NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|73997759|ref|XP_534913|]
View 

pleckstrin homology domain-containing family G member 6 [Canis lupus familiaris]

Protein Classification

pleckstrin homology domain-containing family G member 6( domain architecture ID 10457356)

pleckstrin homology domain-containing family G member 6 (PLEKHG6) acts as a guanine nucleotide exchange factor activating the small GTPase RHOA, which, in turn, induces myosin filament formation. Also activates RHOG

Gene Symbol:  PLEKHG6
Gene Ontology:  GO:0005085|GO:0051056|GO:0005096
PubMed:  11738596

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PH_PLEKHG5_G6 cd13244
Pleckstrin homology domain-containing family G member 5 and 6 pleckstrin homology (PH) domain; ...
408-506 4.17e-44

Pleckstrin homology domain-containing family G member 5 and 6 pleckstrin homology (PH) domain; PLEKHG5 has a RhoGEF DH/double-homology domain in tandem with a PH domain which is involved in phospholipid binding. PLEKHG5 activates the nuclear factor kappa B (NFKB1) signaling pathway. Mutations in PLEKHG5 are associated with autosomal recessive distal spinal muscular atrophy. PLEKHG6 (also called MyoGEF) has no known function to date. 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: 270064  Cd Length: 100  Bit Score: 153.92  E-value: 4.17e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759 408 RQLLLEGPVRVKEGREGKLDVYLFLFSDVLLVTKP-QRKADRAKVIRPPLMLEKLVCQPLRDPNSFLVIHLTDFQCVSSA 486
Cdd:cd13244   1 RRLLLEGDLRLKEGKGSKVDVHCFLFTDMLLICKPvKRKKDRLKVIRPPYLVDKLVVQELKDPGGFLLVYLNEFHTAVAA 80
                        90       100
                ....*....|....*....|
gi 73997759 487 FIVHCPSATDCAQWLKKTQQ 506
Cdd:cd13244  81 YTFQTSSQEDTRRWLDAIRK 100
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
165-351 5.50e-44

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: 425783 [Multi-domain]  Cd Length: 176  Bit Score: 156.69  E-value: 5.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759   165 AIWELLTTELTYVRKLKIMTDLLVsgllnLQRVELLTEVSAE--TLFGNIPSLIRVHKSFWEEVLGPTLEETRTSGRPld 242
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFL-----PPNSKPLSESEEEikTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDI-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759   243 pvslqngFLTFSQRFQPYVQYCLQVKRTMAYAREQQDNNPLFHAFVQWCEKHKRSGRQMLGDLLIKPHQRITKYPLLLQA 322
Cdd:pfam00621  74 -------FLKFAPGFKVYSTYCSNYPKALELLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKE 146
                         170       180       190
                  ....*....|....*....|....*....|
gi 73997759   323 VLKRSPEAHA-REALNTMIAAVESFLRHIN 351
Cdd:pfam00621 147 LLKHTPPDHPdYEDLKKALEAIKEVAKQIN 176
 
Name Accession Description Interval E-value
PH_PLEKHG5_G6 cd13244
Pleckstrin homology domain-containing family G member 5 and 6 pleckstrin homology (PH) domain; ...
408-506 4.17e-44

Pleckstrin homology domain-containing family G member 5 and 6 pleckstrin homology (PH) domain; PLEKHG5 has a RhoGEF DH/double-homology domain in tandem with a PH domain which is involved in phospholipid binding. PLEKHG5 activates the nuclear factor kappa B (NFKB1) signaling pathway. Mutations in PLEKHG5 are associated with autosomal recessive distal spinal muscular atrophy. PLEKHG6 (also called MyoGEF) has no known function to date. 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: 270064  Cd Length: 100  Bit Score: 153.92  E-value: 4.17e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759 408 RQLLLEGPVRVKEGREGKLDVYLFLFSDVLLVTKP-QRKADRAKVIRPPLMLEKLVCQPLRDPNSFLVIHLTDFQCVSSA 486
Cdd:cd13244   1 RRLLLEGDLRLKEGKGSKVDVHCFLFTDMLLICKPvKRKKDRLKVIRPPYLVDKLVVQELKDPGGFLLVYLNEFHTAVAA 80
                        90       100
                ....*....|....*....|
gi 73997759 487 FIVHCPSATDCAQWLKKTQQ 506
Cdd:cd13244  81 YTFQTSSQEDTRRWLDAIRK 100
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
165-351 5.50e-44

