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Conserved domains on  [gi|15822816|dbj|BAB69038|]
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kinesin-related protein [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Kinesin_assoc super family cl24686
Kinesin-associated;
21-120 3.81e-65

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 318424  Cd Length: 181  Bit Score: 218.20  E-value: 3.81e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816     21 SVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLV 100
Cdd:pfam16183   82 SVSSLHERIMFTPGSEEAIERLKETEKIIAELNETWEEKLRRTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLV 161
                           90       100
                   ....*....|....*....|
gi 15822816    101 NLNEDPLMSECLLYYIKDGI 120
Cdd:pfam16183  162 NLNEDPLMSECLLYYIKDGI 181
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
832-978 3.42e-57

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: 338370  Cd Length: 148  Bit Score: 193.96  E-value: 3.42e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816    832 YIPAVVDHTAGLPcQGTFLLHQGIQRRITVTIIHEKGSELHWKDVRELVVGRIRNKPE---VDEAAVDAILSLNIISAKY 908
Cdd:pfam12473    1 YVPVPVDQSSELD-PGAFQLHQGLQRRIVITLTHSSGDQLPWERVREVRVGDVRLLDSmgrVPDSESTPDVSLKLLSEPV 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816    909 LKSSHNSsRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAVITKDVCMVFYSRDA 978
Cdd:pfam12473   80 VEFNADG-TSSYTIEAQWDSSLHNSLLLNRVTADGERVYLTLSWDLVSEKCAEPVRFSKDTAVQIYPRDE 148
PH_KIFIA_KIFIB cd01233
KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA ...
1262-1364 1.12e-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: 185.10  E-value: 1.12e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816 1262 RPSSVVSKKGYLHFKEPLYSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMVKTPNTFAVCTKHRG 1341
Cdd:cd01233    1 PKSPVVSKRGYLLFLEDATDGWVRRWVVLRRPYLHIYSSEKDGDERGVINLSTARVEYSPDQEALLGRPNVFAVYTPTNS 80
                         90       100
                 ....*....|....*....|...
gi 15822816 1342 VLLQALNDKDMNDWLYAFNPLLA 1364
Cdd:cd01233   81 YLLQARSEKEMQDWLYAIDPLLA 103
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
97-201 1.25e-13

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


:

Pssm-ID: 238017 [Multi-domain]  Cd Length: 102  Bit Score: 67.80  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816   97 PHLVNLNEDplmSECLLYYIK-DGITRVGQADaeRRQDIVLSGAHIKEEHCIFRSERSNSGeviVTLEPCERSETYVNGK 175
Cdd:cd00060    2 PRLVVLSGD---ASGRRYYLDpGGTYTIGRDS--DNCDIVLDDPSVSRRHAVIRYDGDGGV---VLIDLGSTNGTFVNGQ 73
                         90       100
                 ....*....|....*....|....*....
gi 15822816  176 RVSQ--PVQLRSGNRIIMGK-NHVFRFNH 201
Cdd:cd00060   74 RVSPgePVRLRDGDVIRLGNtSISFRFES 102
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
410-457 1.85e-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: 338345  Cd Length: 44  Bit Score: 65.63  E-value: 1.85e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 15822816    410 LKQRLDLMREMYDRAGEMASSAQDESETTvtgsDPFYDRFHWFKLVGS 457
Cdd:pfam12423    1 LENRLIDMREMYQEYKEGEYRNHFKPEEG----DPFYESQENHSLIGV 44
Prefoldin super family cl09111
Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, ...
227-282 3.93e-03

Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


The actual alignment was detected with superfamily member TIGR02338:

Pssm-ID: 352933 [Multi-domain]  Cd Length: 110  Bit Score: 38.10  E-value: 3.93e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15822816    227 AQRELLEKQGIDMKQ-EMEKRLQEME--------------ILYKKEKEEADLLLEQQRLDYESKLQALQKQ 282
Cdd:TIGR02338   19 LQAVATQKQQVEAQLkEAEKALEELErlpddtpvyksvgnLLVKTDKEEAIQELKEKKETLELRVKTLQRQ 89
 
Name Accession Description Interval E-value
Kinesin_assoc pfam16183
Kinesin-associated;
21-120 3.81e-65

Kinesin-associated;


