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Conserved domains on  [gi|569007912|ref|XP_006527449|]
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PH and SEC7 domain-containing protein 1 isoform X1 [Mus musculus]

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 ...
 543-709 4.91e-72

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: 236.74  E-value: 4.91e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  543 GSTDTLSNGQKADlEAAQRLAKRLYRLDGFRKADVARHLGKNNDFSKLVAGEYLKFFVFTGMTLDQALRVFLKELALMGE 622
Cdd:cd00171    19 GISFLIEKGFLED-DSPKEIAKFLYETEGLNKKAIGEYLGENNEFNSLVLHEFVDLFDFSGLRLDEALRKFLQSFRLPGE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  623 TQERERVLAHFSQRYFQCNPEAL-SSEDGAHTLTCALMLLNTDLHGHNIGKRMTCGDFIGNLEGLNDGGDFPRELLKALY 701
Cdd:cd00171    98 AQKIDRLLEKFSERYCECNPGIFsSSADAAYTLAYSIIMLNTDLHNPNVKKKMTLEDFIKNLRGINDGEDFPREFLKELY 177


                  ....*...
gi 569007912  702 SSIKNEKL 709
Cdd:cd00171   178 DSIKNNEI 185
PH_EFA6 cd13295
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ...
 754-878 2.26e-65

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: 215.66  E-value: 2.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  754 PGAAVYKHGALVRKVHADPDCRKTPRGKRGWKSFHGILKGMILYLQKEEYQPGKALSEAELKNAISIHHALATRASDYSK 833
Cdd:cd13295     2 PNAVEYKKGYLMRKCCADPDGKKTPFGKRGWKMFYATLKGLVLYLHKDEYGCKKALRYESLRNAISVHHSLATKATDYTK 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 569007912  834 RPHVFYLRTADWRVFLFQAPSLEQMQSWITRINVVAAMFSAPPFP 878
Cdd:cd13295    82 KPHVFRLRTADWREYLFQASDTKEMQSWIEAINLVAAAFSAPPLP 126
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 17-426 1.05e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912   17 SPPRCPRRWLPEGPVPQSPPASMYGSTGSLIRRVVGPGPRGrdlgrVTAPCTPLR--APPSPHIAPSPWGPSSPTGQPPP 94
Cdd:PHA03247 2707 TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG-----PATPGGPARpaRPPTTAGPPAPAPPAAPAAGPPR 2781

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912   95 GAQSSVVIFRFVEKASVrPLNGLPASGGLSRSWDLGGI-SAPRPTPALGPGCNRKLRLEASTSDPLP---AGGGSVLPGS 170
Cdd:PHA03247 2782 RLTRPAVASLSESRESL-PSPWDPADPPAAVLAPAAALpPAASPAGPLPPPTSAQPTAPPPPPGPPPpslPLGGSVAPGG 2860

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  171 ----RDPSRGPLVPPQIGADGLYSSLPN-GLGGTPEHLAMHFRGPADtgfLNQGDTWSSPREVSSHAQRIARAKWEFFYG 245
Cdd:PHA03247 2861 dvrrRPPSRSPAAKPAAPARPPVRRLARpAVSRSTESFALPPDQPER---PPQPQAPPPPQPQPQPPPPPQPQPPPPPPP 2937

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  246 SLDAP-SSGAKPPEQVLPSRGVGSKQGSGVAVGRaakYSETDLDKVPLRCYRETDIDEVLAEREEADSAIESQPSSEGPH 324
Cdd:PHA03247 2938 RPQPPlAPTTDPAGAGEPSGAVPQPWLGALVPGR---VAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALH 3014

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  325 GTAQPPASRPSPCPGPSsslgSGNEDDEAGGEEDVDDEVFEAsEGARPGDHMPHSGLLKSPVPfllgTSPSADGPDSFSC 404
Cdd:PHA03247 3015 EETDPPPVSLKQTLWPP----DDTEDSDADSLFDSDSERSDL-EALDPLPPEPHDPFAHEPDP----ATPEAGARESPSS 3085

