKSSFIPYRDSVLTW 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 688611584  313 LLRENLGGNSRTAMVAALSPADINFDETLSTLRYADRAKQIKCNAVIN 360
Cdd:cd01365   314 LLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
5-360 2.10e-152

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: 472.44  E-value: 2.10e-152
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584      5 SVKVAVRVRPFNSRETGKESKCIIQMQGN---STTILNPKNPKEPKTFSFDYSYwshtspddPSFASQNQVYNDIGKEML 81
Cdd:smart00129    1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKvgkTLTVRSPKNRQGEKKFTFDKVF--------DATASQEDVFEETAAPLV 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584     82 QHAFEGYNVCIFAYGQTGAGKSYTMMGKQEEgqEGIIPQLCEELFEKInDNNNEEISYSVEVAYMEIYCERVRDLLNPkN 161
Cdd:smart00129   73 DSVLEGYNATIFAYGQTGSGKTYTMIGTPDS--PGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP-S 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    162 KGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYDSETDlsTEKVS 241
Cdd:smart00129  149 SKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSG--SGKAS 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    242 KISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkkTDFIPYRDSVLTWLLRENLGGN 321
Cdd:smart00129  227 KLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK----------SRHIPYRDSKLTRLLQDSLGGN 296
                           330       340       350
                    ....*....|....*....|....*....|....*....
gi 688611584    322 SRTAMVAALSPADINFDETLSTLRYADRAKQIKCNAVIN 360
Cdd:smart00129  297 SKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
5-351 7.29e-148

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: 459.80  E-value: 7.29e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    5 SVKVAVRVRPFNSREtGKESKCIIQMQGNSTTILNPK--NPKEPKTFSFDYSYWSHtspddpsfASQNQVYNDIGKEMLQ 82
Cdd:cd00106     1 NVRVAVRVRPLNGRE-ARSAKSVISVDGGKSVVLDPPknRVAPPKTFAFDAVFDST--------STQEEVYEGTAKPLVD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   83 HAFEGYNVCIFAYGQTGAGKSYTMMGKQEEgQEGIIPQLCEELFEKINDNNNEEISYSVEVAYMEIYCERVRDLLNPKNK 162
Cdd:cd00106    72 SALEGYNGTIFAYGQTGSGKTYTMLGPDPE-QRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLLSPVPK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  163 GNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKydSETDLSTEKVSK 242
Cdd:cd00106   151 KPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRN--REKSGESVTSSK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  243 ISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkktDFIPYRDSVLTWLLRENLGGNS 322
Cdd:cd00106   229 LNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN-----------KHIPYRDSKLTRLLQDSLGGNS 297
                         330       340
                  ....*....|....*....|....*....
gi 688611584  323 RTAMVAALSPADINFDETLSTLRYADRAK 351
Cdd:cd00106   298 KTIMIACISPSSENFEETLSTLRFASRAK 326
Kinesin pfam00225
Kinesin motor domain;
11-353 1.58e-143

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 447.79  E-value: 1.58e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    11 RVRPFNSRETGKESKCIIQM--QGNSTTILNPKNPK-EPKTFSFDYSYWSHtspddpsfASQNQVYNDIGKEMLQHAFEG 87
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVesVDSETVESSHLTNKnRTKTFTFDKVFDPE--------ATQEDVYEETAKPLVESVLEG 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    88 YNVCIFAYGQTGAGKSYTMMGKQEegQEGIIPQLCEELFEKINDNNnEEISYSVEVAYMEIYCERVRDLLNP--KNKGNL 165
Cdd:pfam00225   73 YNVTIFAYGQTGSGKTYTMEGSDE--QPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPsnKNKRKL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   166 RVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYDSETDLSTeKVSKISL 245
Cdd:pfam00225  150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKLNL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   246 VDLAGSERADSTG-AKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkktDFIPYRDSVLTWLLRENLGGNSRT 324
Cdd:pfam00225  229 VDLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALADKKS-----------KHIPYRDSKLTRLLQDSLGGNSKT 297
                          330       340
                   ....*....|....*....|....*....
gi 688611584   325 AMVAALSPADINFDETLSTLRYADRAKQI 353
Cdd:pfam00225  298 LMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
5-353 2.36e-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: 366.40  E-value: 2.36e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    5 SVKVAVRVRPFNSRETGKESKCIIQM--QGNSTTILNPKNP--KEPKTFSFDYSYwshtspdDPSfASQNQVYNDIGKEM 80
Cdd:cd01371     2 NVKVVVRCRPLNGKEKAAGALQIVDVdeKRGQVSVRNPKATanEPPKTFTFDAVF-------DPN-SKQLDVYDETARPL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   81 LQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEEGQE-GIIPQLCEELFEKINDNNNEEiSYSVEVAYMEIYCERVRDLLNP 159
Cdd:cd01371    74 VDSVLEGYNGTIFAYGQTGTGKTYTMEGKREDPELrGIIPNSFAHIFGHIARSQNNQ-QFLVRVSYLEIYNEEIRDLLGK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  160 KNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFtQRKYDSETDLSTEK 239
Cdd:cd01371   153 DQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI-ECSEKGEDGENHIR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  240 VSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALaeVDNctskskkkkKTDFIPYRDSVLTWLLRENLG 319
Cdd:cd01371   232 VGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISAL--VDG---------KSTHIPYRDSKLTRLLQDSLG 300
                         330       340       350
                  ....*....|....*....|....*....|....
gi 688611584  320 GNSRTAMVAALSPADINFDETLSTLRYADRAKQI 353
Cdd:cd01371   301 GNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
5-353 2.94e-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: 2.94e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    5 SVKVAVRVRPFNSRETGKESKCIIQMQGNSTTILNPKNpkEPKTFSFDYSYwshtspdDPSfASQNQVYNDIGKEMLQHA 84
Cdd:cd01369     3 NIKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVIATSE--TGKTFSFDRVF-------DPN-TTQEDVYNFAAKPIVDDV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   85 FEGYNVCIFAYGQTGAGKSYTMMG-KQEEGQEGIIPQLCEELFEKINdNNNEEISYSVEVAYMEIYCERVRDLLNPKNKg 163
Cdd:cd01369    73 LNGYNGTIFAYGQTSSGKTYTMEGkLGDPESMGIIPRIVQDIFETIY-SMDENLEFHVKVSYFEIYMEKIRDLLDVSKT- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  164 NLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRkyDSETDlsTEKVSKI 243
Cdd:cd01369   151 NLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE--NVETE--KKKSGKL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  244 SLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEvdnctskskkkKKTDFIPYRDSVLTWLLRENLGGNSR 323
Cdd:cd01369   227 YLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----------GKKTHIPYRDSKLTRILQDSLGGNSR 295
                         330       340       350
                  ....*....|....*....|....*....|
gi 688611584  324 TAMVAALSPADINFDETLSTLRYADRAKQI 353
Cdd:cd01369   296 TTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
5-354 3.81e-105

