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Conserved domains on  [gi|90652857|ref|NP_116207|]
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rho guanine nucleotide exchange factor 39 [Homo sapiens]

Protein Classification

rho guanine nucleotide exchange factor( domain architecture ID 107588)

rho guanine nucleotide exchange factor containing a pleckstrin homology (PH) domain, similar to Homo sapiens rho guanine nucleotide exchange factor 39 (Arhgef39) that promotes cell proliferation

CATH:  2.30.29.30|1.20.900.10
Gene Ontology:  GO:0005085|GO:0051056|GO:0005515
PubMed:  22728242|11738596
SCOP:  4002395|4001108

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGEF super family cl47571
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 27-195 2.52e-20

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


The actual alignment was detected with superfamily member pfam00621:

Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 86.58  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857    27 ARELLETERRYQEQLGLVATYFLGILKAKGTLRPPERQALFGSWELIYGASQELL------PYLEGGCWGQGLEGFCRHL 100
Cdd:pfam00621   2 IKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLLleellkEWISIQRIGDIFLKFAPGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857   101 ELYNQFAANSERSQTTLQEQLKKNKGFRRFVRLQEGRPEFGGLQLQDLLPLPLQRLQQYENLVVALAENTGPNSPDHQQL 180
Cdd:pfam00621  82 KVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHPDYEDL 161

                         170
                  ....*....|....*
gi 90652857   181 TRAARLISETAQRVH 195
Cdd:pfam00621 162 KKALEAIKEVAKQIN 176
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 225-269 1.27e-05

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13389:

Pssm-ID: 473070  Cd Length: 124  Bit Score: 43.80  E-value: 1.27e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 90652857 225 GRWFLRQGWLLVVPpHGEPRPRMFFLFTDVLLMAKPRPPLHLLRS 269
Cdd:cd13389  11 GRKLIKEGELMKVS-RKEMQPRYFFLFNDCLLYTTPVQSSGMLKL 54
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 230-331 1.66e-03

PH domain; PH stands for pleckstrin homology.


:

Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857   230 RQGWLL--VVPPHGEPRPRMFFLFTDVLLMAKPRPPLHLlrsgtFACKALYPMAQCHLSRVFGHS--GGPCGGLLSLS-- 303
Cdd:pfam00169   3 KEGWLLkkGGGKKKSWKKRYFVLFDGSLLYYKDDKSGKS-----KEPKGSISLSGCEVVEVVASDspKRKFCFELRTGer 77

                          90       100
                  ....*....|....*....|....*...
gi 90652857   304 FPHEKLLLMSTDQEELSRWYHSLTWAIS 331
Cdd:pfam00169  78 TGKRTYLLQAESEEERKDWIKAIQSAIR 105
 
Name Accession Description Interval E-value
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 27-195 2.52e-20

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 86.58  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857    27 ARELLETERRYQEQLGLVATYFLGILKAKGTLRPPERQALFGSWELIYGASQELL------PYLEGGCWGQGLEGFCRHL 100
Cdd:pfam00621   2 IKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLLleellkEWISIQRIGDIFLKFAPGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857   101 ELYNQFAANSERSQTTLQEQLKKNKGFRRFVRLQEGRPEFGGLQLQDLLPLPLQRLQQYENLVVALAENTGPNSPDHQQL 180
Cdd:pfam00621  82 KVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHPDYEDL 161

                         170
                  ....*....|....*
gi 90652857   181 TRAARLISETAQRVH 195
Cdd:pfam00621 162 KKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 27-195 5.22e-15

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 71.95  E-value: 5.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857     27 ARELLETERRYQEQLGLVATYFLGILKAKGT-LRPPERQALFGSWELIYGASQELLPYLE--GGCW-------GQGLEGF 96
Cdd:smart00325   2 LKELLQTERNYVRDLKLLVEVFLKPLKKELKlLSPNELETLFGNIEEIYEFHRDFLDELEerIEEWddsveriGDVFLKL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857     97 CRHLELYNQFAANSERSQTTLqEQLKKNKGFRRFVRLQEGRPEFGGLQLQDLLPLPLQRLQQYENLVVALAENTGPNSPD 176
Cdd:smart00325  82 EEFFKIYSEYCSNHPDALELL-KKLKKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHTPEDHED 160

                          170
                   ....*....|....*....
gi 90652857    177 HQQLTRAARLISETAQRVH 195
Cdd:smart00325 161 REDLKKALKAIKELANQVN 179
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 23-195 2.25e-12