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: 425783 [Multi-domain]  Cd Length: 176  Bit Score: 156.69  E-value: 5.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759   165 AIWELLTTELTYVRKLKIMTDLLVsgllnLQRVELLTEVSAE--TLFGNIPSLIRVHKSFWEEVLGPTLEETRTSGRPld 242
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFL-----PPNSKPLSESEEEikTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDI-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759   243 pvslqngFLTFSQRFQPYVQYCLQVKRTMAYAREQQDNNPLFHAFVQWCEKHKRSGRQMLGDLLIKPHQRITKYPLLLQA 322
Cdd:pfam00621  74 -------FLKFAPGFKVYSTYCSNYPKALELLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKE 146
                         170       180       190
                  ....*....|....*....|....*....|
gi 73997759   323 VLKRSPEAHA-REALNTMIAAVESFLRHIN 351
Cdd:pfam00621 147 LLKHTPPDHPdYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
165-352 3.95e-41

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: 148.60  E-value: 3.95e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759    165 AIWELLTTELTYVRKLKIMTDLLVSGLLnlQRVELLTEVSAETLFGNIPSLIRVHKSFWEEVlgptleETRTSGRPLDPV 244
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLK--KELKLLSPNELETLFGNIEEIYEFHRDFLDEL------EERIEEWDDSVE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759    245 SLQNGFLTFSQRFQPYVQYCLQVKRTMAYaREQQDNNPLFHAFVQWCEKHKRSGRQMLGDLLIKPHQRITKYPLLLQAVL 324
Cdd:smart00325  73 RIGDVFLKLEEFFKIYSEYCSNHPDALEL-LKKLKKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELL 151
                          170       180
                   ....*....|....*....|....*....
gi 73997759    325 KRSPEAHA-REALNTMIAAVESFLRHINQ 352
Cdd:smart00325 152 KHTPEDHEdREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
162-351 1.88e-40

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: 146.67  E-value: 1.88e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759 162 QQEAIWELLTTELTYVRKLKIMTDLLVSGLLnlQRVELLTEVSAETLFGNIPSLIRVHKSFWEEVlgptleETRTSGRPL 241
Cdd:cd00160   1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLD--KELLPLSPEEVELLFGNIEEIYEFHRIFLKSL------EERVEEWDK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759 242 DPVSLQNGFLTFSQRFQPYVQYCLQVKRTMAYAREQQDNNPLFHAFVQWCEKhkRSGRQMLGDLLIKPHQRITKYPLLLQ 321
Cdd:cd00160  73 SGPRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAES--ECGRLKLESLLLKPVQRLTKYPLLLK 150
                       170       180       190
                ....*....|....*....|....*....|.
gi 73997759 322 AVLKRSPEAHA-REALNTMIAAVESFLRHIN 351
Cdd:cd00160 151 ELLKHTPDGHEdREDLKKALEAIKEVASQVN 181
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
143-468 3.59e-11