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: 340.46  E-value: 3.81e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    5 SVKVAVRVRPFNSRETGKESKCIIQMQGNSTTILNPKNpkepKTFSFDYSYwshtspdDPSfASQNQVYNDIGKEMLQHA 84
Cdd:cd01372     2 SVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTD----KSFTFDYVF-------DPS-TEQEEVYNTCVAPLVDGL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   85 FEGYNVCIFAYGQTGAGKSYTMMG----KQEEGQEGIIPQLCEELFEKInDNNNEEISYSVEVAYMEIYCERVRDLLNPK 160
Cdd:cd01372    70 FEGYNATVLAYGQTGSGKTYTMGTaytaEEDEEQVGIIPRAIQHIFKKI-EKKKDTFEFQLKVSFLEIYNEEIRDLLDPE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  161 N--KGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYDSETDLSTE 238
Cdd:cd01372   149 TdkKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  239 K------VSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEvdnctskskKKKKTDFIPYRDSVLTW 312
Cdd:cd01372   229 DdknstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGD---------ESKKGAHVPYRDSKLTR 299
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 688611584  313 LLRENLGGNSRTAMVAALSPADINFDETLSTLRYADRAKQIK 354
Cdd:cd01372   300 LLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
11-355 1.35e-103

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: 335.33  E-value: 1.35e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   11 RVRPFNSRETGKESKCI-IQMQGNSTTILNPKNPKEpKTFSFDYSYwshtspdDPSfASQNQVYNDIgKEMLQHAFEGYN 89
Cdd:cd01366     9 RVRPLLPSEENEDTSHItFPDEDGQTIELTSIGAKQ-KEFSFDKVF-------DPE-ASQEDVFEEV-SPLVQSALDGYN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   90 VCIFAYGQTGAGKSYTMMGKQEegQEGIIPQLCEELFEKINDNNNEEISYSVEVAYMEIYCERVRDLLNPKNKGNLR--V 167
Cdd:cd01366    79 VCIFAYGQTGSGKTYTMEGPPE--SPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLLAPGNAPQKKleI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  168 REHPLLGP-YVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFtqRKYDSETDLSTekVSKISLV 246
Cdd:cd01366   157 RHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--SGRNLQTGEIS--VGKLNLV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  247 DLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAevdnctskskkkKKTDFIPYRDSVLTWLLRENLGGNSRTAM 326
Cdd:cd01366   233 DLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------------QKQSHIPYRNSKLTYLLQDSLGGNSKTLM 300
                         330       340
                  ....*....|....*....|....*....
gi 688611584  327 VAALSPADINFDETLSTLRYADRAKQIKC 355
Cdd:cd01366   301 FVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
5-353 2.82e-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: 334.30  E-value: 2.82e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    5 SVKVAVRVRPFNSRETGKESKCIIQMQGNstTILNPKNPkePKTFSFDYSYWSHtspddpsfaSQN-QVYNDIGKEMLQH 83
Cdd:cd01374     1 KITVTVRVRPLNSREIGINEQVAWEIDND--TIYLVEPP--STSFTFDHVFGGD---------STNrEVYELIAKPVVKS 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   84 AFEGYNVCIFAYGQTGAGKSYTMMGKQEEgqEGIIPQLCEELFEKINDNNNEEisYSVEVAYMEIYCERVRDLLNPKNKg 163
Cdd:cd01374    68 ALEGYNGTIFAYGQTSSGKTFTMSGDEDE--PGIIPLAIRDIFSKIQDTPDRE--FLLRVSYLEIYNEKINDLLSPTSQ- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  164 NLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFtQRKYDSETDLSTEKVSKI 243
Cdd:cd01374   143 NLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI-ESSERGELEEGTVRVSTL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  244 SLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEvdnctskskkKKKTDFIPYRDSVLTWLLRENLGGNSR 323
Cdd:cd01374   222 NLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE----------GKVGGHIPYRDSKLTRILQPSLGGNSR 291
                         330       340       350
                  ....*....|....*....|....*....|
gi 688611584  324 TAMVAALSPADINFDETLSTLRYADRAKQI 353
Cdd:cd01374   292 TAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
5-353 1.71e-97

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 318.52  E-value: 1.71e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    5 SVKVAVRVRPFNSRETGKESKCIIQMQGNSTTILNP------------------KNPKEPKTFSFDYSYwshtspdDPSf 66
Cdd:cd01370     1 SLTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPkdeedgffhggsnnrdrrKRRNKELKYVFDRVF-------DET- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   67 ASQNQVYNDIGKEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEEgqEGIIPQLCEELFEKINDNNNEEIsYSVEVAYM 146
Cdd:cd01370    73 STQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQE--PGLMVLTMKELFKRIESLKDEKE-FEVSMSYL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  147 EIYCERVRDLLNPKNKGnLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQ 226
Cdd:cd01370   150 EIYNETIRDLLNPSSGP-LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQ 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  227 RkydSETDLSTEKVS--KISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEvdnctskskKKKKTDFIP 304
Cdd:cd01370   229 Q---DKTASINQQVRqgKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD---------PGKKNKHIP 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 688611584  305 YRDSVLTWLLRENLGGNSRTAMVAALSPADINFDETLSTLRYADRAKQI 353
Cdd:cd01370   297 YRDSKLTRLLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
6-362 2.50e-96