                         410       420
                  ....*....|....*....|....*....
gi 569007912  405 VF-------EAILESHRAKGTSYSSLASL 426
Cdd:PHA03247 3086 QFgppplsaNAALSRRYVRSTGRSALAVL 3114
 
Name Accession Description Interval E-value
Sec7 cd00171
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the ...
 543-709 4.91e-72

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: 236.74  E-value: 4.91e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  543 GSTDTLSNGQKADlEAAQRLAKRLYRLDGFRKADVARHLGKNNDFSKLVAGEYLKFFVFTGMTLDQALRVFLKELALMGE 622
Cdd:cd00171    19 GISFLIEKGFLED-DSPKEIAKFLYETEGLNKKAIGEYLGENNEFNSLVLHEFVDLFDFSGLRLDEALRKFLQSFRLPGE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  623 TQERERVLAHFSQRYFQCNPEAL-SSEDGAHTLTCALMLLNTDLHGHNIGKRMTCGDFIGNLEGLNDGGDFPRELLKALY 701
Cdd:cd00171    98 AQKIDRLLEKFSERYCECNPGIFsSSADAAYTLAYSIIMLNTDLHNPNVKKKMTLEDFIKNLRGINDGEDFPREFLKELY 177


                  ....*...
gi 569007912  702 SSIKNEKL 709
Cdd:cd00171   178 DSIKNNEI 185
PH_EFA6 cd13295
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ...
 754-878 2.26e-65

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: 215.66  E-value: 2.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  754 PGAAVYKHGALVRKVHADPDCRKTPRGKRGWKSFHGILKGMILYLQKEEYQPGKALSEAELKNAISIHHALATRASDYSK 833
Cdd:cd13295     2 PNAVEYKKGYLMRKCCADPDGKKTPFGKRGWKMFYATLKGLVLYLHKDEYGCKKALRYESLRNAISVHHSLATKATDYTK 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 569007912  834 RPHVFYLRTADWRVFLFQAPSLEQMQSWITRINVVAAMFSAPPFP 878
Cdd:cd13295    82 KPHVFRLRTADWREYLFQASDTKEMQSWIEAINLVAAAFSAPPLP 126
Sec7 smart00222
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for ...
 524-709 1.11e-62

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: 210.61  E-value: 1.11e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912    524 SQLVSDSDSELDSTERLALGSTDTLSNGQKADleaAQRLAKRLYRLDGFRKADVARHLGKNNDFSKLVAGEYLKFFVFTG 603
Cdd:smart00222    5 KKLLSEGIVKFNDKPKKGIQSLQEKGFLANED---PQDVADFLSKNEGLNKKAIGDYLGEHDEFNRLVLHAFVDLFDFSA 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912    604 MTLDQALRVFLKELALMGETQERERVLAHFSQRYFQCNPEALS--SEDGAHTLTCALMLLNTDLHGHNIGKRMTCGDFIG 681
Cdd:smart00222   82 KDLDQALREFLESFRLPGEAQKIDRLLEAFSSRYCECNPGVFSkaNADAAYTLAYSLIMLNTDLHNPNVKKKMTLEDFIK 161

                           170       180
                    ....*....|....*....|....*...
gi 569007912    682 NLEGLNDGGDFPRELLKALYSSIKNEKL 709
Cdd:smart00222  162 NVRGSNDGEDLPREFLEELYDSIKNNEI 189
Sec7 pfam01369
Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 ...
 559-709 1.62e-53

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


Pssm-ID: 460178  Cd Length: 183  Bit Score: 184.59  E-value: 1.62e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912   559 AQRLAKRLYRLDGFRKADVARHLGKNNDFSKLVAGEYLKFFVFTGMTLDQALRVFLKELALMGETQERERVLAHFSQRYF 638
Cdd:pfam01369   33 PESIAKFLFETPGLDKKAIGEYLGKPDEFNIEVLKAFVDLFDFKGLRIDEALRLFLESFRLPGEAQKIDRIMEAFAERYY 112