Pssm-ID: 318424  Cd Length: 181  Bit Score: 218.20  E-value: 3.81e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816     21 SVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLV 100
Cdd:pfam16183   82 SVSSLHERIMFTPGSEEAIERLKETEKIIAELNETWEEKLRRTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLV 161
                           90       100
                   ....*....|....*....|
gi 15822816    101 NLNEDPLMSECLLYYIKDGI 120
Cdd:pfam16183  162 NLNEDPLMSECLLYYIKDGI 181
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
832-978 3.42e-57

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: 338370  Cd Length: 148  Bit Score: 193.96  E-value: 3.42e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816    832 YIPAVVDHTAGLPcQGTFLLHQGIQRRITVTIIHEKGSELHWKDVRELVVGRIRNKPE---VDEAAVDAILSLNIISAKY 908
Cdd:pfam12473    1 YVPVPVDQSSELD-PGAFQLHQGLQRRIVITLTHSSGDQLPWERVREVRVGDVRLLDSmgrVPDSESTPDVSLKLLSEPV 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816    909 LKSSHNSsRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAVITKDVCMVFYSRDA 978
Cdd:pfam12473   80 VEFNADG-TSSYTIEAQWDSSLHNSLLLNRVTADGERVYLTLSWDLVSEKCAEPVRFSKDTAVQIYPRDE 148
PH_KIFIA_KIFIB cd01233
KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA ...
1262-1364 1.12e-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: 185.10  E-value: 1.12e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816 1262 RPSSVVSKKGYLHFKEPLYSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMVKTPNTFAVCTKHRG 1341
Cdd:cd01233    1 PKSPVVSKRGYLLFLEDATDGWVRRWVVLRRPYLHIYSSEKDGDERGVINLSTARVEYSPDQEALLGRPNVFAVYTPTNS 80
                         90       100
                 ....*....|....*....|...
gi 15822816 1342 VLLQALNDKDMNDWLYAFNPLLA 1364
Cdd:cd01233   81 YLLQARSEKEMQDWLYAIDPLLA 103
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
97-201 1.25e-13

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


Pssm-ID: 238017 [Multi-domain]  Cd Length: 102  Bit Score: 67.80  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816   97 PHLVNLNEDplmSECLLYYIK-DGITRVGQADaeRRQDIVLSGAHIKEEHCIFRSERSNSGeviVTLEPCERSETYVNGK 175
Cdd:cd00060    2 PRLVVLSGD---ASGRRYYLDpGGTYTIGRDS--DNCDIVLDDPSVSRRHAVIRYDGDGGV---VLIDLGSTNGTFVNGQ 73
                         90       100
                 ....*....|....*....|....*....
gi 15822816  176 RVSQ--PVQLRSGNRIIMGK-NHVFRFNH 201
Cdd:cd00060   74 RVSPgePVRLRDGDVIRLGNtSISFRFES 102
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
410-457 1.85e-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: 338345  Cd Length: 44  Bit Score: 65.63  E-value: 1.85e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 15822816    410 LKQRLDLMREMYDRAGEMASSAQDESETTvtgsDPFYDRFHWFKLVGS 457
Cdd:pfam12423    1 LENRLIDMREMYQEYKEGEYRNHFKPEEG----DPFYESQENHSLIGV 44
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1267-1360 7.98e-13

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


Pssm-ID: 214574  Cd Length: 102  Bit Score: 65.65  E-value: 7.98e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816    1267 VSKKGYLHFKEPLYS-NWAKHFVVVRRPYVFIYNSDK---DPVERGIINLSTAQVEYSEDQQaMVKTPNTFAVCTKHRGV 1342
Cdd:smart00233    1 VIKEGWLYKKSGGGKkSWKKRYFVLFNSTLLYYKSKKdkkSYKPKGSIDLSGCTVREAPDPD-SSKKPHCFEIKTSDRKT 79
                            90
                    ....*....|....*....
gi 15822816    1343 L-LQALNDKDMNDWLYAFN 1360
Cdd:smart00233   80 LlLQAESEEEREKWVEALR 98
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1267-1360 6.31e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 333896  Cd Length: 103  Bit Score: 57.55  E-value: 6.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816   1267 VSKKGYLHFKEP-LYSNWAKHFVVVRRPYVFIY---NSDKDPVERGIINLSTAQVEYSEDQqAMVKTPNTFAVCTKH--- 1339
Cdd:pfam00169    1 VIKEGWLLKKGGgKKKSWKKRYFVLFDGSLLYYkdsSRGKSKEPKGSISLSGCTVVEVVAP-DKPKRKFCFELRTGEldg 79
                           90       100
                   ....*....|....*....|..
gi 15822816   1340 -RGVLLQALNDKDMNDWLYAFN 1360
Cdd:pfam00169   80 kRTYLLQAESEEERKEWIKAIQ 101
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
121-191 1.03e-08