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 66.84  E-value: 3.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759  143 KSWKELVPghKEMSRELCHQ----QEAIWELLTTELTYVRKLKIMTDLLVsgllnlqrvELLTEVSAetlfgnIPS---- 214
Cdd:COG5422  464 NLWTLSVP--KEVWESLPKQeikrQEAIYEVIYTERDFVKDLEYLRDTWI---------KPLEESNI------IPEnarr 526
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759  215 -LIRVHKSFWEEVLGPT--LEETRTSGRPLDPV--SLQNGFLTFSQRFQPYVQYclqVKRTMAYARE---QQDNNPLFHA 286
Cdd:COG5422  527 nFIKHVFANINEIYAVNskLLKALTNRQCLSPIvnGIADIFLDYVPKFEPFIKY---GASQPYAKYEferEKSVNPNFAR 603
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759  287 FVQWCEKHKRSGRQMLGDLLIKPHQRITKYPLLLQAVLKRS-PEAHAREALNTMIAAVESFLRHINQQVRQGEEQESLVA 365
Cdd:COG5422  604 FDHEVERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTdPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLFH 683
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759  366 AAQRIgpyevlEPSSEEVEKNLRpfctldlmspmlgvasEHIRQLLLEGPVRVKEGR----EGKLDVYLFLFSDVLLVTK 441
Cdd:COG5422  684 LNQQL------LFKPEYVNLGLN----------------DEYRKIIFKGVLKRKAKSktdgSLRGDIQFFLLDNMLLFCK 741
                        330       340
                 ....*....|....*....|....*....
gi 73997759  442 PQRKADR--AKVIRPPLMLEKLVCQPLRD 468
Cdd:COG5422  742 AKAVNKWrqHKVFQRPIPLELLFISPDED 770
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
410-509 1.61e-05

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


Pssm-ID: 214574  Cd Length: 102  Bit Score: 44.46  E-value: 1.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759    410 LLLEGPVRVKE--GREGKLDVYLFLFSDVLLVTKpQRKADRAKVIRPPLMLEKLVCQPLRD------PNSFLVIHLTDFQ 481
Cdd:smart00233   1 VIKEGWLYKKSggGKKSWKKRYFVLFNSTLLYYK-SKKDKKSYKPKGSIDLSGCTVREAPDpdsskkPHCFEIKTSDRKT 79
                           90       100
                   ....*....|....*....|....*...
gi 73997759    482 cvssaFIVHCPSATDCAQWLKKTQQAQA 509
Cdd:smart00233  80 -----LLLQAESEEEREKWVEALRKAIA 102
PH pfam00169
PH domain; PH stands for pleckstrin homology.
410-507 1.91e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 395117 [Multi-domain]  Cd Length: 105  Bit Score: 38.31  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759   410 LLLEGPVRVKEGREGKL--DVYLFLFSDVLLVTKPqRKADRAKVIRPPLMLEKLVCQPLRD------PNSFLVIHLTdfQ 481
Cdd:pfam00169   1 VVKEGWLLKKGGGKKKSwkKRYFVLFDGSLLYYKD-DKSKKSKEPKGSISLSGCEVVEVVAsdspkrKFCFELRTGE--R 77
                          90       100
                  ....*....|....*....|....*.
gi 73997759   482 CVSSAFIVHCPSATDCAQWLKKTQQA 507
Cdd:pfam00169  78 TGKRTYLLQAESEEERKDWIKAIQSA 103
 
Name Accession Description Interval E-value
PH_PLEKHG5_G6 cd13244
Pleckstrin homology domain-containing family G member 5 and 6 pleckstrin homology (PH) domain; ...
408-506 4.17e-44

Pleckstrin homology domain-containing family G member 5 and 6 pleckstrin homology (PH) domain; PLEKHG5 has a RhoGEF DH/double-homology domain in tandem with a PH domain which is involved in phospholipid binding. PLEKHG5 activates the nuclear factor kappa B (NFKB1) signaling pathway. Mutations in PLEKHG5 are associated with autosomal recessive distal spinal muscular atrophy. PLEKHG6 (also called MyoGEF) has no known function to date. 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: 270064  Cd Length: 100  Bit Score: 153.92  E-value: 4.17e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759 408 RQLLLEGPVRVKEGREGKLDVYLFLFSDVLLVTKP-QRKADRAKVIRPPLMLEKLVCQPLRDPNSFLVIHLTDFQCVSSA 486
Cdd:cd13244   1 RRLLLEGDLRLKEGKGSKVDVHCFLFTDMLLICKPvKRKKDRLKVIRPPYLVDKLVVQELKDPGGFLLVYLNEFHTAVAA 80
                        90       100
                ....*....|....*....|
gi 73997759 487 FIVHCPSATDCAQWLKKTQQ 506
Cdd:cd13244  81 YTFQTSSQEDTRRWLDAIRK 100
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
165-351 5.50e-44