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569007912   639 QCNPEALSSEDGAHTLTCALMLLNTDLHGHNIGKRMTCGDFIGNLEGLNDGGDFPRELLKALYSSIKNEKL 709
Cdd:pfam01369  113 EQNPGVFANADAAYVLAYSIIMLNTDLHNPNVKKKMTLEDFIRNLRGINDGKDFPDEYLEEIYDSIKKNEI 183
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
 759-870 6.84e-39

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


Pssm-ID: 434701  Cd Length: 118  Bit Score: 140.26  E-value: 6.84e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912   759 YKHGALVRKVHADPDCRKTPRGKRGWKSFHGILKGMILYLQKEEYQPGKALSEAE--LKNA----ISIHHALATRASDYS 832
Cdd:pfam15410    1 YKKGIVMRKCCFESKGKKTPRGKRSWKMVYAVLKDLVLYLYKDEHPPESSQFEDKksLKNApvgkIRLHHALATPAPDYT 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 569007912   833 KRPHVFYLRTADWRVFLFQAPSLEQMQSWITRINVVAA 870
Cdd:pfam15410   81 KKSHVFRLQTADGAEYLFQTGSPKELQEWVDTLNYWAA 118
PLN03076 PLN03076
ARF guanine nucleotide exchange factor (ARF-GEF); Provisional
 557-707 3.94e-28

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


Pssm-ID: 215560 [Multi-domain]  Cd Length: 1780  Bit Score: 123.01  E-value: 3.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  557 EAAQRLAKRLYRLDGFRKADVARHLGKNNDFSKLVAGEYLKFFVFTGMTLDQALRVFLKELALMGETQERERVLAHFSQR 636
Cdd:PLN03076  646 ESPEEIAAFLKDASGLNKTLIGDYLGEREDLSLKVMHAYVDSFDFQGMEFDEAIRAFLQGFRLPGEAQKIDRIMEKFAER 725

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007912  637 YFQCNPEALSSEDGAHTLTCALMLLNTDLHGHNIGKRMTCGDFIGNLEGLNDGGDFPRELLKALYSSI-KNE 707
Cdd:PLN03076  726 YCKCNPKAFSSADTAYVLAYSVIMLNTDAHNPMVKNKMSADDFIRNNRGIDDGKDLPEEFMRSLYERIsKNE 797
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 758-866 1.97e-15

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: 72.97  E-value: 1.97e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912    758 VYKHGALVRKvhadpdcrkTPRGKRGWKSFHGILKGMILYLqkeeYQPGKALSEAELKNAISIHHALATRASDYS--KRP 835
Cdd:smart00233    1 VIKEGWLYKK---------SGGGKKSWKKRYFVLFNSTLLY----YKSKKDKKSYKPKGSIDLSGCTVREAPDPDssKKP 67

                            90       100       110
                    ....*....|....*....|....*....|.
gi 569007912    836 HVFYLRTADWRVFLFQAPSLEQMQSWITRIN 866
Cdd:smart00233   68 HCFEIKTSDRKTLLLQAESEEEREKWVEALR 98
PHA03247 PHA03247
large tegument protein UL36; Provisional
 17-426 1.05e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912   17 SPPRCPRRWLPEGPVPQSPPASMYGSTGSLIRRVVGPGPRGrdlgrVTAPCTPLR--APPSPHIAPSPWGPSSPTGQPPP 94
Cdd:PHA03247 2707 TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG-----PATPGGPARpaRPPTTAGPPAPAPPAAPAAGPPR 2781

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912   95 GAQSSVVIFRFVEKASVrPLNGLPASGGLSRSWDLGGI-SAPRPTPALGPGCNRKLRLEASTSDPLP---AGGGSVLPGS 170
Cdd:PHA03247 2782 RLTRPAVASLSESRESL-PSPWDPADPPAAVLAPAAALpPAASPAGPLPPPTSAQPTAPPPPPGPPPpslPLGGSVAPGG 2860

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  171 ----RDPSRGPLVPPQIGADGLYSSLPN-GLGGTPEHLAMHFRGPADtgfLNQGDTWSSPREVSSHAQRIARAKWEFFYG 245
Cdd:PHA03247 2861 dvrrRPPSRSPAAKPAAPARPPVRRLARpAVSRSTESFALPPDQPER---PPQPQAPPPPQPQPQPPPPPQPQPPPPPPP 2937