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: 315.22  E-value: 2.50e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    6 VKVAVRVRPFNSRETGKE-SKCIIQMqgNSTTILNPKNPkePKTFSFDYSYWSHTSPDDpsfasqnqVYNDIGKEMLQHA 84
Cdd:cd01373     3 VKVFVRIRPPAEREGDGEyGQCLKKL--SSDTLVLHSKP--PKTFTFDHVADSNTNQES--------VFQSVGKPIVESC 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   85 FEGYNVCIFAYGQTGAGKSYTMMGKQEEGQE------GIIPQLCEELFEKIN---DNNNEEISYSVEVAYMEIYCERVRD 155
Cdd:cd01373    71 LSGYNGTIFAYGQTGSGKTYTMWGPSESDNEsphglrGVIPRIFEYLFSLIQrekEKAGEGKSFLCKCSFLEIYNEQIYD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  156 LLNPKNKgNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTivFTQRKYDSETDL 235
Cdd:cd01373   151 LLDPASR-NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFT--CTIESWEKKACF 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  236 STEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkKKTDFIPYRDSVLTWLLR 315
Cdd:cd01373   228 VNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAH--------GKQRHVCYRDSKLTFLLR 299
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 688611584  316 ENLGGNSRTAMVAALSPADINFDETLSTLRYADRAKQIKCNAVINED 362
Cdd:cd01373   300 DSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
3-362 1.57e-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: 1.57e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    3 GASVKVAVRVRPFNSRETGKESKCIIQMQGNS------TTILNPKNPKepKTFSFDYSYwshtspddPSFASQNQVYNDI 76
Cdd:cd01364     1 GKNIQVVVRCRPFNLRERKASSHSVVEVDPVRkevsvrTGGLADKSST--KTYTFDMVF--------GPEAKQIDVYRSV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   77 GKEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEEGQE---------GIIPQLCEELFEKINDNNNEeisYSVEVAYME 147
Cdd:cd01364    71 VCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDRSPNEEytweldplaGIIPRTLHQLFEKLEDNGTE---YSVKVSYLE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  148 IYCERVRDLLNPKNKGNLRVREHPLL----GPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIV 223
Cdd:cd01364   148 IYNEELFDLLSPSSDVSERLRMFDDPrnkrGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSIT 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  224 FTQRkydsETDLSTE---KVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEvdnctskskkkkKT 300
Cdd:cd01364   228 IHIK----ETTIDGEelvKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------------RA 291
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688611584  301 DFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINFDETLSTLRYADRAKQIKCNAVINED 362
Cdd:cd01364   292 PHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
Kinesin_assoc pfam16183
Kinesin-associated;
357-593 1.97e-89

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 288.28  E-value: 1.97e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   357 AVINEDPNAKLVRELKDEVSRLKELLRAQGLGDILDIEPMGDdclgsgskcddindvkTLLSSQTEAMLYRRKAPMGCLT 436
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLYAQGLGDIIDTIAHPT----------------KKRANTPAANASAATAAMAGAS 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   437 ASPSSGSLCSQAGlqSVSSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDG 516
Cdd:pfam16183   65 PSPSLSALSSRAA--SVSSLHERIMFTPGSEEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDG 142
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688611584   517 GTLgvfspkkfgpdrptslsiedfsvyssnqlfverpcevytdfnGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGI 593
Cdd:pfam16183  143 GTL------------------------------------------GVFSPKKTPHLVNLNEDPLMSECLLYYIKDGI 177
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
1-380 7.51e-83

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 284.71  E-value: 7.51e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    1 MSGASVKVAVRVRPFNSRETGKESKCIIQMQGNSTTILNPKNPKepkTFSFDYSYwshtspdDPSfASQNQVYNDIGKEM 80
Cdd:COG5059    13 LSSRNEKSVSDIKSTIRIIPGELGERLINTSKKSHVSLEKSKEG---TYAFDKVF-------GPS-ATQEDVYEETIKPL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   81 LQHAFEGYNVCIFAYGQTGAGKSYTMMGkqEEGQEGIIPQLCEELFEKInDNNNEEISYSVEVAYMEIYCERVRDLLNPK 160
Cdd:COG5059    82 IDSLLLGYNCTVFAYGQTGSGKTYTMSG--TEEEPGIIPLSLKELFSKL-EDLSMTKDFAVSISYLEIYNEKIYDLLSPN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  161 NKGnLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYDSETDLStekv 240
Cdd:COG5059   159 EES-LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSET---- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  241 SKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkkTDFIPYRDSVLTWLLRENLGG 320
Cdd:COG5059   234 SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKK----------SGHIPYRESKLTRLLQDSLGG 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688611584  321 NSRTAMVAALSPADINFDETLSTLRYADRAKQIK-----CNAVINEDPNAKLVREL---KDEVSRLKE 380
Cdd:COG5059   304 NCNTRVICTISPSSNSFEETINTLKFASRAKSIKnkiqvNSSSDSSREIEEIKFDLsedRSEIEILVF 371
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
568-677 1.62e-77

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: 251.49  E-value: 1.62e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  568 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNANGHVIVTLEPCEGSETYVNG 647
Cdd:cd22727     1 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNNNGEVIVTLEPCERSETYVNG 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 688611584  648 KRVNSAVQLRSGNRIIMGKNHVFRFNHPEQ 677
Cdd:cd22727    81 KRVVQPVQLRSGNRIIMGKNHVFRFNHPEQ 110
PLN03188 PLN03188
kinesin-12 family protein; Provisional
1-379 5.73e-77

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 282.21  E-value: 5.73e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    1 MSGASVKVAVRVRPFNSretGKESKCIIQ-MQGNSTTILNpknpkepKTFSFDysywshtSPDDPSfASQNQVYNDIGKE 79
Cdd:PLN03188   95 VSDSGVKVIVRMKPLNK---GEEGEMIVQkMSNDSLTING-------QTFTFD-------SIADPE-STQEDIFQLVGAP 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   80 MLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQ----EEG----QEGIIPQLCEELFEKINDNN----NEEISYSVEVAYME 147
Cdd:PLN03188  157 LVENCLAGFNSSVFAYGQTGSGKTYTMWGPAngllEEHlsgdQQGLTPRVFERLFARINEEQikhaDRQLKYQCRCSFLE 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  148 IYCERVRDLLNPKNKgNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQR 227
Cdd:PLN03188  237 IYNEQITDLLDPSQK-NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESR 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  228 KYDSETDLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKkkkktdfIPYRD 307
Cdd:PLN03188  316 CKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRH-------IPYRD 388
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688611584  308 SVLTWLLRENLGGNSRTAMVAALSPADINFDETLSTLRYADRAKQIKCNAVINE----DPN--AKLVRELKDEVSRLK 379
Cdd:PLN03188  389 SRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
6-351 9.90e-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: 244.23  E-value: 9.90e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    6 VKVAVRVRPFNSRETGKESKCIIQMQGNSTTILNPknPKEPKTFSFD---------YSYWSHTSPDdpsfASQNQVYNDI 76
Cdd:cd01368     3 VKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHP--PKGSAANKSErnggqketkFSFSKVFGPN----TTQKEFFQGT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   77 GKEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEEGqeGIIPQLCEELFEKINDnnneeisYSVEVAYMEIYCERVRDL 156
Cdd:cd01368    77 ALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDG--GILPRSLDVIFNSIGG-------YSVFVSYIEIYNEYIYDL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  157 LNP------KNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYD 230
Cdd:cd01368   148 LEPspssptKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGD 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  231 SETDLSTEK----VSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEvdnctskSKKKKKTDFIPYR 306
Cdd:cd01368   228 SDGDVDQDKdqitVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRE-------NQLQGTNKMVPFR 300
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 688611584  307 DSVLTWLLRENLGGNSRTAMVAALSPADINFDETLSTLRYADRAK 351
Cdd:cd01368   301 DSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
6-351 2.28e-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: 2.28e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    6 VKVAVRVRPFNSRETGKESK-CIIQMQGNSTTILNPKNPKEPKTFSFDYSYWSHtspddpsfASQNQVYNDIGKEMLQHA 84
Cdd:cd01376     2 VRVAVRVRPFVDGTAGASDPsCVSGIDSCSVELADPRNHGETLKYQFDAFYGEE--------STQEDIYAREVQPIVPHL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   85 FEGYNVCIFAYGQTGAGKSYTMMGkqEEGQEGIIPQLCEELFEKindNNNEEISYSVEVAYMEIYCERVRDLLNPKNKgN 164
Cdd:cd01376    74 LEGQNATVFAYGSTGAGKTFTMLG--SPEQPGLMPLTVMDLLQM---TRKEAWALSFTMSYLEIYQEKILDLLEPASK-E 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  165 LRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKYDSETDLSTekvSKIS 244
Cdd:cd01376   148 LVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRT---GKLN 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  245 LVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCtskskkkkktdfIPYRDSVLTWLLRENLGGNSRT 324
Cdd:cd01376   225 LIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR------------IPYRDSKLTRLLQDSLGGGSRC 292
                         330       340
                  ....*....|....*....|....*..
gi 688611584  325 AMVAALSPADINFDETLSTLRYADRAK 351
Cdd:cd01376   293 IMVANIAPERTFYQDTLSTLNFAARSR 319
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
569-683 6.28e-69

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: 227.12  E-value: 6.28e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  569 TPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNANGHVIVTLEPCEGSETYVNGK 648
Cdd:cd22726     1 TPHLVNLNEDPLMSECLLYYIKDGITRVGREDAERRQDIVLSGHFIKEEHCIFRSDTRSGGEAVVTLEPCEGADTYVNGK 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 688611584  649 RVNSAVQLRSGNRIIMGKNHVFRFNHPEQARAERE 683
Cdd:cd22726    81 KVTEPSILRSGNRIIMGKSHVFRFNHPEQARQERE 115
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
6-351 8.56e-69

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: 235.27  E-value: 8.56e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    6 VKVAVRVRPFNSRETGKESKCIIQMQGNSTTILNPKNPK-------EPKTFSFDYSYwshtspDDPSfaSQNQVYNDIGK 78
Cdd:cd01367     2 IKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKvdltkyiENHTFRFDYVF------DESS--SNETVYRSTVK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   79 EMLQHAFEGYNVCIFAYGQTGAGKSYTMMGK--QEEGQEGIIPQLCEELFEKINDNNNEEiSYSVEVAYMEIYCERVRDL 156
Cdd:cd01367    74 PLVPHIFEGGKATCFAYGQTGSGKTYTMGGDfsGQEESKGIYALAARDVFRLLNKLPYKD-NLGVTVSFFEIYGGKVFDL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  157 LNPKNKgnLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRKydsetdlS 236
Cdd:cd01367   153 LNRKKR--VRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRG-------T 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  237 TEKVSKISLVDLAGSER-ADSTGAKGTRLKEGANINKSLTTLGKVISALAevdnctskskkkKKTDFIPYRDSVLTWLLR 315
Cdd:cd01367   224 NKLHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALG------------QNKAHIPFRGSKLTQVLK 291
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 688611584  316 ENL-GGNSRTAMVAALSPADINFDETLSTLRYADRAK 351
Cdd:cd01367   292 DSFiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
5-351 2.55e-66

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 228.23  E-value: 2.55e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    5 SVKVAVRVRPfnsreTGKESKCIIQM--QGNSTTILNPK--------NPKEPKTFSFDYSYwshtspDDpsfASQNQVYN 74
Cdd:cd01375     1 KVQAFVRVRP-----TDDFAHEMIKYgeDGKSISIHLKKdlrrgvvnNQQEDWSFKFDGVL------HN---ASQELVYE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   75 DIGKEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEE-GQEGIIPQLCEELFEKINDNNNEeiSYSVEVAYMEIYCERV 153
Cdd:cd01375    67 TVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENyKHRGIIPRALQQVFRMIEERPTK--AYTVHVSYLEIYNEQL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  154 RDLLNPKNKGN-----LRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQRK 228
Cdd:cd01375   145 YDLLSTLPYVGpsvtpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHS 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  229 ydseTDLSTEKV--SKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNctskskkkkktDFIPYR 306
Cdd:cd01375   225 ----RTLSSEKYitSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDR-----------THVPFR 289
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 688611584  307 DSVLTWLLRENLGGNSRTAMVAALSPADINFDETLSTLRYADRAK 351
Cdd:cd01375   290 QSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
569-674 1.31e-61

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: 205.55  E-value: 1.31e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  569 TPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNanghvIVTLEPCEGSETYVNGK 648
Cdd:cd22705     1 TPHLVNLNEDPLMSECLLYYIKPGITRVGRADADVPQDIQLSGTHILEEHCTFENEDG-----VVTLEPCEGALTYVNGK 75
                          90       100
                  ....*....|....*....|....*.
gi 688611584  649 RVNSAVQLRSGNRIIMGKNHVFRFNH 674
Cdd:cd22705    76 RVTEPTRLKTGSRVILGKNHVFRFNH 101
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
1370-1526 9.89e-60

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: 463599  Cd Length: 149  Bit Score: 202.04  E-value: 9.89e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  1370 EYIPAVVDHTGGLPcHGTYLLHQGIQRRITVTLIHEKGSELHWKDVRELVVGRIRN---KPEVDDSAADAVLSLNIISAK 1446
Cdd:pfam12473    1 EYVPVPVDQRSELD-PGTFQLHQGLQRRIVITLTHSSGDELPWERVRNVRVGDVRLldmKGRVPDSDSTPDVSLKLLSKP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  1447 NLKSSHNSsslcidsdisRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAIITKDICMVFYSRDA 1526
Cdd:pfam12473   80 VVRFNADG----------TSSYTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVSEKCAEPVRFSMDTAVQIYPRDE 149
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
569-674 1.73e-55

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: 188.16  E-value: 1.73e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  569 TPHLVNLNEDPLMSECLLYYIKDGITRVGQADAerrqDIVLSGAHIKEEHCIFRSERNANGHVIVTLEPCEGSETYVNGK 648
Cdd:cd22728     1 TPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDV----DIKLSGQFIREQHCLFRSIPNPSGEVVVTLEPCEGAETYVNGK 76
                          90       100
                  ....*....|....*....|....*.
gi 688611584  649 RVNSAVQLRSGNRIIMGKNHVFRFNH 674
Cdd:cd22728    77 QVTEPLVLKSGNRIVMGKNHVFRFNH 102
PH_KIFIA_KIFIB cd01233
KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA ...
1805-1907 1.32e-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: 185.49  E-value: 1.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584 1805 RPGSVVSKKGILNFMEPRSNTWVKHFVVVRRPYVFIYNNDKDPVERGVLNLSTAQVEYSEDQQAMLKTPHTFAMCTKHRG 1884
Cdd:cd01233     1 PKSPVVSKRGYLLFLEDATDGWVRRWVVLRRPYLHIYSSEKDGDERGVINLSTARVEYSPDQEALLGRPNVFAVYTPTNS 80
                          90       100
                  ....*....|....*....|...
gi 688611584 1885 ILLQANNDKDMNDWLYAFNPLLA 1907
Cdd:cd01233    81 YLLQARSEKEMQDWLYAIDPLLA 103
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
8-283 1.22e-36

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: 136.71  E-value: 1.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584    8 VAVRVRPFNSRETGKESKCIIQMQGnsttilnpKNPKEpktfsfdysywshtspddpsfaSQNQVYNDIGkEMLQHAFEG 87
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKIIVFYRG--------FRRSE----------------------SQPHVFAIAD-PAYQSMLDG 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   88 YNV-CIFAYGQTGAGKSYTMMgkqeegqeGIIPQLCEELFEKINDNNNEEISYsvevaymeiycervrdllnpknkgnlr 166
Cdd:cd01363    50 YNNqSIFAYGESGAGKTETMK--------GVIPYLASVAFNGINKGETEGWVY--------------------------- 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  167 vrehpllgpyvedLSKLAVTSYTDIADLMDAGNKARTvAATNMNETSSRSHAVFTIVftqrkydsetdlstekvskislV 246
Cdd:cd01363    95 -------------LTEITVTLEDQILQANPILEAFGN-AKTTRNENSSRFGKFIEIL----------------------L 138
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 688611584  247 DLAGSERadstgakgtrlkeganINKSLTTLGKVISA 283
Cdd:cd01363   139 DIAGFEI----------------INESLNTLMNVLRA 159
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
568-675 1.30e-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: 134.32  E-value: 1.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  568 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNanghvIVTLEPCEGSETYVNG 647
Cdd:cd22707     6 KLPNLVNLNEDPQLSEMLLYMLKEGQTRVGRSKASSSHDIQLSGALIADDHCTIENNGG-----KVTIIPVGDAETYVNG 80
                          90       100
                  ....*....|....*....|....*...
gi 688611584  648 KRVNSAVQLRSGNRIIMGKNHVFRFNHP 675
Cdd:cd22707    81 ELISEPTVLHHGDRVILGGDHYFRFNHP 108
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
570-675 3.24e-35

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: 130.03  E-value: 3.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  570 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrseRNANGHviVTLEPC-EGSETYVNGK 648
Cdd:cd22709     1 PHLLNLNEDPQLSGVIVHFLQEGETTIGRADAEPEPDIVLSGLSIQKQHAVI---TNTDGK--VTIEPVsPGAKVIVNGV 75
                          90       100
                  ....*....|....*....|....*..
gi 688611584  649 RVNSAVQLRSGNRIIMGKNHVFRFNHP 675
Cdd:cd22709    76 PVTGETELHHLDRVILGSNHLYVFVGP 102
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
568-675 2.38e-33

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: 125.08  E-value: 2.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  568 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNAnghviVTLEPCEGSETYVNG 647
Cdd:cd22708     7 ELPHLIGIDDDLLSTGVVLYHLKEGKTRIGREDAPQEQDIVLDGEDIEAEHCIIENVGGV-----VTLHPLPGALCAVNG 81
                          90       100
                  ....*....|....*....|....*...
gi 688611584  648 KRVNSAVQLRSGNRIIMGKNHVFRFNHP 675
Cdd:cd22708    82 QVITQPTRLTQGDVILLGKTNMFRFNHP 109
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
572-675 4.54e-32

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: 121.25  E-value: 4.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  572 LVNLNEDPLMSECLLYYIKDgITRVGQADAERRQDIVLSGAHIKEEHCIFRSErnaNGHVIVTlePCEGSETYVNGKRVN 651
Cdd:cd22706     4 LVNLNADPSLNELLVYYLKE-HTLIGRSDAPTQQDIQLSGLGIQPEHCIITIE---NEDVYLT--PLEGARTCVNGSIVT 77
                          90       100
                  ....*....|....*....|....
gi 688611584  652 SAVQLRSGNRIIMGKNHVFRFNHP 675
Cdd:cd22706    78 EKTQLRHGDRILWGNNHFFRLNCP 101
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
562-684 3.47e-30

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: 116.41  E-value: 3.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  562 GVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNanghvIVTLEPCEGS 641
Cdd:cd22731     1 GVTIDSNLPHLIAMDDDILSTGVVLYHLREGTTKIGRSDSEQEQDIVLQGPWIERDHCMIHNECG-----VVTLRPAQGA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 688611584  642 ETYVNGKRVNSAVQLRSGNRIIMGKNHVFRFNHPEQARAEREK 684
Cdd:cd22731    76 QCTVNGREVTESCRLSQGAVIVLGKTHKFRFNHPAEAAILRQR 118
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
562-683 1.41e-26

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: 106.17  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  562 GVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFrseRNANGhvIVTLEPCEGS 641
Cdd:cd22732     1 GVVLDSELPHLIGIDDDLLSTGIILYHLKEGRTYVGRDDATTEQDIVLHGLDLESEHCIF---ENLNG--TVTLIPLNGA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 688611584  642 ETYVNGKRVNSAVQLRSGNRIIMGKNHVFRFNHPEQARAERE 683
Cdd:cd22732    76 QCSVNGVQITEATQLNQGAVILLGRTNMFRFNHPKEAAKLRE 117
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
572-675 5.02e-23

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: 95.37  E-value: 5.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  572 LVNLNEDPLMSECLLYYIKDGiTRVGQADAerrQDIVLSGAHIKEEHCIFrsERNANGHVIVTlePCEGSETYVNGKRVN 651
Cdd:cd22730     4 LVNLNADPALNELLVYYLKEH-TLIGSADS---QDIQLCGMGILPEHCII--DITPEGQVMLT--PQKNTRTFVNGSAVT 75
                          90       100
                  ....*....|....*....|....
gi 688611584  652 SAVQLRSGNRIIMGKNHVFRFNHP 675
Cdd:cd22730    76 SPIQLHHGDRILWGNNHFFRINLP 99
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
572-684 2.50e-22

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: 93.80  E-value: 2.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  572 LVNLNEDPLMSECLLYYIKDGiTRVGqadAERRQDIVLSGAHIKEEHCIFrsERNANGHVIVTlePCEGSETYVNGKRVN 651
Cdd:cd22729     4 LVNLNADPALNELLVYYLKDH-TRVG---ADTSQDIQLFGIGIQPEHCVI--DIAADGDVTLT--PKENARTCVNGTLVC 75
                          90       100       110
                  ....*....|....*....|....*....|...
gi 688611584  652 SAVQLRSGNRIIMGKNHVFRFNHPEQARAEREK 684
Cdd:cd22729    76 SVTQLWHGDRILWGNNHFFRINLPKRKRRDWLK 108
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
5-157 1.43e-17

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 81.11  E-value: 1.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584     5 SVKVAVRVRPFNSREtgkeskciIQMQGNSTTILNPKNPKEPKTFSFDYSYwshtspddPSFASQNQVYNDIgkEML-QH 83
Cdd:pfam16796   21 NIRVFARVRPELLSE--------AQIDYPDETSSDGKIGSKNKSFSFDRVF--------PPESEQEDVFQEI--SQLvQS 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688611584    84 AFEGYNVCIFAYGQTGAGKSYTMmgkqeegqegiIPQLCEELFEKINDNNNeEISYSVEVAYMEIYCERVRDLL 157
Cdd:pfam16796   83 CLDGYNVCIFAYGQTGSGSNDGM-----------IPRAREQIFRFISSLKK-GWKYTIELQFVEIYNESSQDLL 144
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
570-678 1.05e-16

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: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  570 PHLVNLNEDPLMSECLLYYIKDGITRVGQADAErrqDIVLSGAHIKEEHCIFRSERNanghvIVTLEPCeGSETYVNGKR 649
Cdd:cd22713    17 PHLVSLGSGRLSTAVTLLPLPEGKTTIGTAASD---IISLQGPGVEPEHCYIENING-----TVTLYPC-GNLCSVDGLP 87
                          90       100
                  ....*....|....*....|....*....
gi 688611584  650 VNSAVQLRSGNRIIMGKNHVFRFNHPEQA 678
Cdd:cd22713    88 ITEPTRLTQGCMICLGRSNYFRFNHPAEA 116
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
570-675 4.53e-16

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: 75.82  E-value: 4.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  570 PHLVNLNEDPLMSECL-LYYIKDGITRVG--QADAERRQDIVLSGAHIKEEHCIFRserNANGhvIVTLEPCEG-SETYV 645
Cdd:cd22711     2 PYLLELSPDGSDRDKPrRHRLQPNVTEVGseRSPANSGQFIQLFGPDILPRHCVIT---HMEG--VVTVTPASQdAETYV 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 688611584  646 NGKRVNSAVQLRSGNRIIMGKNHVFRFNHP 675
Cdd:cd22711    77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
886-934 1.12e-13

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


Pssm-ID: 463574  Cd Length: 43  Bit Score: 66.86  E-value: 1.12e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 688611584   886 LKQRLDQMREMYDRAGEMASSNQGDDGEgaltgsDPFYDRFHWFKLVGS 934
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR------DPFYEPPENHNLIGV 43
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1810-1903 2.18e-11

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 [Multi-domain]  Cd Length: 102  Bit Score: 62.18  E-value: 2.18e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   1810 VSKKGILNFMEPRSN-TWVKHFVVVRRPYVFIYNNDK---DPVERGVLNLSTAQVEYSEDQQAMlKTPHTFAMCTKHRG- 1884
Cdd:smart00233    1 VIKEGWLYKKSGGGKkSWKKRYFVLFNSTLLYYKSKKdkkSYKPKGSIDLSGCTVREAPDPDSS-KKPHCFEIKTSDRKt 79
                            90
                    ....*....|....*....
gi 688611584   1885 ILLQANNDKDMNDWLYAFN 1903
Cdd:smart00233   80 LLLQAESEEEREKWVEALR 98
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1810-1903 1.79e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 59.88  E-value: 1.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  1810 VSKKGILNFMEP-RSNTWVKHFVVVRRPYVFIYNNDKDPVE---RGVLNLSTAQVEYSEDQqAMLKTPHTFAMCTKH--- 1882
Cdd:pfam00169    1 VVKEGWLLKKGGgKKKSWKKRYFVLFDGSLLYYKDDKSGKSkepKGSISLSGCEVVEVVAS-DSPKRKFCFELRTGErtg 79
                           90       100
                   ....*....|....*....|..
gi 688611584  1883 -RGILLQANNDKDMNDWLYAFN 1903
Cdd:pfam00169   80 kRTYLLQAESEEERKDWIKAIQ 101
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
571-672 1.87e-09

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: 56.51  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  571 HLVNLNEDPLMSEcllYYIKDGITRVGQADAerrQDIVLSGAHIKEEHCIFrsERNANGHVIVTLEPCEGseTYVNGKRV 650
Cdd:cd00060     1 RLIVLDGDGGGRE---FPLTKGVVTIGRSPD---CDIVLDDPSVSRRHARI--EVDGGGVYLEDLGSTNG--TFVNGKRI 70
                          90       100
                  ....*....|....*....|..
gi 688611584  651 NSAVQLRSGNRIIMGkNHVFRF 672
Cdd:cd00060    71 TPPVPLQDGDVIRLG-DTTFRF 91
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
65-284 1.51e-07

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 56.29  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584   65 SFASQNQVYND-IGKEMLQHAFEGynvcIFAYGQTGAGKSYTMMGKQEEGQEGIIpqlcEELFEKINDNNNEEISYSVEV 143
Cdd:COG5059   361 EDRSEIEILVFrEQSQLSQSSLSG----IFAYMQSLKKETETLKSRIDLIMKSII----SGTFERKKLLKEEGWKYKSTL 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  144 AYMEIYCERVRDLLNPKNKGNLRVREHpllgpyVEDLSKLAVTSYT-------DIADLMDAGNKaRTVAATNMNETSSRS 216
Cdd:COG5059   433 QFLRIEIDRLLLLREEELSKKKTKIHK------LNKLRHDLSSLLSsipeetsDRVESEKASKL-RSSASTKLNLRSSRS 505
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688611584  217 HAVFtivftqRKYDSETDLSTEKVSKIsLVDLAGSERaDSTGAKGTRLKEGANINKSLTTLGKVISAL 284
Cdd:COG5059   506 HSKF------RDHLNGSNSSTKELSLN-QVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
569-675 2.21e-07

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: 51.15  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  569 TPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQ-DIVLSGAHIKEEHC-IFRSERNANGHV---------IVTLEP 637
Cdd:cd22712     3 YPYLLTLRGFSPKQDLLVYPLLEQVILVGSRTEGARKvDISLRAPDILPQHCwIRRKPEPLSDDEdsdkesadyRVVLSP 82
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 688611584  638 CEGSETYVNGKRVNSAVQLRSGNRIIMGKNHVFRFNHP 675
Cdd:cd22712    83 LRGAHVTVNGVPVLSETELHPGDLLGIGEHYLFLFKDP 120
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
589-672 2.21e-07

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


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 50.73  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  589 IKDGITRVGQADaerRQDIVLSGAHIKEEHCIFRseRNANGHVIVTLepceGSE--TYVNGKRVNSAVQLRSGNRIIMGK 666
Cdd:COG1716    18 LDGGPLTIGRAP---DNDIVLDDPTVSRRHARIR--RDGGGWVLEDL----GSTngTFVNGQRVTEPAPLRDGDVIRLGK 88

                  ....*.
gi 688611584  667 nHVFRF 672
Cdd:COG1716    89 -TELRF 93
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
568-675 1.45e-06

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: 48.64  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  568 KTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSER--NANGHVIVTLEPCEGSETYV 645
Cdd:cd22733     4 QSPHLLLLQGYNQQHDCLVYLLNREQHTVGQETPSSKPNISLSAPDILPLHCTIRRVRlpKHRSEEKLVLEPIPGAHVSV 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 688611584  646 NGKRVNSAVQLRSGNRIIMGKNHVFRFNHP 675
Cdd:cd22733    84 NFSEVERTTLLRHGDLLSFGAYYLFLFKDP 113
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
594-662 2.84e-06

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


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 46.42  E-value: 2.84e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688611584   594 TRVGQADaerRQDIVLSGAHIKEEHCIFRSERNANghviVTLEPCeGSE--TYVNGKRVNS-AVQLRSGNRI 662
Cdd:pfam00498    1 VTIGRSP---DCDIVLDDPSVSRRHAEIRYDGGGR----FYLEDL-GSTngTFVNGQRLGPePVRLKDGDVI 64
PH_TBC1D2A cd01265
TBC1 domain family member 2A pleckstrin homology (PH) domain; TBC1D2A (also called PARIS-1 ...
1814-1899 1.05e-05

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: 46.16  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584 1814 GILNFMEPRS---NTWVKHFVVV--RRPYVFIYNNDKDPVERGVLNLSTAQVEYSEDQQamlktPHTFAMCTKHRGILLQ 1888
Cdd:cd01265     4 GYLNKLETRGlglKGWKRRWFVLdeSKCQLYYYRSPQDATPLGSIDLSGAAFSYDPEAE-----PGQFEIHTPGRVHILK 78
                          90
                  ....*....|.
gi 688611584 1889 ANNDKDMNDWL 1899
Cdd:cd01265    79 ASTRQAMLYWL 89
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
1812-1902 1.11e-05

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: 45.61  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584 1812 KKGILNFMEPRSN-TWVKHFVVVRRPYVFIYNNDKDP--VERGVLNLStAQVEYSEDQQamLKTPHTFAMCT-KHRGILL 1887
Cdd:cd00821     1 KEGYLLKRGGGGLkSWKKRWFVLFEGVLLYYKSKKDSsyKPKGSIPLS-GILEVEEVSP--KERPHCFELVTpDGRTYYL 77
                          90
                  ....*....|....*
gi 688611584 1888 QANNDKDMNDWLYAF 1902
Cdd:cd00821    78 QADSEEERQEWLKAL 92
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
1812-1903 1.18e-05

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: 46.25  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584 1812 KKGIlnfmepRSNTWVKHFVVVRRPYVFIYNNDKdpvERGVLNL-------STAQVEysedqqaMLKTPHTFAMCTKHRG 1884
Cdd:cd13255    14 KKGE------RRKTWKKRWFVLRPTKLAYYKNDK---EYRLLRLidltdihTCTEVQ-------LKKHDNTFGIVTPART 77
                          90
                  ....*....|....*....
gi 688611584 1885 ILLQANNDKDMNDWLYAFN 1903
Cdd:cd13255    78 FYVQADSKAEMESWISAIN 96
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
606-672 7.62e-05

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


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 43.36  E-value: 7.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688611584  606 DIVLSGAHIKEEHCifRSERNANGHVivTLEP-CEGSETYVNGKRVNSAVQLRSGNRIIMGkNHVFRF 672
Cdd:cd22673    32 DIRIQLPGVSREHC--RIEVDENGKA--YLENlSTTNPTLVNGKAIEKSAELKDGDVITIG-GRSFRF 94
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
1825-1903 4.79e-04

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: 41.46  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584 1825 TWVKHFVVVRRPYVFIYNNDKDPVERGVLNLS--TAqVEYSEDQqamlKTPHTFAMCTKHRGILLQANNDKDMNDWLYAF 1902
Cdd:cd13298    21 NWKKRWVVLRPCQLSYYKDEKEYKLRRVINLSelLA-VAPLKDK----KRKNVFGIYTPSKNLHFRATSEKDANEWVEAL 95

                  .
gi 688611584 1903 N 1903
Cdd:cd13298    96 R 96
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
677-751 7.37e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.72  E-value: 7.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688611584  677 QARAEREKTPSAEtpvepvdwtfAQRELLEKQGIDMKQEMEKR----LTEMEILYKKEKEEADQLLEQQRLVYESKLQE 751
Cdd:cd16269   199 EIEAERAKAEAAE----------QERKLLEEQQRELEQKLEDQersyEEHLRQLKEKMEEERENLLKEQERALESKLKE 267
PH_CNK_mammalian-like cd01260
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
1823-1899 8.25e-04

Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; CNK family members function as protein scaffolds, regulating the activity and the subcellular localization of RAS activated RAF. There is a single CNK protein present in Drosophila and Caenorhabditis elegans in contrast to mammals which have 3 CNK proteins (CNK1, CNK2, and CNK3). All of the CNK members contain a sterile a motif (SAM), a conserved region in CNK (CRIC) domain, and a PSD-95/DLG-1/ZO-1 (PDZ) domain, and, with the exception of CNK3, a PH domain. A CNK2 splice variant CNK2A also has a PDZ domain-binding motif at its C terminus and Drosophila CNK (D-CNK) also has a domain known as the Raf-interacting region (RIR) that mediates binding of the Drosophila Raf kinase. This cd contains CNKs from mammals, chickens, amphibians, fish, and crustacea. 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: 269962  Cd Length: 114  Bit Score: 40.85  E-value: 8.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688611584 1823 SNTWVKHFVVVRRPYVFIYNNDKDPVERGVLNLStaqvEYSEDQQAMLKTPHTFAMC-TKHRGILLQANNDKDMNDWL 1899
Cdd:cd01260    30 GQKWKKYWFVLKGSSLYWYSNQQDEKAEGFINLP----DFKIERASECKKKYAFKAChPKIKTFYFAAENLDDMNKWL 103
FHA_GarA_OdhI-like cd22684
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ...
604-672 1.56e-03

forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438736 [Multi-domain]  Cd Length: 94  Bit Score: 39.67  E-value: 1.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688611584  604 RQDIVLSGAHIKEEHCIFRseRNANGHVIVTLEPCEGseTYVNGKRVNSAVqLRSGNRIIMGKnhvFRF 672
Cdd:cd22684    30 ESDIFLDDVTVSRRHAEFR--RAEGGFVVRDVGSLNG--TYVNRERIDSAV-LRNGDEVQIGK---FRL 90
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
700-757 2.37e-03

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 39.87  E-value: 2.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688611584  700 AQRELLEKQGIDMK-QEMEKRLTEME--------------ILYKKEKEEADQLLEQQRLVYESKLQELQKQVE 757
Cdd:COG1382    23 LQAVAAQKQQVESElKEAEKALEELEklpddaevyksvgnLLVKTDKEEVIKELEEKKETLELRLKTLEKQEE 95
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
996-1018 3.84e-03

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


Pssm-ID: 463574  Cd Length: 43  Bit Score: 36.81  E-value: 3.84e-03
                           10        20
                   ....*....|....*....|...
gi 688611584   996 SDIFSDGQDPFYDRSPWFILVGR 1018
Cdd:pfam12423   21 SQHFEVDRDPFYEPPENHNLIGV 43
PH_DAPP1 cd10573
Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; ...
1808-1898 3.86e-03

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: 38.46  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584 1808 SVVSKKGILNFMEPRSNTWVKHFVVVRRPYVFIYNNDKDPVERGVLNLSTAQ-VEYSEDQQamlkTPHTFAMCTKHRGIL 1886
Cdd:cd10573     1 SLGSKEGYLTKLGGIVKNWKTRWFVLRRNELKYFKTRGDTKPIRVLDLRECSsVQRDYSQG----KVNCFCLVFPERTFY 76
                          90
                  ....*....|..
gi 688611584 1887 LQANNDKDMNDW 1898
Cdd:cd10573    77 MYANTEEEADEW 88
FHA_FHAD1 cd22700
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ...
586-672 3.90e-03

forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438752 [Multi-domain]  Cd Length: 96  Bit Score: 38.39  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  586 LYYIKDGITRVGQADAerrqDIVLSGAHIKEEHCIFRSERNANGHVIVTLEPCEGseTYVNGKRV-NSAVQLRSGNRIIM 664
Cdd:cd22700    10 IFQLDPKVTTIGREGC----DLVLQSPGVEEQHAVIEYSEQENCFVLQDLNTAQG--TYVNDCRIqNAAVRLAPGDVLRF 83

                  ....*....
gi 688611584  665 GKN-HVFRF 672
Cdd:cd22700    84 GFGgLPYEL 92
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
1824-1901 4.56e-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: 38.89  E-value: 4.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584 1824 NTWVKHFVVVRRPYVFIYNnDKDPVERGV-----------LNLSTAQVEYSEdqqamLKTPHTFAMCTKHRG-ILLQANN 1891
Cdd:cd01253    22 RSWKQAWAVLRGHSLYLYK-DKREQTPALsielgseqrisIRGCIVDIAYSY-----TKRKHVFRLTTSDFSeYLFQAED 95
                          90
                  ....*....|
gi 688611584 1892 DKDMNDWLYA 1901
Cdd:cd01253    96 RDDMLGWIKA 105
PH1_ARAP cd13253
ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, ...
1811-1898 5.32e-03

ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 1; ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the first PH domain in ARAP. 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: 270073  Cd Length: 94  Bit Score: 38.14  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584 1811 SKKGILNFMEPRSNT--WVKHFVVVRRPYVFIYNNDKDPVERGVLNLSTAQVEYSE-DQQamlktphtFAMCTKHRGILL 1887
Cdd:cd13253     1 IKSGYLDKQGGQGNNkgFQKRWVVFDGLSLRYFDSEKDAYSKRIIPLSAISTVRAVgDNK--------FELVTTNRTFVF 72
                          90
                  ....*....|.
gi 688611584 1888 QANNDKDMNDW 1898
Cdd:cd13253    73 RAESDDERNLW 83
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
591-690 8.51e-03

forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.


Pssm-ID: 438737 [Multi-domain]  Cd Length: 130  Bit Score: 38.55  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688611584  591 DGITRVGQADAErrQDIVL-SGAH---IKEEHCIFRSERNANGHVIVTLEPCEGSETYVNGKRvnsavqLRSGNRIIMGK 666
Cdd:cd22685    27 LCEYRIGRNPEV--CDVFLcSSQHpnlISREHAEIHAERDGNGNWKVLIEDRSTNGTYVNDVR------LQDGQRRELSD 98
                          90       100
                  ....*....|....*....|....*
gi 688611584  667 NHVFRFNHPEQAR-AEREKTPSAET 690
Cdd:cd22685    99 GDTITFGHKNGRRvKQWPYQKSSEF 123
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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