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: 425783 [Multi-domain]  Cd Length: 176  Bit Score: 156.69  E-value: 5.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759   165 AIWELLTTELTYVRKLKIMTDLLVsgllnLQRVELLTEVSAE--TLFGNIPSLIRVHKSFWEEVLGPTLEETRTSGRPld 242
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFL-----PPNSKPLSESEEEikTIFSNIEEIYELHRQLLLEELLKEWISIQRIGDI-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759   243 pvslqngFLTFSQRFQPYVQYCLQVKRTMAYAREQQDNNPLFHAFVQWCEKHKRSGRQMLGDLLIKPHQRITKYPLLLQA 322
Cdd:pfam00621  74 -------FLKFAPGFKVYSTYCSNYPKALELLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKE 146
                         170       180       190
                  ....*....|....*....|....*....|
gi 73997759   323 VLKRSPEAHA-REALNTMIAAVESFLRHIN 351
Cdd:pfam00621 147 LLKHTPPDHPdYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
165-352 3.95e-41

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: 148.60  E-value: 3.95e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759    165 AIWELLTTELTYVRKLKIMTDLLVSGLLnlQRVELLTEVSAETLFGNIPSLIRVHKSFWEEVlgptleETRTSGRPLDPV 244
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLK--KELKLLSPNELETLFGNIEEIYEFHRDFLDEL------EERIEEWDDSVE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759    245 SLQNGFLTFSQRFQPYVQYCLQVKRTMAYaREQQDNNPLFHAFVQWCEKHKRSGRQMLGDLLIKPHQRITKYPLLLQAVL 324
Cdd:smart00325  73 RIGDVFLKLEEFFKIYSEYCSNHPDALEL-LKKLKKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELL 151
                          170       180
                   ....*....|....*....|....*....
gi 73997759    325 KRSPEAHA-REALNTMIAAVESFLRHINQ 352
Cdd:smart00325 152 KHTPEDHEdREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
162-351 1.88e-40

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: 146.67  E-value: 1.88e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759 162 QQEAIWELLTTELTYVRKLKIMTDLLVSGLLnlQRVELLTEVSAETLFGNIPSLIRVHKSFWEEVlgptleETRTSGRPL 241
Cdd:cd00160   1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLD--KELLPLSPEEVELLFGNIEEIYEFHRIFLKSL------EERVEEWDK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759 242 DPVSLQNGFLTFSQRFQPYVQYCLQVKRTMAYAREQQDNNPLFHAFVQWCEKhkRSGRQMLGDLLIKPHQRITKYPLLLQ 321
Cdd:cd00160  73 SGPRIGDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAES--ECGRLKLESLLLKPVQRLTKYPLLLK 150
                       170       180       190
                ....*....|....*....|....*....|.
gi 73997759 322 AVLKRSPEAHA-REALNTMIAAVESFLRHIN 351
Cdd:cd00160 151 ELLKHTPDGHEdREDLKKALEAIKEVASQVN 181
PH_PLEKHG7 cd13245
Pleckstrin homology domain-containing family G member 7 pleckstrin homology (PH) domain; ...
409-505 1.75e-13