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  246 SLDAP-SSGAKPPEQVLPSRGVGSKQGSGVAVGRaakYSETDLDKVPLRCYRETDIDEVLAEREEADSAIESQPSSEGPH 324
Cdd:PHA03247 2938 RPQPPlAPTTDPAGAGEPSGAVPQPWLGALVPGR---VAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALH 3014

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  325 GTAQPPASRPSPCPGPSsslgSGNEDDEAGGEEDVDDEVFEAsEGARPGDHMPHSGLLKSPVPfllgTSPSADGPDSFSC 404
Cdd:PHA03247 3015 EETDPPPVSLKQTLWPP----DDTEDSDADSLFDSDSERSDL-EALDPLPPEPHDPFAHEPDP----ATPEAGARESPSS 3085

                         410       420
                  ....*....|....*....|....*....
gi 569007912  405 VF-------EAILESHRAKGTSYSSLASL 426
Cdd:PHA03247 3086 QFgppplsaNAALSRRYVRSTGRSALAVL 3114
 
Name Accession Description Interval E-value
Sec7 cd00171
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product. The Sec7 domain is the ...
 543-709 4.91e-72

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: 236.74  E-value: 4.91e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  543 GSTDTLSNGQKADlEAAQRLAKRLYRLDGFRKADVARHLGKNNDFSKLVAGEYLKFFVFTGMTLDQALRVFLKELALMGE 622
Cdd:cd00171    19 GISFLIEKGFLED-DSPKEIAKFLYETEGLNKKAIGEYLGENNEFNSLVLHEFVDLFDFSGLRLDEALRKFLQSFRLPGE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  623 TQERERVLAHFSQRYFQCNPEAL-SSEDGAHTLTCALMLLNTDLHGHNIGKRMTCGDFIGNLEGLNDGGDFPRELLKALY 701
Cdd:cd00171    98 AQKIDRLLEKFSERYCECNPGIFsSSADAAYTLAYSIIMLNTDLHNPNVKKKMTLEDFIKNLRGINDGEDFPREFLKELY 177


                  ....*...
gi 569007912  702 SSIKNEKL 709
Cdd:cd00171   178 DSIKNNEI 185
PH_EFA6 cd13295
Exchange Factor for ARF6 Pleckstrin homology (PH) domain; EFA6 (also called PSD/pleckstrin and ...
 754-878 2.26e-65

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: 215.66  E-value: 2.26e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  754 PGAAVYKHGALVRKVHADPDCRKTPRGKRGWKSFHGILKGMILYLQKEEYQPGKALSEAELKNAISIHHALATRASDYSK 833
Cdd:cd13295     2 PNAVEYKKGYLMRKCCADPDGKKTPFGKRGWKMFYATLKGLVLYLHKDEYGCKKALRYESLRNAISVHHSLATKATDYTK 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 569007912  834 RPHVFYLRTADWRVFLFQAPSLEQMQSWITRINVVAAMFSAPPFP 878
Cdd:cd13295    82 KPHVFRLRTADWREYLFQASDTKEMQSWIEAINLVAAAFSAPPLP 126
Sec7 smart00222
Sec7 domain; Domain named after the S. cerevisiae SEC7 gene product, which is required for ...
 524-709 1.11e-62

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: 210.61  E-value: 1.11e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912    524 SQLVSDSDSELDSTERLALGSTDTLSNGQKADleaAQRLAKRLYRLDGFRKADVARHLGKNNDFSKLVAGEYLKFFVFTG 603
Cdd:smart00222    5 KKLLSEGIVKFNDKPKKGIQSLQEKGFLANED---PQDVADFLSKNEGLNKKAIGDYLGEHDEFNRLVLHAFVDLFDFSA 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912    604 MTLDQALRVFLKELALMGETQERERVLAHFSQRYFQCNPEALS--SEDGAHTLTCALMLLNTDLHGHNIGKRMTCGDFIG 681
Cdd:smart00222   82 KDLDQALREFLESFRLPGEAQKIDRLLEAFSSRYCECNPGVFSkaNADAAYTLAYSLIMLNTDLHNPNVKKKMTLEDFIK 161