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


Pssm-ID: 334113 [Multi-domain]  Cd Length: 66  Bit Score: 52.56  E-value: 1.03e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15822816    121 TRVGQAdaeRRQDIVLSGAHIKEEHCIFRSERSNSgeviVTLEPC-ERSETYVNGKRVS-QPVQLRSGNRIIM 191
Cdd:pfam00498    1 VTIGRS---PDCDIVLDDPSVSRRHAEIRYDGGGR----FYLEDLgSTNGTFVNGQRLGpEPVRLKDGDVIRL 66
gimC_beta TIGR02338
prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular ...
227-282 3.93e-03

prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and is found (usually) in bacteria and organelles of bacterial origin. The group II chaperonin system, called the thermosome in Archaea and TRiC or CCT in the Eukaryota, is structurally similar but only distantly related. Prefoldin, also called GimC, is a complex in Archaea and Eukaryota, that works with group II chaperonins. Members of this protein family are the archaeal clade of the beta class of prefoldin subunit. Closely related, but outside the scope of this family are the eukaryotic beta-class prefoldin subunits, Gim-1,3,4 and 6. The alpha class prefoldin subunits are more distantly related.


Pssm-ID: 131391 [Multi-domain]  Cd Length: 110  Bit Score: 38.10  E-value: 3.93e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15822816    227 AQRELLEKQGIDMKQ-EMEKRLQEME--------------ILYKKEKEEADLLLEQQRLDYESKLQALQKQ 282
Cdd:TIGR02338   19 LQAVATQKQQVEAQLkEAEKALEELErlpddtpvyksvgnLLVKTDKEEAIQELKEKKETLELRVKTLQRQ 89
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
204-290 4.69e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816   204 QARAEREKTPSAETPSEpvdwtfaqrELLEKQGID---MKQEMEKRLQEMEIlyKKEKEE-ADLLLEQQRLDYEsklqAL 279
Cdd:PRK09510   74 AKRAEEQRKKKEQQQAE---------ELQQKQAAEqerLKQLEKERLAAQEQ--KKQAEEaAKQAALKQKQAEE----AA 138
                          90
                  ....*....|.
gi 15822816   280 QKQVETRSLAA 290
Cdd:PRK09510  139 AKAAAAAKAKA 149
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
204-277 8.53e-03

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: 39.48  E-value: 8.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15822816  204 QARAEREKTPSAEtpsepvdwtfAQRELLEKQGIDMKQEM---EKRLQE-MEILYKKEKEEADLLLEQQRLDYESKLQ 277
Cdd:cd16269  199 EIEAERAKAEAAE----------QERKLLEEQQRELEQKLedqERSYEEhLRQLKEKMEEERENLLKEQERALESKLK 266
 
Name Accession Description Interval E-value
Kinesin_assoc pfam16183
Kinesin-associated;
21-120 3.81e-65

Kinesin-associated;


Pssm-ID: 318424  Cd Length: 181  Bit Score: 218.20  E-value: 3.81e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816     21 SVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLV 100
Cdd:pfam16183   82 SVSSLHERIMFTPGSEEAIERLKETEKIIAELNETWEEKLRRTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLV 161
                           90       100
                   ....*....|....*....|
gi 15822816    101 NLNEDPLMSECLLYYIKDGI 120
Cdd:pfam16183  162 NLNEDPLMSECLLYYIKDGI 181
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
832-978 3.42e-57

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: 338370  Cd Length: 148  Bit Score: 193.96  E-value: 3.42e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816    832 YIPAVVDHTAGLPcQGTFLLHQGIQRRITVTIIHEKGSELHWKDVRELVVGRIRNKPE---VDEAAVDAILSLNIISAKY 908
Cdd:pfam12473    1 YVPVPVDQSSELD-PGAFQLHQGLQRRIVITLTHSSGDQLPWERVREVRVGDVRLLDSmgrVPDSESTPDVSLKLLSEPV 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816    909 LKSSHNSsRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAVITKDVCMVFYSRDA 978
Cdd:pfam12473   80 VEFNADG-TSSYTIEAQWDSSLHNSLLLNRVTADGERVYLTLSWDLVSEKCAEPVRFSKDTAVQIYPRDE 148
PH_KIFIA_KIFIB cd01233
KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA ...
1262-1364 1.12e-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: 185.10  E-value: 1.12e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816 1262 RPSSVVSKKGYLHFKEPLYSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMVKTPNTFAVCTKHRG 1341
Cdd:cd01233    1 PKSPVVSKRGYLLFLEDATDGWVRRWVVLRRPYLHIYSSEKDGDERGVINLSTARVEYSPDQEALLGRPNVFAVYTPTNS 80
                         90       100
                 ....*....|....*....|...
gi 15822816 1342 VLLQALNDKDMNDWLYAFNPLLA 1364
Cdd:cd01233   81 YLLQARSEKEMQDWLYAIDPLLA 103
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
97-201 1.25e-13