Pleckstrin homology domain-containing family G member 7 pleckstrin homology (PH) domain; PLEKHG7 has a RhoGEF DH/double-homology domain in tandem with a PH domain which is involved in phospholipid binding. PLEKHG7 is proposed to functions as a guanine nucleotide exchange factor (GEF) and is involved in the regulation of Rho protein signal transduction. 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: 270065  Cd Length: 128  Bit Score: 67.69  E-value: 1.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759 409 QLLLEGPVRVKEGreGK-LDVYLFLFSDVLLVTKPQRKADRAK------------------------VIRPPLMLEKLV- 462
Cdd:cd13245   1 QLLHEGPLTLIES--GKtLDVYLFLFDDMLLITKMKKNLKKKKssdsensmpsleltplikeggsytVYKQPIPLDRLCl 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 73997759 463 -------CQPLRDPNSFLVIHLTDFQCVSSAFIVHCPSATDCAQWLKKTQ 505
Cdd:cd13245  79 hdvdpneATANGLKHAFVLVHLNRYQQVIGVYTLQASSENTKQTWMSKLR 128
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
143-468 3.59e-11

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 66.84  E-value: 3.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759  143 KSWKELVPghKEMSRELCHQ----QEAIWELLTTELTYVRKLKIMTDLLVsgllnlqrvELLTEVSAetlfgnIPS---- 214
Cdd:COG5422  464 NLWTLSVP--KEVWESLPKQeikrQEAIYEVIYTERDFVKDLEYLRDTWI---------KPLEESNI------IPEnarr 526
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759  215 -LIRVHKSFWEEVLGPT--LEETRTSGRPLDPV--SLQNGFLTFSQRFQPYVQYclqVKRTMAYARE---QQDNNPLFHA 286
Cdd:COG5422  527 nFIKHVFANINEIYAVNskLLKALTNRQCLSPIvnGIADIFLDYVPKFEPFIKY---GASQPYAKYEferEKSVNPNFAR 603
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759  287 FVQWCEKHKRSGRQMLGDLLIKPHQRITKYPLLLQAVLKRS-PEAHAREALNTMIAAVESFLRHINQQVRQGEEQESLVA 365
Cdd:COG5422  604 FDHEVERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTdPDNPDTEDIPKVIDMLREFLSRLNFESGKAENRGDLFH 683
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759  366 AAQRIgpyevlEPSSEEVEKNLRpfctldlmspmlgvasEHIRQLLLEGPVRVKEGR----EGKLDVYLFLFSDVLLVTK 441
Cdd:COG5422  684 LNQQL------LFKPEYVNLGLN----------------DEYRKIIFKGVLKRKAKSktdgSLRGDIQFFLLDNMLLFCK 741
                        330       340
                 ....*....|....*....|....*....
gi 73997759  442 PQRKADR--AKVIRPPLMLEKLVCQPLRD 468
Cdd:COG5422  742 AKAVNKWrqHKVFQRPIPLELLFISPDED 770
PH_RARhoGAP cd13319
RA and RhoGAP domain-containing protein Pleckstrin homology PH domain; RARhoGAP (also called ...
408-442 4.53e-06

RA and RhoGAP domain-containing protein Pleckstrin homology PH domain; RARhoGAP (also called Rho GTPase-activating protein 20 and ARHGAP20 ) is thought to function in rearrangements of the cytoskeleton and cell signaling events that occur during spermatogenesis. RARhoGAP was also shown to be activated by Rap1 and to induce inactivation of Rho, resulting in the neurite outgrowth. Recent findings show that ARHGAP20, even although it is located in the middle of the MDR on 11q22-23, is expressed at higher levels in chronic lymphocytic leukemia patients with 11q22-23 and/or 13q14 deletions and its expression pattern suggests a functional link between cases with 11q22-23 and 13q14 deletions. The mechanism needs to be further studied. RARhoGAP contains a PH domain, a Ras-associating domain, a Rho-GAP domain, and ANXL repeats. 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: 270129  Cd Length: 97  Bit Score: 45.69  E-value: 4.53e-06
                        10        20        30
                ....*....|....*....|....*....|....*
gi 73997759 408 RQLLLEGPVRVKEGREGKlDVYLFLFSDVLLVTKP 442
Cdd:cd13319   1 RTFLLEGPVQLTRGLQTQ-ERHLFLFSDVLVVAKP 34
PH1_FGD5_FGD6 cd13389
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal ...
408-516 4.59e-06