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 64.63  E-value: 2.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857  23 RACTARELLETERRYQEQLGLVATYFL-GILKAKGTLRPPERQALFGSWELIYGASQELLPYLE---------GGCWGQG 92
Cdd:cd00160   1 RQEVIKELLQTERNYVRDLKLLVEVFLkPLDKELLPLSPEEVELLFGNIEEIYEFHRIFLKSLEerveewdksGPRIGDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857  93 LEGFCRHLELYNQFAANSERSQTTLQEQLKKNKGFRRFVRLQEGRPefGGLQLQDLLPLPLQRLQQYENLVVALAENTGP 172
Cdd:cd00160  81 FLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESEC--GRLKLESLLLKPVQRLTKYPLLLKELLKHTPD 158

                       170       180
                ....*....|....*....|...
gi 90652857 173 NSPDHQQLTRAARLISETAQRVH 195
Cdd:cd00160 159 GHEDREDLKKALEAIKEVASQVN 181
PH1_FGD5_FGD6 cd13389
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal ...
 225-269 1.27e-05

FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal Pleckstrin Homology (PH) domain; FGD5 regulates promotes angiogenesis of vascular endothelial growth factor (VEGF) in vascular endothelial cells, including network formation, permeability, directional movement, and proliferation. The specific function of FGD6 is unknown. In general, FGDs have a RhoGEF (DH) domain, followed by a PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activate the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the PH domain is involved in intracellular targeting of the DH 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: 275424  Cd Length: 124  Bit Score: 43.80  E-value: 1.27e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 90652857 225 GRWFLRQGWLLVVPpHGEPRPRMFFLFTDVLLMAKPRPPLHLLRS 269
Cdd:cd13389  11 GRKLIKEGELMKVS-RKEMQPRYFFLFNDCLLYTTPVQSSGMLKL 54
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 230-331 1.66e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857   230 RQGWLL--VVPPHGEPRPRMFFLFTDVLLMAKPRPPLHLlrsgtFACKALYPMAQCHLSRVFGHS--GGPCGGLLSLS-- 303
Cdd:pfam00169   3 KEGWLLkkGGGKKKSWKKRYFVLFDGSLLYYKDDKSGKS-----KEPKGSISLSGCEVVEVVASDspKRKFCFELRTGer 77

                          90       100
                  ....*....|....*....|....*...
gi 90652857   304 FPHEKLLLMSTDQEELSRWYHSLTWAIS 331
Cdd:pfam00169  78 TGKRTYLLQAESEEERKDWIKAIQSAIR 105
 
Name Accession Description Interval E-value
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 27-195 2.52e-20

RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that pfam00169 domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 459876 [Multi-domain]  Cd Length: 176  Bit Score: 86.58  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857    27 ARELLETERRYQEQLGLVATYFLGILKAKGTLRPPERQALFGSWELIYGASQELL------PYLEGGCWGQGLEGFCRHL 100
Cdd:pfam00621   2 IKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHRQLLleellkEWISIQRIGDIFLKFAPGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857   101 ELYNQFAANSERSQTTLQEQLKKNKGFRRFVRLQEGRPEFGGLQLQDLLPLPLQRLQQYENLVVALAENTGPNSPDHQQL 180
Cdd:pfam00621  82 KVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHTPPDHPDYEDL 161

                         170
                  ....*....|....*
gi 90652857   181 TRAARLISETAQRVH 195
Cdd:pfam00621 162 KKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 27-195 5.22e-15

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains. Improved coverage.


Pssm-ID: 214619 [Multi-domain]  Cd Length: 180  Bit Score: 71.95  E-value: 5.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857     27 ARELLETERRYQEQLGLVATYFLGILKAKGT-LRPPERQALFGSWELIYGASQELLPYLE--GGCW-------GQGLEGF 96
Cdd:smart00325   2 LKELLQTERNYVRDLKLLVEVFLKPLKKELKlLSPNELETLFGNIEEIYEFHRDFLDELEerIEEWddsveriGDVFLKL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857     97 CRHLELYNQFAANSERSQTTLqEQLKKNKGFRRFVRLQEGRPEFGGLQLQDLLPLPLQRLQQYENLVVALAENTGPNSPD 176
Cdd:smart00325  82 EEFFKIYSEYCSNHPDALELL-KKLKKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKHTPEDHED 160

                          170
                   ....*....|....*....
gi 90652857    177 HQQLTRAARLISETAQRVH 195
Cdd:smart00325 161 REDLKKALKAIKELANQVN 179
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 23-195 2.25e-12

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091 [Multi-domain]  Cd Length: 181  Bit Score: 64.63  E-value: 2.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857  23 RACTARELLETERRYQEQLGLVATYFL-GILKAKGTLRPPERQALFGSWELIYGASQELLPYLE---------GGCWGQG 92
Cdd:cd00160   1 RQEVIKELLQTERNYVRDLKLLVEVFLkPLDKELLPLSPEEVELLFGNIEEIYEFHRIFLKSLEerveewdksGPRIGDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857  93 LEGFCRHLELYNQFAANSERSQTTLQEQLKKNKGFRRFVRLQEGRPefGGLQLQDLLPLPLQRLQQYENLVVALAENTGP 172
Cdd:cd00160  81 FLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESEC--GRLKLESLLLKPVQRLTKYPLLLKELLKHTPD 158

                       170       180
                ....*....|....*....|...
gi 90652857 173 NSPDHQQLTRAARLISETAQRVH 195
Cdd:cd00160 159 GHEDREDLKKALEAIKEVASQVN 181
PH1_FGD5_FGD6 cd13389
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal ...
 225-269 1.27e-05

FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal Pleckstrin Homology (PH) domain; FGD5 regulates promotes angiogenesis of vascular endothelial growth factor (VEGF) in vascular endothelial cells, including network formation, permeability, directional movement, and proliferation. The specific function of FGD6 is unknown. In general, FGDs have a RhoGEF (DH) domain, followed by a PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activate the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the PH domain is involved in intracellular targeting of the DH 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: 275424  Cd Length: 124  Bit Score: 43.80  E-value: 1.27e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 90652857 225 GRWFLRQGWLLVVPpHGEPRPRMFFLFTDVLLMAKPRPPLHLLRS 269
Cdd:cd13389  11 GRKLIKEGELMKVS-RKEMQPRYFFLFNDCLLYTTPVQSSGMLKL 54
PH1_FARP1-like cd01220
FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin ...
 222-258 4.05e-05

FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins Pleckstrin Homology (PH) domain, repeat 1; Members here include FARP1 (also called Chondrocyte-derived ezrin-like protein; PH domain-containing family C member 2), FARP2 (also called FIR/FERM domain including RhoGEF; FGD1-related Cdc42-GEF/FRG), and FARP6 (also called Zinc finger FYVE domain-containing protein 24). They are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases. Little is known about FARP1 and FARP6, though FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons. FARP1 and FARP2 are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains. FARP6 is composed of Dbl-homology (DH), and two C-terminal PH domains separated by a FYVE domain. This hierarchy contains the first PH repeat. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269928  Cd Length: 109  Bit Score: 42.30  E-value: 4.05e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 90652857 222 LTSGRWFLRQGWLLVVPPHGePRPRMFFLFTDVLLMA 258
Cdd:cd01220   2 VQPGREFIREGCLQKLSKKG-LQQRMFFLFSDVLLYT 37
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 230-326 1.05e-03

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: 37.91  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857 230 RQGWLLVV--PPHGEPRPRMFFLFTDVLLMAKPRPplhllrSGTFACKALYPMAQCHLSRVFGHSGGPCGglLSLSFP-H 306
Cdd:cd00821   1 KEGYLLKRggGGLKSWKKRWFVLFEGVLLYYKSKK------DSSYKPKGSIPLSGILEVEEVSPKERPHC--FELVTPdG 72

                        90       100
                ....*....|....*....|
gi 90652857 307 EKLLLMSTDQEELSRWYHSL 326
Cdd:cd00821  73 RTYYLQADSEEERQEWLKAL 92
PH1_FGD6 cd15793
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 6, N-terminal Pleckstrin ...
 225-287 1.20e-03

FYVE, RhoGEF and PH domain containing/faciogenital dysplasia protein 6, N-terminal Pleckstrin Homology (PH) domain; FGD5 regulates promotes angiogenesis of vascular endothelial growth factor (VEGF) in vascular endothelial cells, including network formation, permeability, directional movement, and proliferation. The specific function of FGD6 is unknown. In general, FGDs have a RhoGEF (DH) domain, followed by a PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activate the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the PH domain is involved in intracellular targeting of the DH 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: 275436  Cd Length: 123  Bit Score: 38.47  E-value: 1.20e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90652857 225 GRWFLRQGWLLVVPpHGEPRPRMFFLFTDVLLMAKPrpplhlLRSGTFACKALYPMAQCHLSR 287
Cdd:cd15793  11 GRVFLKEGTLMKLS-RKVMQPRMFFLFNDALLYTTP------VQSGMYKLNNMLSLAGMKVSK 66
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 230-331 1.66e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90652857   230 RQGWLL--VVPPHGEPRPRMFFLFTDVLLMAKPRPPLHLlrsgtFACKALYPMAQCHLSRVFGHS--GGPCGGLLSLS-- 303
Cdd:pfam00169   3 KEGWLLkkGGGKKKSWKKRYFVLFDGSLLYYKDDKSGKS-----KEPKGSISLSGCEVVEVVASDspKRKFCFELRTGer 77

                          90       100
                  ....*....|....*....|....*...
gi 90652857   304 FPHEKLLLMSTDQEELSRWYHSLTWAIS 331
Cdd:pfam00169  78 TGKRTYLLQAESEEERKDWIKAIQSAIR 105
 
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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