                           170       180
                    ....*....|....*....|....*...
gi 569007912    682 NLEGLNDGGDFPRELLKALYSSIKNEKL 709
Cdd:smart00222  162 NVRGSNDGEDLPREFLEELYDSIKNNEI 189
Sec7 pfam01369
Sec7 domain; The Sec7 domain is a guanine-nucleotide-exchange-factor (GEF) for the pfam00025 ...
 559-709 1.62e-53

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


Pssm-ID: 460178  Cd Length: 183  Bit Score: 184.59  E-value: 1.62e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912   559 AQRLAKRLYRLDGFRKADVARHLGKNNDFSKLVAGEYLKFFVFTGMTLDQALRVFLKELALMGETQERERVLAHFSQRYF 638
Cdd:pfam01369   33 PESIAKFLFETPGLDKKAIGEYLGKPDEFNIEVLKAFVDLFDFKGLRIDEALRLFLESFRLPGEAQKIDRIMEAFAERYY 112

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569007912   639 QCNPEALSSEDGAHTLTCALMLLNTDLHGHNIGKRMTCGDFIGNLEGLNDGGDFPRELLKALYSSIKNEKL 709
Cdd:pfam01369  113 EQNPGVFANADAAYVLAYSIIMLNTDLHNPNVKKKMTLEDFIRNLRGINDGKDFPDEYLEEIYDSIKKNEI 183
PH_9 pfam15410
Pleckstrin homology domain; This Pleckstrin homology domain is found in some fungal species.
 759-870 6.84e-39

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


Pssm-ID: 434701  Cd Length: 118  Bit Score: 140.26  E-value: 6.84e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912   759 YKHGALVRKVHADPDCRKTPRGKRGWKSFHGILKGMILYLQKEEYQPGKALSEAE--LKNA----ISIHHALATRASDYS 832
Cdd:pfam15410    1 YKKGIVMRKCCFESKGKKTPRGKRSWKMVYAVLKDLVLYLYKDEHPPESSQFEDKksLKNApvgkIRLHHALATPAPDYT 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 569007912   833 KRPHVFYLRTADWRVFLFQAPSLEQMQSWITRINVVAA 870
Cdd:pfam15410   81 KKSHVFRLQTADGAEYLFQTGSPKELQEWVDTLNYWAA 118
PLN03076 PLN03076
ARF guanine nucleotide exchange factor (ARF-GEF); Provisional
 557-707 3.94e-28

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


Pssm-ID: 215560 [Multi-domain]  Cd Length: 1780  Bit Score: 123.01  E-value: 3.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  557 EAAQRLAKRLYRLDGFRKADVARHLGKNNDFSKLVAGEYLKFFVFTGMTLDQALRVFLKELALMGETQERERVLAHFSQR 636
Cdd:PLN03076  646 ESPEEIAAFLKDASGLNKTLIGDYLGEREDLSLKVMHAYVDSFDFQGMEFDEAIRAFLQGFRLPGEAQKIDRIMEKFAER 725

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569007912  637 YFQCNPEALSSEDGAHTLTCALMLLNTDLHGHNIGKRMTCGDFIGNLEGLNDGGDFPRELLKALYSSI-KNE 707
Cdd:PLN03076  726 YCKCNPKAFSSADTAYVLAYSVIMLNTDAHNPMVKNKMSADDFIRNNRGIDDGKDLPEEFMRSLYERIsKNE 797
PH_beta_spectrin cd10571
Beta-spectrin pleckstrin homology (PH) domain; Beta spectrin binds actin and functions as a ...
 762-866 4.27e-19

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: 83.43  E-value: 4.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  762 GALVRKVHADPDCRKTPrgKRGWKSFHGILKGMILYLQKEEyqpgKALSEAELKNA---ISIHHALATRASDYSKRPHVF 838
Cdd:cd10571     3 GFLERKHEWESGGKKAS--NRSWKNVYTVLRGQELSFYKDQ----KAAKSGITYAAeppLNLYNAVCEVASDYTKKKHVF 76