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: 46.49  E-value: 4.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759 408 RQLLLEGPVrVKEGREGKLDVYLFLFSDVLLVTKPQRKADRAKVIRP-PLMLEKlVCQPLRD--PNSFLVIHltdfqcVS 484
Cdd:cd13389  12 RKLIKEGEL-MKVSRKEMQPRYFFLFNDCLLYTTPVQSSGMLKLNNElPLSGMK-VKLPEDEeySNEFQIIS------TK 83
                        90       100       110
                ....*....|....*....|....*....|..
gi 73997759 485 SAFIVHCPSATDCAQWLKKTQQAQATLQKLKA 516
Cdd:cd13389  84 RSFTLIASSEEERDEWVKALSRAIEEHTKKQR 115
PH_RalBD_exo84 cd01226
Exocyst complex 84-kDa subunit Ral-binding domain/Pleckstrin Homology (PH) domain; The Sec6/8 ...
408-513 8.09e-06

Exocyst complex 84-kDa subunit Ral-binding domain/Pleckstrin Homology (PH) domain; The Sec6/8 complex, also called the exocyst complex, forms an octameric protein (Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70 and Exo84) involved in the tethering of secretory vesicles to specific regions on the plasma membrane. The regulation of Sec6/8 complex differs between mammals and yeast. Mamalian Exo84 and Sec5 are effector targets for active Ral GTPases which are not present in yeast. Ral GTPases are members of the Ras superfamily, and as such cycle between an active GTP-bound state and an inactive GDP-bound state. The Exo84 Ral-binding domain adopts a PH domain fold. Mammalian Exo84 and Sec5 competitively bind to active RalA. 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: 269933  Cd Length: 115  Bit Score: 45.34  E-value: 8.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759 408 RQLLLEGPVRVKEGREGKL--DVYLFLFSDVLLVTKPqrKADRakviRPPLMLEKLVCQPLRDpnsFLVIHLTDFQCVSS 485
Cdd:cd01226   6 RYLLHEGDLLELDPDDYKPiqKVHLFLLNDVLLIASW--LPNR----RGPVRYKFQALYPLED---LAVVNVKDLGPVKN 76
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 73997759 486 AFIVH---------CPSATDCAQWLKKTQQA-QATLQK 513
Cdd:cd01226  77 AFKLLtfpetrvfqCENAKIKKEWLEKFEQAkRAKLAK 114
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
410-509 1.61e-05

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


Pssm-ID: 214574  Cd Length: 102  Bit Score: 44.46  E-value: 1.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759    410 LLLEGPVRVKE--GREGKLDVYLFLFSDVLLVTKpQRKADRAKVIRPPLMLEKLVCQPLRD------PNSFLVIHLTDFQ 481
Cdd:smart00233   1 VIKEGWLYKKSggGKKSWKKRYFVLFNSTLLYYK-SKKDKKSYKPKGSIDLSGCTVREAPDpdsskkPHCFEIKTSDRKT 79
                           90       100
                   ....*....|....*....|....*...
gi 73997759    482 cvssaFIVHCPSATDCAQWLKKTQQAQA 509
Cdd:smart00233  80 -----LLLQAESEEEREKWVEALRKAIA 102
PH_ephexin cd01221
Ephexin Pleckstrin homology (PH) domain; Ephexin-1 (also called NGEF/ neuronal guanine ...
402-501 4.46e-05