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


Pssm-ID: 238017 [Multi-domain]  Cd Length: 102  Bit Score: 67.80  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816   97 PHLVNLNEDplmSECLLYYIK-DGITRVGQADaeRRQDIVLSGAHIKEEHCIFRSERSNSGeviVTLEPCERSETYVNGK 175
Cdd:cd00060    2 PRLVVLSGD---ASGRRYYLDpGGTYTIGRDS--DNCDIVLDDPSVSRRHAVIRYDGDGGV---VLIDLGSTNGTFVNGQ 73
                         90       100
                 ....*....|....*....|....*....
gi 15822816  176 RVSQ--PVQLRSGNRIIMGK-NHVFRFNH 201
Cdd:cd00060   74 RVSPgePVRLRDGDVIRLGNtSISFRFES 102
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
410-457 1.85e-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: 338345  Cd Length: 44  Bit Score: 65.63  E-value: 1.85e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 15822816    410 LKQRLDLMREMYDRAGEMASSAQDESETTvtgsDPFYDRFHWFKLVGS 457
Cdd:pfam12423    1 LENRLIDMREMYQEYKEGEYRNHFKPEEG----DPFYESQENHSLIGV 44
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
1267-1360 7.98e-13

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


Pssm-ID: 214574  Cd Length: 102  Bit Score: 65.65  E-value: 7.98e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816    1267 VSKKGYLHFKEPLYS-NWAKHFVVVRRPYVFIYNSDK---DPVERGIINLSTAQVEYSEDQQaMVKTPNTFAVCTKHRGV 1342
Cdd:smart00233    1 VIKEGWLYKKSGGGKkSWKKRYFVLFNSTLLYYKSKKdkkSYKPKGSIDLSGCTVREAPDPD-SSKKPHCFEIKTSDRKT 79
                            90
                    ....*....|....*....
gi 15822816    1343 L-LQALNDKDMNDWLYAFN 1360
Cdd:smart00233   80 LlLQAESEEEREKWVEALR 98
PH pfam00169
PH domain; PH stands for pleckstrin homology.
1267-1360 6.31e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 333896  Cd Length: 103  Bit Score: 57.55  E-value: 6.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816   1267 VSKKGYLHFKEP-LYSNWAKHFVVVRRPYVFIY---NSDKDPVERGIINLSTAQVEYSEDQqAMVKTPNTFAVCTKH--- 1339
Cdd:pfam00169    1 VIKEGWLLKKGGgKKKSWKKRYFVLFDGSLLYYkdsSRGKSKEPKGSISLSGCTVVEVVAP-DKPKRKFCFELRTGEldg 79
                           90       100
                   ....*....|....*....|..
gi 15822816   1340 -RGVLLQALNDKDMNDWLYAFN 1360
Cdd:pfam00169   80 kRTYLLQAESEEERKEWIKAIQ 101
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
121-191 1.03e-08

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


Pssm-ID: 334113 [Multi-domain]  Cd Length: 66  Bit Score: 52.56  E-value: 1.03e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15822816    121 TRVGQAdaeRRQDIVLSGAHIKEEHCIFRSERSNSgeviVTLEPC-ERSETYVNGKRVS-QPVQLRSGNRIIM 191
Cdd:pfam00498    1 VTIGRS---PDCDIVLDDPSVSRRHAEIRYDGGGR----FYLEDLgSTNGTFVNGQRLGpEPVRLKDGDVIRL 66
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
1269-1359 2.46e-07

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  Cd Length: 92  Bit Score: 49.85  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816 1269 KKGYLHFKE-PLYSNWAKHFVVVRRPYVFIYNSDKDP--VERGIINLStAQVEYSEDQQamVKTPNTFAVCT-KHRGVLL 1344
Cdd:cd00821    1 KEGYLLKRGgGGLKSWKKRWFVLFEGVLLYYKSKKDSsyKPKGSIPLS-GILEVEEVSP--KERPHCFELVTpDGRTYYL 77
                         90
                 ....*....|....*
gi 15822816 1345 QALNDKDMNDWLYAF 1359
Cdd:cd00821   78 QADSEEERQEWLKAL 92
PH_TBC1D2A cd01265
TBC1 domain family member 2A pleckstrin homology (PH) domain; TBC1D2A (also called PARIS-1 ...
1271-1356 7.38e-07

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


Pssm-ID: 269966  Cd Length: 102  Bit Score: 48.47  E-value: 7.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816 1271 GYLHFKE---PLYSNWAKHFVVV--RRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQamvktPNTFAVCTKHRGVLLQ 1345
Cdd:cd01265    4 GYLNKLEtrgLGLKGWKRRWFVLdeSKCQLYYYRSPQDATPLGSIDLSGAAFSYDPEAE-----PGQFEIHTPGRVHILK 78
                         90
                 ....*....|.
gi 15822816 1346 ALNDKDMNDWL 1356
Cdd:cd01265   79 ASTRQAMLYWL 89
PH1_PH_fungal cd13298
Fungal proteins Pleckstrin homology (PH) domain, repeat 1; The functions of these fungal ...
1267-1360 3.11e-06

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: 46.85  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816 1267 VSKKGYLHFKEPLYSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLS--TAqVEYSEDQqamvKTPNTFAVCTKHRGVLL 1344
Cdd:cd13298    6 VLKSGYLLKRSRKTKNWKKRWVVLRPCQLSYYKDEKEYKLRRVINLSelLA-VAPLKDK----KRKNVFGIYTPSKNLHF 80
                         90
                 ....*....|....*.
gi 15822816 1345 QALNDKDMNDWLYAFN 1360
Cdd:cd13298   81 RATSEKDANEWVEALR 96
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
1264-1360 2.65e-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: 44.33  E-value: 2.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816 1264 SSVVSKKGYLHFKEPLYSNWAKHFVVVRRPYVFIYNSDKDPVERGIINL----STAQVEysedqqaMVKTPNTFAVCTKH 1339
Cdd:cd13255    3 SEAVLKAGYLEKKGERRKTWKKRWFVLRPTKLAYYKNDKEYRLLRLIDLtdihTCTEVQ-------LKKHDNTFGIVTPA 75
                         90       100
                 ....*....|....*....|.
gi 15822816 1340 RGVLLQALNDKDMNDWLYAFN 1360
Cdd:cd13255   76 RTFYVQADSKAEMESWISAIN 96
PH1_ARAP cd13253
ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, ...
1268-1355 3.79e-05

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: 43.53  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816 1268 SKKGYLHFKEPLYSN--WAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSedqqamvKTPNTFAVCTKHRGVLLQ 1345
Cdd:cd13253    1 IKSGYLDKQGGQGNNkgFQKRWVVFDGLSLRYFDSEKDAYSKRIIPLSAISTVRA-------VGDNKFELVTTNRTFVFR 73
                         90
                 ....*....|
gi 15822816 1346 ALNDKDMNDW 1355
Cdd:cd13253   74 AESDDERNLW 83
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
1269-1358 2.03e-04

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: 41.97  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816 1269 KKGYLHFKEPLYS--------NWAKHFVVVRRPYVFIYNsDKDPVERGI-----------INLSTAQVEYSEdqqamVKT 1329
Cdd:cd01253    2 REGWLHYKQIVTDkgkrvsdrSWKQAWAVLRGHSLYLYK-DKREQTPALsielgseqrisIRGCIVDIAYSY-----TKR 75
                         90       100       110
                 ....*....|....*....|....*....|
gi 15822816 1330 PNTFAVCTKHRG-VLLQALNDKDMNDWLYA 1358
Cdd:cd01253   76 KHVFRLTTSDFSeYLFQAEDRDDMLGWIKA 105
PH_DAPP1 cd10573
Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; ...
1265-1355 3.39e-04

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  Cd Length: 96  Bit Score: 40.77  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816 1265 SVVSKKGYLHFKEPLYSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQ-VEYSEDQQamvkTPNTFAVCTKHRGVL 1343
Cdd:cd10573    1 SLGSKEGYLTKLGGIVKNWKTRWFVLRRNELKYFKTRGDTKPIRVLDLRECSsVQRDYSQG----KVNCFCLVFPERTFY 76
                         90
                 ....*....|..
gi 15822816 1344 LQALNDKDMNDW 1355
Cdd:cd10573   77 MYANTEEEADEW 88
PH_Ses cd13288
Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 ...
1265-1358 2.06e-03

Sesquipedalian family Pleckstrin homology (PH) domain; The sesquipedalian family has 2 mammalian members: Ses1 and Ses2, which are also callled 7 kDa inositol polyphosphate phosphatase-interacting protein 1 and 2. They play a role in endocytic trafficking and are required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane. Members of this family form homodimers and heterodimers. Sesquipedalian interacts with inositol polyphosphate 5-phosphatase OCRL-1 (INPP5F) also known as Lowe oculocerebrorenal syndrome protein, a phosphatase enzyme that is involved in actin polymerization and is found in the trans-Golgi network and INPP5B. Sesquipedalian contains a single 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: 270105  Cd Length: 120  Bit Score: 39.14  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816 1265 SVVSKKGYLHFKEPLYSNWAKHFVVVRRPYVFIYNS--DKDPVerGIINLSTAQVEYSEDQqamvkTPNTFAVCT---KH 1339
Cdd:cd13288    6 SPVDKEGYLWKKGERNTSYQKRWFVLKGNLLFYFEKkgDREPL--GVIVLEGCTVELAEDA-----EPYAFAIRFdgpGA 78
                         90
                 ....*....|....*....
gi 15822816 1340 RGVLLQALNDKDMNDWLYA 1358
Cdd:cd13288   79 RSYVLAAENQEDMESWMKA 97
gimC_beta TIGR02338
prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular ...
227-282 3.93e-03

prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and is found (usually) in bacteria and organelles of bacterial origin. The group II chaperonin system, called the thermosome in Archaea and TRiC or CCT in the Eukaryota, is structurally similar but only distantly related. Prefoldin, also called GimC, is a complex in Archaea and Eukaryota, that works with group II chaperonins. Members of this protein family are the archaeal clade of the beta class of prefoldin subunit. Closely related, but outside the scope of this family are the eukaryotic beta-class prefoldin subunits, Gim-1,3,4 and 6. The alpha class prefoldin subunits are more distantly related.


Pssm-ID: 131391 [Multi-domain]  Cd Length: 110  Bit Score: 38.10  E-value: 3.93e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15822816    227 AQRELLEKQGIDMKQ-EMEKRLQEME--------------ILYKKEKEEADLLLEQQRLDYESKLQALQKQ 282
Cdd:TIGR02338   19 LQAVATQKQQVEAQLkEAEKALEELErlpddtpvyksvgnLLVKTDKEEAIQELKEKKETLELRVKTLQRQ 89
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
204-290 4.69e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816   204 QARAEREKTPSAETPSEpvdwtfaqrELLEKQGID---MKQEMEKRLQEMEIlyKKEKEE-ADLLLEQQRLDYEsklqAL 279
Cdd:PRK09510   74 AKRAEEQRKKKEQQQAE---------ELQQKQAAEqerLKQLEKERLAAQEQ--KKQAEEaAKQAALKQKQAEE----AA 138
                          90
                  ....*....|.
gi 15822816   280 QKQVETRSLAA 290
Cdd:PRK09510  139 AKAAAAAKAKA 149
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
122-203 7.88e-03

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 318828 [Multi-domain]  Cd Length: 91  Bit Score: 36.80  E-value: 7.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15822816    122 RVGQADaerRQDIVLSGAHIKEEHCIFRSErsnsGEVIVTLEPCERSETYVNGKRVSQPvqLRSGNRIIMGKNHvFRFNH 201
Cdd:pfam16697   20 RIGSDP---DCDIVLSDKEVSRVHLKLEVD----DEGVRLTDLGSRNGTLVNGQRVELE--LRPGDVIELGTTE-FKLVP 89

                   ..
gi 15822816    202 PE 203
Cdd:pfam16697   90 ED 91
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
204-277 8.53e-03

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: 39.48  E-value: 8.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15822816  204 QARAEREKTPSAEtpsepvdwtfAQRELLEKQGIDMKQEM---EKRLQE-MEILYKKEKEEADLLLEQQRLDYESKLQ 277
Cdd:cd16269  199 EIEAERAKAEAAE----------QERKLLEEQQRELEQKLedqERSYEEhLRQLKEKMEEERENLLKEQERALESKLK 266
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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