                          90       100
                  ....*....|....*....|....*...
gi 569007912  839 YLRTADWRVFLFQAPSLEQMQSWITRIN 866
Cdd:cd10571    77 RLKLSDGAEFLFQAKDEEEMNQWVKKIS 104
PH_ARHGAP21-like cd01253
ARHGAP21 and related proteins pleckstrin homology (PH) domain; ARHGAP family genes encode Rho ...
 759-865 1.86e-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: 73.17  E-value: 1.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  759 YKHGALVRKVHADPDCRKTPRgkRGWKSFHGILKGMILYLQKEEYQPGKALS-EAELKNAISIHHALATRASDYSKRPHV 837
Cdd:cd01253     1 AREGWLHYKQIVTDKGKRVSD--RSWKQAWAVLRGHSLYLYKDKREQTPALSiELGSEQRISIRGCIVDIAYSYTKRKHV 78

                          90       100
                  ....*....|....*....|....*...
gi 569007912  838 FYLRTADWRVFLFQAPSLEQMQSWITRI 865
Cdd:cd01253    79 FRLTTSDFSEYLFQAEDRDDMLGWIKAI 106
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 758-866 1.97e-15

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: 72.97  E-value: 1.97e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912    758 VYKHGALVRKvhadpdcrkTPRGKRGWKSFHGILKGMILYLqkeeYQPGKALSEAELKNAISIHHALATRASDYS--KRP 835
Cdd:smart00233    1 VIKEGWLYKK---------SGGGKKSWKKRYFVLFNSTLLY----YKSKKDKKSYKPKGSIDLSGCTVREAPDPDssKKP 67

                            90       100       110
                    ....*....|....*....|....*....|.
gi 569007912    836 HVFYLRTADWRVFLFQAPSLEQMQSWITRIN 866
Cdd:smart00233   68 HCFEIKTSDRKTLLLQAESEEEREKWVEALR 98
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 758-866 4.25e-13

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 66.43  E-value: 4.25e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912   758 VYKHGALVRKvhadpdcrkTPRGKRGWKSFHGILKGMILYLqkeeYQPGKALSEAELKNAISIHHALATR--ASDYSKRP 835
Cdd:pfam00169    1 VVKEGWLLKK---------GGGKKKSWKKRYFVLFDGSLLY----YKDDKSGKSKEPKGSISLSGCEVVEvvASDSPKRK 67

                           90       100       110
                   ....*....|....*....|....*....|....
gi 569007912   836 HVFYLRTADW---RVFLFQAPSLEQMQSWITRIN 866
Cdd:pfam00169   68 FCFELRTGERtgkRTYLLQAESEEERKDWIKAIQ 101
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 774-865 1.67e-11

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: 61.40  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  774 CRKTPRGKRGWKSFHGILKGMILYLQKEEYQPGKalseaELKNAISIHHALATRASDYSKRPHVFYLRTADWRVFLFQAP 853
Cdd:cd00821     6 LKRGGGGLKSWKKRWFVLFEGVLLYYKSKKDSSY-----KPKGSIPLSGILEVEEVSPKERPHCFELVTPDGRTYYLQAD 80

                          90
                  ....*....|..
gi 569007912  854 SLEQMQSWITRI 865
Cdd:cd00821    81 SEEERQEWLKAL 92
PH1_Tiam1_2 cd01230
T-lymphoma invasion and metastasis 1 and 2 Pleckstrin Homology (PH) domain, N-terminal domain; ...
 781-870 4.90e-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: 52.46  E-value: 4.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  781 KRGWKSFHGILKG-MILYLQKEEYQPGKALSEAelKNAISIHHALATRASDYSKRPHVFYLRTADWRVFLFQAPSLEQMQ 859
Cdd:cd01230    28 RRKWKKYWVCLKGcTLLFYECDERSGIDENSEP--KHALFVEGSIVQAVPEHPKKDFVFCLSNSFGDAYLFQATSQTELE 105