Ephexin Pleckstrin homology (PH) domain; Ephexin-1 (also called NGEF/ neuronal guanine nucleotide exchange factor) plays a role in the homeostatic modulation of presynaptic neurotransmitter release. Specific functions are still unknown for Ephexin-2 (also called RhoGEF19) and Ephexin-3 (also called Rho guanine nucleotide exchange factor 5/RhoGEF5, Transforming immortalized mammary oncogene/p60 TIM, and NGEF/neuronalGEF). Ephexin-4 (also called RhoGEF16) acts downstream of EphA2 to promote ligand-independent breast cancer cell migration and invasion toward epidermal growth factor through activation of RhoG. This in turn results in the activation of RhoG which recruits ELMO2 and Dock4 to form a complex with EphA2 at the tips of cortactin-rich protrusions in migrating breast cancer cells. Ephexin-5 is the specific GEF for RhoA activation and the regulation of vascular smooth muscle contractility. It interacts with EPHA4 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. The members of the Ephexin family contains a RhoGEF (DH) followed by a PH domain and an SH3 domain. The ephexin PH domain is believed to act with the DH domain in mediating protein-protein interactions. 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: 269929  Cd Length: 131  Bit Score: 43.78  E-value: 4.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759 402 VASEHiRQLLLEGPVRVKEGREGKL---------DVYLFLFSDVLLVTKP------------QRKADRAKVIRPPLMLEK 460
Cdd:cd01221   7 LISSS-RWLVKRGELTELVEDGGSLtfrkkfsktPVYLFLFNDLLLITKKkseerylvldyaPRNLVQVEEVEDPLQLPQ 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 73997759 461 LVCqplrdPNSFLVIHLTDFQCVSSAFIVHCPSATDCAQWL 501
Cdd:cd01221  86 PLG-----KNLFLLTLLENHEGKTVELLLSAESESDRERWL 121
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
412-502 1.03e-04

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: 41.76  E-value: 1.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759 412 LEGPVRVKEGREGKL--DVYLFLFSDVLLVTKPQRKADRA--KVIRPPLMLEKLVCQPLRDPNSFLVIHLTdfqcvSSAF 487
Cdd:cd00821   1 KEGYLLKRGGGGLKSwkKRWFVLFEGVLLYYKSKKDSSYKpkGSIPLSGILEVEEVSPKERPHCFELVTPD-----GRTY 75
                        90
                ....*....|....*
gi 73997759 488 IVHCPSATDCAQWLK 502
Cdd:cd00821  76 YLQADSEEERQEWLK 90
PH_Net1 cd13224
Neuroepithelial cell transforming 1 Pleckstrin homology (PH) domain; Net1 (also called ArhGEF8) ...
405-468 1.77e-04

Neuroepithelial cell transforming 1 Pleckstrin homology (PH) domain; Net1 (also called ArhGEF8) is part of the family of Rho guanine nucleotide exchange factors. Members of this family activate Rho proteins by catalyzing the exchange of GDP for GTP. The protein encoded by this gene interacts with RhoA within the cell nucleus and may play a role in repairing DNA damage after ionizing radiation. Net1 binds to caspase activation and recruitment domain (CARD)- and membrane-associated guanylate kinase-like domain-containing (CARMA) proteins and regulates nuclear factor kB activation. Net1 contains a RhoGEF domain N-terminal to a single PH domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270044  Cd Length: 135  Bit Score: 42.20  E-value: 1.77e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73997759 405 EHIRQLLLEGPVRVKEGREgkldVYLFLFSDVLLVTKPQRKADRA--KVIRPPLMLEKLVCQPLRD 468
Cdd:cd13224  15 ENSKALLCHGELRNKSGHK----LYVFLFQDILVLTRPVTRNERQsfQVYRQPIPVQELVLEDLQD 76
PH pfam00169
PH domain; PH stands for pleckstrin homology.
410-507 1.91e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 395117 [Multi-domain]  Cd Length: 105  Bit Score: 38.31  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759   410 LLLEGPVRVKEGREGKL--DVYLFLFSDVLLVTKPqRKADRAKVIRPPLMLEKLVCQPLRD------PNSFLVIHLTdfQ 481
Cdd:pfam00169   1 VVKEGWLLKKGGGKKKSwkKRYFVLFDGSLLYYKD-DKSKKSKEPKGSISLSGCEVVEVVAsdspkrKFCFELRTGE--R 77
                          90       100
                  ....*....|....*....|....*.
gi 73997759   482 CVSSAFIVHCPSATDCAQWLKKTQQA 507
Cdd:pfam00169  78 TGKRTYLLQAESEEERKDWIKAIQSA 103
PH_16 pfam17838
PH domain;
385-507 2.92e-03

