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Conserved domains on  [gi|56788370|ref|NP_036587|]
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PH and SEC7 domain-containing protein 4 [Homo sapiens]

Protein Classification

PH and SEC7 domain-containing protein( domain architecture ID 10074498)

PH and SEC7 domain-containing protein may function as a guanine nucleotide exchange factor, similar to human PH and SEC7 domain-containing protein 4 (PSD4), also called exchange factor for ARF6 B (EFA6B), that is a guanine nucleotide exchange factor for ARF6 and ARL14/ARF7

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sec7 cd00171
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the ...
570-738 1.16e-70

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the central domain of the guanine-nucleotide-exchange factors (GEFs) of the ADP-ribosylation factor family of small GTPases (ARFs) . It carries the exchange factor activity.


:

Pssm-ID: 238100  Cd Length: 185  Bit Score: 232.88  E-value: 1.16e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  570 QRPPAGDKLA--NGVRNNKVAWNLASRLYRLEGFRKSEVAAYLQKNNDFSRAVAEEYLSFFQFGGQSLDRALRSFLQALV 647
Cdd:cd00171   14 RKPKKGISFLieKGFLEDDSPKEIAKFLYETEGLNKKAIGEYLGENNEFNSLVLHEFVDLFDFSGLRLDEALRKFLQSFR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  648 LSGETQERERILYQFSRRFHHCNPGIF-PSVDSVHTLTCAIMLLNTDLHGQNIGKSMSCQEFITNLNGLRDGGNFPKELL 726
Cdd:cd00171   94 LPGEAQKIDRLLEKFSERYCECNPGIFsSSADAAYTLAYSIIMLNTDLHNPNVKKKMTLEDFIKNLRGINDGEDFPREFL 173
                        170
                 ....*....|..
gi 56788370  727 KALYWSIRSEKL 738
Cdd:cd00171  174 KELYDSIKNNEI 185
PH_EFA6 cd13295
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ...
772-900 7.21e-70

Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. 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: 270107  Cd Length: 126  Bit Score: 228.37  E-value: 7.21e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  772 DPTVPTYKQGILARKMHQDADGKKTPWGKRGWKMFHTLLRGMVLYFLKqGEDHCLEGesLVGQMVDEPVGVHHSLATPAT 851
Cdd:cd13295    1 DPNAVEYKKGYLMRKCCADPDGKKTPFGKRGWKMFYATLKGLVLYLHK-DEYGCKKA--LRYESLRNAISVHHSLATKAT 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 56788370  852 HYTKKPHVFQLRTADWRLYLFQAPTAKEMSSWIARINLAAATHSAPPFP 900
Cdd:cd13295   78 DYTKKPHVFRLRTADWREYLFQASDTKEMQSWIEAINLVAAAFSAPPLP 126
 
Name Accession Description Interval E-value
Sec7 cd00171
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the ...
570-738 1.16e-70

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the central domain of the guanine-nucleotide-exchange factors (GEFs) of the ADP-ribosylation factor family of small GTPases (ARFs) . It carries the exchange factor activity.


Pssm-ID: 238100  Cd Length: 185  Bit Score: 232.88  E-value: 1.16e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  570 QRPPAGDKLA--NGVRNNKVAWNLASRLYRLEGFRKSEVAAYLQKNNDFSRAVAEEYLSFFQFGGQSLDRALRSFLQALV 647
Cdd:cd00171   14 RKPKKGISFLieKGFLEDDSPKEIAKFLYETEGLNKKAIGEYLGENNEFNSLVLHEFVDLFDFSGLRLDEALRKFLQSFR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  648 LSGETQERERILYQFSRRFHHCNPGIF-PSVDSVHTLTCAIMLLNTDLHGQNIGKSMSCQEFITNLNGLRDGGNFPKELL 726
Cdd:cd00171   94 LPGEAQKIDRLLEKFSERYCECNPGIFsSSADAAYTLAYSIIMLNTDLHNPNVKKKMTLEDFIKNLRGINDGEDFPREFL 173
                        170
                 ....*....|..
gi 56788370  727 KALYWSIRSEKL 738
Cdd:cd00171  174 KELYDSIKNNEI 185
PH_EFA6 cd13295
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ...
772-900 7.21e-70

Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. 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: 270107  Cd Length: 126  Bit Score: 228.37  E-value: 7.21e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  772 DPTVPTYKQGILARKMHQDADGKKTPWGKRGWKMFHTLLRGMVLYFLKqGEDHCLEGesLVGQMVDEPVGVHHSLATPAT 851
Cdd:cd13295    1 DPNAVEYKKGYLMRKCCADPDGKKTPFGKRGWKMFYATLKGLVLYLHK-DEYGCKKA--LRYESLRNAISVHHSLATKAT 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 56788370  852 HYTKKPHVFQLRTADWRLYLFQAPTAKEMSSWIARINLAAATHSAPPFP 900
Cdd:cd13295   78 DYTKKPHVFRLRTADWREYLFQASDTKEMQSWIEAINLVAAAFSAPPLP 126
Sec7 pfam01369
Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 ...
591-738 1.72e-49

Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 family.


Pssm-ID: 460178  Cd Length: 183  Bit Score: 173.41  E-value: 1.72e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370    591 LASRLYRLEGFRKSEVAAYLQKNNDFSRAVAEEYLSFFQFGGQSLDRALRSFLQALVLSGETQERERILYQFSRRFHHCN 670
Cdd:pfam01369   36 IAKFLFETPGLDKKAIGEYLGKPDEFNIEVLKAFVDLFDFKGLRIDEALRLFLESFRLPGEAQKIDRIMEAFAERYYEQN 115
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56788370    671 PGIFPSVDSVHTLTCAIMLLNTDLHGQNIGKSMSCQEFITNLNGLRDGGNFPKELLKALYWSIRSEKL 738
Cdd:pfam01369  116 PGVFANADAAYVLAYSIIMLNTDLHNPNVKKKMTLEDFIRNLRGINDGKDFPDEYLEEIYDSIKKNEI 183
Sec7 smart00222
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for ...
590-738 7.55e-48

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for proper protein transport through the Golgi. The domain facilitates guanine nucleotide exchange on the small GTPases, ARFs (ADP ribosylation factors).


Pssm-ID: 214569 [Multi-domain]  Cd Length: 189  Bit Score: 169.01  E-value: 7.55e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370     590 NLASRLYRLEGFRKSEVAAYLQKNNDFSRAVAEEYLSFFQFGGQSLDRALRSFLQALVLSGETQERERILYQFSRRFHHC 669
Cdd:smart00222   39 DVADFLSKNEGLNKKAIGDYLGEHDEFNRLVLHAFVDLFDFSAKDLDQALREFLESFRLPGEAQKIDRLLEAFSSRYCEC 118
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56788370     670 NPGIF--PSVDSVHTLTCAIMLLNTDLHGQNIGKSMSCQEFITNLNGLRDGGNFPKELLKALYWSIRSEKL 738
Cdd:smart00222  119 NPGVFskANADAAYTLAYSLIMLNTDLHNPNVKKKMTLEDFIKNVRGSNDGEDLPREFLEELYDSIKNNEI 189
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
778-892 3.06e-36

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 434701  Cd Length: 118  Bit Score: 132.94  E-value: 3.06e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370    778 YKQGILARKMHQDADGKKTPWGKRGWKMFHTLLRGMVLYFLKqgedhcLEGESLVGQMVDE------PVG---VHHSLAT 848
Cdd:pfam15410    1 YKKGIVMRKCCFESKGKKTPRGKRSWKMVYAVLKDLVLYLYK------DEHPPESSQFEDKkslknaPVGkirLHHALAT 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 56788370    849 PATHYTKKPHVFQLRTADWRLYLFQAPTAKEMSSWIARINLAAA 892
Cdd:pfam15410   75 PAPDYTKKSHVFRLQTADGAEYLFQTGSPKELQEWVDTLNYWAA 118
PLN03076 PLN03076
ARF guanine nucleotide exchange factor (ARF-GEF); Provisional
600-756 1.84e-26

ARF guanine nucleotide exchange factor (ARF-GEF); Provisional


Pssm-ID: 215560 [Multi-domain]  Cd Length: 1780  Bit Score: 117.62  E-value: 1.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370   600 GFRKSEVAAYLQKNNDFSRAVAEEYLSFFQFGGQSLDRALRSFLQALVLSGETQERERILYQFSRRFHHCNPGIFPSVDS 679
Cdd:PLN03076  660 GLNKTLIGDYLGEREDLSLKVMHAYVDSFDFQGMEFDEAIRAFLQGFRLPGEAQKIDRIMEKFAERYCKCNPKAFSSADT 739
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56788370   680 VHTLTCAIMLLNTDLHGQNIGKSMSCQEFITNLNGLRDGGNFPKELLKALYWSIRSEKLEWavdEEDTARPEKAQPS 756
Cdd:PLN03076  740 AYVLAYSVIMLNTDAHNPMVKNKMSADDFIRNNRGIDDGKDLPEEFMRSLYERISKNEIKM---KEDDLVPQQKQSA 813
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
794-892 1.27e-12

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


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 64.88  E-value: 1.27e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370     794 KKTPWGKRGWKMFHTLLRGMVLYFLKQGEDHClegeslvGQMVDEPVGVHHSLATPATHYT--KKPHVFQLRTADWRLYL 871
Cdd:smart00233    9 KKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKK-------SYKPKGSIDLSGCTVREAPDPDssKKPHCFEIKTSDRKTLL 81
                            90       100
                    ....*....|....*....|.
gi 56788370     872 FQAPTAKEMSSWIARINLAAA 892
Cdd:smart00233   82 LQAESEEEREKWVEALRKAIA 102
 
Name Accession Description Interval E-value
Sec7 cd00171
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the ...
570-738 1.16e-70

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the central domain of the guanine-nucleotide-exchange factors (GEFs) of the ADP-ribosylation factor family of small GTPases (ARFs) . It carries the exchange factor activity.


Pssm-ID: 238100  Cd Length: 185  Bit Score: 232.88  E-value: 1.16e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  570 QRPPAGDKLA--NGVRNNKVAWNLASRLYRLEGFRKSEVAAYLQKNNDFSRAVAEEYLSFFQFGGQSLDRALRSFLQALV 647
Cdd:cd00171   14 RKPKKGISFLieKGFLEDDSPKEIAKFLYETEGLNKKAIGEYLGENNEFNSLVLHEFVDLFDFSGLRLDEALRKFLQSFR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  648 LSGETQERERILYQFSRRFHHCNPGIF-PSVDSVHTLTCAIMLLNTDLHGQNIGKSMSCQEFITNLNGLRDGGNFPKELL 726
Cdd:cd00171   94 LPGEAQKIDRLLEKFSERYCECNPGIFsSSADAAYTLAYSIIMLNTDLHNPNVKKKMTLEDFIKNLRGINDGEDFPREFL 173
                        170
                 ....*....|..
gi 56788370  727 KALYWSIRSEKL 738
Cdd:cd00171  174 KELYDSIKNNEI 185
PH_EFA6 cd13295
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ...
772-900 7.21e-70

Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and Sec7 domain containing) is an guanine nucleotide exchange factor for ADP ribosylation factor 6 (ARF6), which is involved in membrane recycling. EFA6 has four structurally related polypeptides: EFA6A, EFA6B, EFA6C and EFA6D. It consists of a N-terminal proline rich region (PR), a SEC7 domain, a PH domain, a PR, a coiled-coil region, and a C-terminal PR. The EFA6 PH domain regulates its association with the plasma membrane. EFA6 activates Arf6 through its Sec7 catalytic domain and modulates this activity through its C-terminal domain, which rearranges the actin cytoskeleton in fibroblastic cell lines. 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: 270107  Cd Length: 126  Bit Score: 228.37  E-value: 7.21e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  772 DPTVPTYKQGILARKMHQDADGKKTPWGKRGWKMFHTLLRGMVLYFLKqGEDHCLEGesLVGQMVDEPVGVHHSLATPAT 851
Cdd:cd13295    1 DPNAVEYKKGYLMRKCCADPDGKKTPFGKRGWKMFYATLKGLVLYLHK-DEYGCKKA--LRYESLRNAISVHHSLATKAT 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 56788370  852 HYTKKPHVFQLRTADWRLYLFQAPTAKEMSSWIARINLAAATHSAPPFP 900
Cdd:cd13295   78 DYTKKPHVFRLRTADWREYLFQASDTKEMQSWIEAINLVAAAFSAPPLP 126
Sec7 pfam01369
Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 ...
591-738 1.72e-49

Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 family.


Pssm-ID: 460178  Cd Length: 183  Bit Score: 173.41  E-value: 1.72e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370    591 LASRLYRLEGFRKSEVAAYLQKNNDFSRAVAEEYLSFFQFGGQSLDRALRSFLQALVLSGETQERERILYQFSRRFHHCN 670
Cdd:pfam01369   36 IAKFLFETPGLDKKAIGEYLGKPDEFNIEVLKAFVDLFDFKGLRIDEALRLFLESFRLPGEAQKIDRIMEAFAERYYEQN 115
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56788370    671 PGIFPSVDSVHTLTCAIMLLNTDLHGQNIGKSMSCQEFITNLNGLRDGGNFPKELLKALYWSIRSEKL 738
Cdd:pfam01369  116 PGVFANADAAYVLAYSIIMLNTDLHNPNVKKKMTLEDFIRNLRGINDGKDFPDEYLEEIYDSIKKNEI 183
Sec7 smart00222
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for ...
590-738 7.55e-48

Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for proper protein transport through the Golgi. The domain facilitates guanine nucleotide exchange on the small GTPases, ARFs (ADP ribosylation factors).


Pssm-ID: 214569 [Multi-domain]  Cd Length: 189  Bit Score: 169.01  E-value: 7.55e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370     590 NLASRLYRLEGFRKSEVAAYLQKNNDFSRAVAEEYLSFFQFGGQSLDRALRSFLQALVLSGETQERERILYQFSRRFHHC 669
Cdd:smart00222   39 DVADFLSKNEGLNKKAIGDYLGEHDEFNRLVLHAFVDLFDFSAKDLDQALREFLESFRLPGEAQKIDRLLEAFSSRYCEC 118
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56788370     670 NPGIF--PSVDSVHTLTCAIMLLNTDLHGQNIGKSMSCQEFITNLNGLRDGGNFPKELLKALYWSIRSEKL 738
Cdd:smart00222  119 NPGVFskANADAAYTLAYSLIMLNTDLHNPNVKKKMTLEDFIKNVRGSNDGEDLPREFLEELYDSIKNNEI 189
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
778-892 3.06e-36

Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.


Pssm-ID: 434701  Cd Length: 118  Bit Score: 132.94  E-value: 3.06e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370    778 YKQGILARKMHQDADGKKTPWGKRGWKMFHTLLRGMVLYFLKqgedhcLEGESLVGQMVDE------PVG---VHHSLAT 848
Cdd:pfam15410    1 YKKGIVMRKCCFESKGKKTPRGKRSWKMVYAVLKDLVLYLYK------DEHPPESSQFEDKkslknaPVGkirLHHALAT 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 56788370    849 PATHYTKKPHVFQLRTADWRLYLFQAPTAKEMSSWIARINLAAA 892
Cdd:pfam15410   75 PAPDYTKKSHVFRLQTADGAEYLFQTGSPKELQEWVDTLNYWAA 118
PLN03076 PLN03076
ARF guanine nucleotide exchange factor (ARF-GEF); Provisional
600-756 1.84e-26

ARF guanine nucleotide exchange factor (ARF-GEF); Provisional


Pssm-ID: 215560 [Multi-domain]  Cd Length: 1780  Bit Score: 117.62  E-value: 1.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370   600 GFRKSEVAAYLQKNNDFSRAVAEEYLSFFQFGGQSLDRALRSFLQALVLSGETQERERILYQFSRRFHHCNPGIFPSVDS 679
Cdd:PLN03076  660 GLNKTLIGDYLGEREDLSLKVMHAYVDSFDFQGMEFDEAIRAFLQGFRLPGEAQKIDRIMEKFAERYCKCNPKAFSSADT 739
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56788370   680 VHTLTCAIMLLNTDLHGQNIGKSMSCQEFITNLNGLRDGGNFPKELLKALYWSIRSEKLEWavdEEDTARPEKAQPS 756
Cdd:PLN03076  740 AYVLAYSVIMLNTDAHNPMVKNKMSADDFIRNNRGIDDGKDLPEEFMRSLYERISKNEIKM---KEDDLVPQQKQSA 813
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
780-890 1.09e-20

Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a major component of the cytoskeleton underlying cellular membranes. Beta spectrin consists of multiple spectrin repeats followed by a PH domain, which binds to inositol-1,4,5-trisphosphate. The PH domain of beta-spectrin is thought to play a role in the association of spectrin with the plasma membrane of cells. 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: 269975  Cd Length: 106  Bit Score: 88.05  E-value: 1.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  780 QGILARKMHQDADGKKTPwgKRGWKMFHTLLRGMVLYFLKQGEDHCLE----GESlvgqmvdePVGVHHSLATPATHYTK 855
Cdd:cd10571    2 EGFLERKHEWESGGKKAS--NRSWKNVYTVLRGQELSFYKDQKAAKSGityaAEP--------PLNLYNAVCEVASDYTK 71
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 56788370  856 KPHVFQLRTADWRLYLFQAPTAKEMSSWIARINLA 890
Cdd:cd10571   72 KKHVFRLKLSDGAEFLFQAKDEEEMNQWVKKISFA 106
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
778-887 3.24e-15

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: 72.79  E-value: 3.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  778 YKQGILarKMHQDADGKKTPWGKRGWKMFHTLLRGMVLYFLKQgedhclEGESLVGQMVDE----PVGVHHSLATPATHY 853
Cdd:cd01253    1 AREGWL--HYKQIVTDKGKRVSDRSWKQAWAVLRGHSLYLYKD------KREQTPALSIELgseqRISIRGCIVDIAYSY 72
                         90       100       110
                 ....*....|....*....|....*....|....
gi 56788370  854 TKKPHVFQLRTADWRLYLFQAPTAKEMSSWIARI 887
Cdd:cd01253   73 TKRKHVFRLTTSDFSEYLFQAEDRDDMLGWIKAI 106
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
794-892 1.27e-12

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


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 64.88  E-value: 1.27e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370     794 KKTPWGKRGWKMFHTLLRGMVLYFLKQGEDHClegeslvGQMVDEPVGVHHSLATPATHYT--KKPHVFQLRTADWRLYL 871
Cdd:smart00233    9 KKSGGGKKSWKKRYFVLFNSTLLYYKSKKDKK-------SYKPKGSIDLSGCTVREAPDPDssKKPHCFEIKTSDRKTLL 81
                            90       100
                    ....*....|....*....|.
gi 56788370     872 FQAPTAKEMSSWIARINLAAA 892
Cdd:smart00233   82 LQAESEEEREKWVEALRKAIA 102
PH pfam00169
PH domain; PH stands for pleckstrin homology.
794-892 4.94e-09

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 54.88  E-value: 4.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370    794 KKTPWGKRGWKMFHTLLRGMVLYFLKqgEDHCLEGESLVG-------QMVDepvgvhhslaTPATHYTKKPHVFQLRTAD 866
Cdd:pfam00169    9 KKGGGKKKSWKKRYFVLFDGSLLYYK--DDKSGKSKEPKGsislsgcEVVE----------VVASDSPKRKFCFELRTGE 76
                           90       100
                   ....*....|....*....|....*....
gi 56788370    867 W---RLYLFQAPTAKEMSSWIARINLAAA 892
Cdd:pfam00169   77 RtgkRTYLLQAESEEERKDWIKAIQSAIR 105
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
794-887 6.17e-09

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: 54.09  E-value: 6.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  794 KKTPWGKRGWKMFHTLLRGMVLYFLKQGEDHCLEgesLVGQM-VDEPVGVHHSLATpathytKKPHVFQLRTADWRLYLF 872
Cdd:cd00821    7 KRGGGGLKSWKKRWFVLFEGVLLYYKSKKDSSYK---PKGSIpLSGILEVEEVSPK------ERPHCFELVTPDGRTYYL 77
                         90
                 ....*....|....*
gi 56788370  873 QAPTAKEMSSWIARI 887
Cdd:cd00821   78 QADSEEERQEWLKAL 92
PH1_Tiam1_2 cd01230
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; ...
777-893 9.66e-08

T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; Tiam1 activates Rac GTPases to induce membrane ruffling and cell motility while Tiam2 (also called STEF (SIF (still life) and Tiam1 like-exchange factor) contributes to neurite growth. Tiam1/2 are Dbl-family of GEFs that possess a Dbl(DH) domain with a PH domain in tandem. DH-PH domain catalyzes the GDP/GTP exchange reaction in the GTPase cycle and facillitating the switch between inactive GDP-bound and active GTP-bound states. Tiam1/2 possess two PH domains, which are often referred to as PHn and PHc domains. The DH-PH tandem domain is made up of the PHc domain while the PHn is part of a novel N-terminal PHCCEx domain which is made up of the PHn domain, a coiled coil region(CC), and an extra region (Ex). PHCCEx mediates binding to plasma membranes and signalling proteins in the activation of Rac GTPases. The PH domain resembles the beta-spectrin PH domain, suggesting non-canonical phosphatidylinositol binding. CC and Ex form a positively charged surface for protein binding. There are 2 motifs in Tiam1/2-interacting proteins that bind to the PHCCEx domain: Motif-I in CD44, ephrinBs, and the NMDA receptor and Motif-II in Par3 and JIP2.Neither of these fall in the PHn 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: 269937  Cd Length: 127  Bit Score: 51.69  E-value: 9.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  777 TYKQGILARK--MHQDADGKKTPWGKRGWKMFHTLLRGMVLYFLKQGEDHCLEGESLVGQMVDepvgVHHSLATPATHYT 854
Cdd:cd01230    3 VRKAGWLSVKnfLVHKKNKKVELATRRKWKKYWVCLKGCTLLFYECDERSGIDENSEPKHALF----VEGSIVQAVPEHP 78
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 56788370  855 KKPHVFQLRTADWRLYLFQAPTAKEMSSWIARINLAAAT 893
Cdd:cd01230   79 KKDFVFCLSNSFGDAYLFQATSQTELENWVTAIHSACAS 117
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
771-891 5.88e-07

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. 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: 270068  Cd Length: 104  Bit Score: 48.81  E-value: 5.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  771 QDPTVPTYKQGILARkmhQDADGKKTpWGKRgWkmFhtLLRGMVLYFLKQGEDhclegESLVGqMVDEPvGVHHSLATPA 850
Cdd:cd13248    1 RDPNAPVVMSGWLHK---QGGSGLKN-WRKR-W--F--VLKDNCLYYYKDPEE-----EKALG-SILLP-SYTISPAPPS 64
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 56788370  851 THYTKKpHVFQLRTADWRLYLFQAPTAKEMSSWIARINLAA 891
Cdd:cd13248   65 DEISRK-FAFKAEHANMRTYYFAADTAEEMEQWMNAMSLAA 104
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
800-890 2.68e-05

Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in platelets. This name is derived from platelet and leukocyte C kinase substrate and the KSTR string of amino acids. Pleckstrin 2 contains two PH domains and a DEP (dishvelled, egl-10, and pleckstrin) domain. Unlike pleckstrin 1, pleckstrin 2 does not contain obvious sites of PKC phosphorylation. Pleckstrin 2 plays a role in actin rearrangement, large lamellipodia and peripheral ruffle formation, and may help orchestrate cytoskeletal arrangement. The PH domains of pleckstrin 2 are thought to contribute to lamellipodia formation. This cd contains the first PH domain 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: 270113  Cd Length: 108  Bit Score: 44.29  E-value: 2.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  800 KRG-----WK-MFHTLLRGMVLYFlKQGEDHCLEGE-SLVGQmvdepvgvhhSLATPATHYTKKPHVFQLRTADWRLYLF 872
Cdd:cd13301   11 KKGhvvnnWKaRWFVLKEDGLEYY-KKKTDSSPKGMiPLKGC----------TITSPCLEYGKRPLVFKLTTAKGQEHFF 79
                         90
                 ....*....|....*...
gi 56788370  873 QAPTAKEMSSWIARINLA 890
Cdd:cd13301   80 QACSREERDAWAKDITKA 97
PH_KIFIA_KIFIB cd01233
KIFIA and KIFIB protein pleckstrin homology (PH) domain; The kinesin-3 family motors KIFIA ...
855-888 3.39e-04

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: 41.04  E-value: 3.39e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 56788370  855 KKPHVFQLRTADwRLYLFQAPTAKEMSSWIARIN 888
Cdd:cd01233   67 GRPNVFAVYTPT-NSYLLQARSEKEMQDWLYAID 99
PH_TAAP2-like cd13255
Tandem PH-domain-containing protein 2 Pleckstrin homology (PH) domain; The binding of TAPP2 ...
839-890 1.53e-03

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: 39.32  E-value: 1.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 56788370  839 PVGVHHSLATpaTHYTKKPHVFQLRTADwRLYLFQAPTAKEMSSWIARINLA 890
Cdd:cd13255   50 DLTDIHTCTE--VQLKKHDNTFGIVTPA-RTFYVQADSKAEMESWISAINLA 98
PH_CNK_mammalian-like cd01260
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
788-894 2.47e-03

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: 38.93  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56788370  788 HQDADG----KKTPWGKRG--WKMFHTLLRGMVLYFLKQGEDHCLEGE-SLVGQMVDEpvgvhhslatpaTHYTKKPHVF 860
Cdd:cd01260   12 RGDCQGwlwkKKEAKSFFGqkWKKYWFVLKGSSLYWYSNQQDEKAEGFiNLPDFKIER------------ASECKKKYAF 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 56788370  861 QLRTADWRLYLFQAPTAKEMSSWIARINLAAATH 894
Cdd:cd01260   80 KACHPKIKTFYFAAENLDDMNKWLSKLNMAINKY 113
 
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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