                          90
                  ....*....|.
gi 569007912  860 SWITRINVVAA 870
Cdd:cd01230   106 NWVTAIHSACA 116
PHA03247 PHA03247
large tegument protein UL36; Provisional
 17-426 1.05e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912   17 SPPRCPRRWLPEGPVPQSPPASMYGSTGSLIRRVVGPGPRGrdlgrVTAPCTPLR--APPSPHIAPSPWGPSSPTGQPPP 94
Cdd:PHA03247 2707 TPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAG-----PATPGGPARpaRPPTTAGPPAPAPPAAPAAGPPR 2781

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912   95 GAQSSVVIFRFVEKASVrPLNGLPASGGLSRSWDLGGI-SAPRPTPALGPGCNRKLRLEASTSDPLP---AGGGSVLPGS 170
Cdd:PHA03247 2782 RLTRPAVASLSESRESL-PSPWDPADPPAAVLAPAAALpPAASPAGPLPPPTSAQPTAPPPPPGPPPpslPLGGSVAPGG 2860

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  171 ----RDPSRGPLVPPQIGADGLYSSLPN-GLGGTPEHLAMHFRGPADtgfLNQGDTWSSPREVSSHAQRIARAKWEFFYG 245
Cdd:PHA03247 2861 dvrrRPPSRSPAAKPAAPARPPVRRLARpAVSRSTESFALPPDQPER---PPQPQAPPPPQPQPQPPPPPQPQPPPPPPP 2937

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  246 SLDAP-SSGAKPPEQVLPSRGVGSKQGSGVAVGRaakYSETDLDKVPLRCYRETDIDEVLAEREEADSAIESQPSSEGPH 324
Cdd:PHA03247 2938 RPQPPlAPTTDPAGAGEPSGAVPQPWLGALVPGR---VAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWASSLALH 3014

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  325 GTAQPPASRPSPCPGPSsslgSGNEDDEAGGEEDVDDEVFEAsEGARPGDHMPHSGLLKSPVPfllgTSPSADGPDSFSC 404
Cdd:PHA03247 3015 EETDPPPVSLKQTLWPP----DDTEDSDADSLFDSDSERSDL-EALDPLPPEPHDPFAHEPDP----ATPEAGARESPSS 3085

                         410       420
                  ....*....|....*....|....*....
gi 569007912  405 VF-------EAILESHRAKGTSYSSLASL 426
Cdd:PHA03247 3086 QFgppplsaNAALSRRYVRSTGRSALAVL 3114
PH1_Pleckstrin_2 cd13301
Pleckstrin 2 Pleckstrin homology (PH) domain, repeat 1; Pleckstrin is a protein found in ...
 758-866 1.59e-04

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: 41.97  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  758 VYKHGALVRKVHADPDcrktprgkrgWKSFHGILK--GMILYLQKEEYQPGKALseaELKNAISIHHALatrasDYSKRP 835
Cdd:cd13301     3 IIKEGYLVKKGHVVNN----------WKARWFVLKedGLEYYKKKTDSSPKGMI---PLKGCTITSPCL-----EYGKRP 64

                          90       100       110
                  ....*....|....*....|....*....|.
gi 569007912  836 HVFYLRTADWRVFLFQAPSLEQMQSWITRIN 866
Cdd:cd13301    65 LVFKLTTAKGQEHFFQACSREERDAWAKDIT 95
PH_CNK_mammalian-like cd01260
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
 772-870 3.08e-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: 38.54  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569007912  772 PDC------RKTPRGKRG--WKSFHGILKGMILYLQKEEyQPGKALSeaelknAISIHHALATRASDySKRPHVFYLRTA 843
Cdd:cd01260    13 GDCqgwlwkKKEAKSFFGqkWKKYWFVLKGSSLYWYSNQ-QDEKAEG------FINLPDFKIERASE-CKKKYAFKACHP 84

                          90       100
                  ....*....|....*....|....*..
gi 569007912  844 DWRVFLFQAPSLEQMQSWITRINVVAA 870
Cdd:cd01260    85 KIKTFYFAAENLDDMNKWLSKLNMAIN 111
 
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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