PH domain;


Pssm-ID: 436083  Cd Length: 127  Bit Score: 38.54  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759   385 KNLRPFCTLDLMSpmlgvasehiRQLLLEGPVRVKEGREGKLDVYLFLFSD--VLLVTKPQRKA----------DRAKVI 452
Cdd:pfam17838   2 PLGEEFKKLDLTT----------RKLIHEGPLTWRNSKGKLVEVHALLLEDilVLLQEKDQKLVlaclstgsenVDQKTQ 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 73997759   453 RPPLMLEKL-VCQPLRDPNSFLVIHLtdfqCVSSAFI--VHCPSATDCAQWLKKTQQA 507
Cdd:pfam17838  72 SPIISLKKLiVREVATDKKAFFLIST----SPSDPQMyeLHASTKSERNTWTKLIQDA 125
PH_ITSN cd13264
Intersectin Pleckstrin homology (PH) domain; ITSNs, an adaptor protein family, play a role in ...
408-507 3.34e-03

Intersectin Pleckstrin homology (PH) domain; ITSNs, an adaptor protein family, play a role in endo- and exocytosis, actin cytoskeleton rearrangement and signal transduction. There are two human ITSN genes: ITSN1 and ITSN2. They share significant sequence identity and a similar domain structure having both short and long isoforms produced by alternative splicing. The short isoform (ITSN-S) consists of two Eps15 homology domains (EH1 and EH2), a coiled-coil region (CCR) and five Src homology 3 domains (SH3A-E). The EH domains bind to Asn-Pro-Phe motifs and are implicated in endocytosis and vesicle transport. The SH3 domains bind to proline-rich sequences and are commonly found in proteins implicated in cell signalling pathways, cytoskeletal organization and membrane traffic. The long isoform (ITSN-L) contains three additional C-terminal domains, a Dbl homology domain (DH), a Pleckstrin homology domain (PH) and a C2 domain. The tandem DH-PH domains are present in all Dbl family of GEFs. ITSN acts specifically on Cdc42 through its DH domain with no portion of the PH domain making contact with Cdc42. This is in contrast to Dbs which requires the PH domain for full catalytic activity. The ITSN PH domain binds phosphoinositides. C2 domains are usually involved in Ca2+-dependent and Ca2+-independent phospholipid binding. There are more than 30 proteins that interact with ITSNs. ITSN-S is present in mammals, frogs, flies and nematodes, while ITSN-L is present only in vertebrates. 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: 270084  Cd Length: 132  Bit Score: 38.59  E-value: 3.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73997759 408 RQLLLEGP-VRVKEGREgkldVYLFLFSDVLLVTKPQR---------KADRAKVI-----RPPLMLEKLVCQPLRDPNS- 471
Cdd:cd13264  14 RKFLHSGKlYKAKSNKE----LYGFLFNDFLLLTQPIKplgssgndfVFDNKANIqykmyKTPIFLNEVLVKLPTDPSGd 89
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 73997759 472 ---FLVIHLtDFQCVSSAfivhcPSATDCAQWLKKTQQA 507
Cdd:cd13264  90 epiFHISHI-DRVYTLRA-----ESINERTAWVQKIKAA 122
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH