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Conserved domains on  [gi|221513155|ref|NP_649182|]
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uncharacterized protein Dmel_CG42674, isoform C [Drosophila melanogaster]

Protein Classification

pleckstrin homology domain-containing family G protein( domain architecture ID 13218851)

pleckstrin homology (PH) domain-containing family G protein contains PH and RhoGEF domains, may function as a guanine nucleotide exchange factor; similar to Homo sapiens pleckstrin homology domain-containing family G member 5 (PLEKHG5) that functions as a guanine exchange factor (GEF) for RAB26 and thus regulates autophagy of synaptic vesicles in axon terminal of motoneurons

Gene Ontology:  GO:0005085|GO:0051056|GO:0007266
PubMed:  11738596

Graphical summary

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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; ...
1271-1366 8.42e-40

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: 142.75  E-value: 8.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155 1271 RHLFMEGDHKFKDNLG-KSDVHCFLLTDLLLVCKTIaKRGLGALKVIRQPYLTDQLIVQ-LAPNNTLNCVYLNEFQVATT 1348
Cdd:cd13244     1 RRLLLEGDLRLKEGKGsKVDVHCFLFTDMLLICKPV-KRKKDRLKVIRPPYLVDKLVVQeLKDPGGFLLVYLNEFHTAVA 79
                          90       100
                  ....*....|....*....|.
gi 221513155 1349 AFTLQCTEA---KNWYDALWR 1366
Cdd:cd13244    80 AYTFQTSSQedtRRWLDAIRK 100
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1027-1213 1.11e-28

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: 113.93  E-value: 1.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155  1027 AIWELVTTEVYYIHALQTVTDLFL----ACLEAVQEeglliDVDQarLFSNVRAVCEANIKFWtlwlypmvaHSAITHEP 1102
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLppnsKPLSESEE-----EIKT--IFSNIEEIYELHRQLL---------LEELLKEW 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155  1103 LRCAFFQEGFLSFASIFAPYKIYCAEQSTCQFYCKELNHNNALFTSYLAWCESQKMCNRLRLADIVVRPMQRLTKYSLLL 1182
Cdd:pfam00621   65 ISIQRIGDIFLKFAPGFKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLL 144
                          170       180       190
                   ....*....|....*....|....*....|..
gi 221513155  1183 AAIKKHMS-DVEEIEAIDVMMHSVENFVGSVN 1213
Cdd:pfam00621  145 KELLKHTPpDHPDYEDLKKALEAIKEVAKQIN 176
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
830-908 5.48e-09

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd17068:

Pssm-ID: 475130  Cd Length: 75  Bit Score: 54.12  E-value: 5.48e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221513155  830 DSSQQPDEEFIPATKGVTLLNALSHALRRRNLSFTQITItdnnptpsFLDAGPSLLPvsvdEQTDVESLAGHHLCITER 908
Cdd:cd17068     9 DDDDDDDVEIVPAVKGKTLRDVLEPLLERRGLDLDRVNV--------FLDSSNTPLP----LEFDTYFLGGHTLRVKAK 75
 
Name Accession Description Interval E-value
PH_PLEKHG5_G6 cd13244
Pleckstrin homology domain-containing family G member 5 and 6 pleckstrin homology (PH) domain; ...
1271-1366 8.42e-40

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: 142.75  E-value: 8.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155 1271 RHLFMEGDHKFKDNLG-KSDVHCFLLTDLLLVCKTIaKRGLGALKVIRQPYLTDQLIVQ-LAPNNTLNCVYLNEFQVATT 1348
Cdd:cd13244     1 RRLLLEGDLRLKEGKGsKVDVHCFLFTDMLLICKPV-KRKKDRLKVIRPPYLVDKLVVQeLKDPGGFLLVYLNEFHTAVA 79
                          90       100
                  ....*....|....*....|.
gi 221513155 1349 AFTLQCTEA---KNWYDALWR 1366
Cdd:cd13244    80 AYTFQTSSQedtRRWLDAIRK 100
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1027-1213 1.11e-28

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: 113.93  E-value: 1.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155  1027 AIWELVTTEVYYIHALQTVTDLFL----ACLEAVQEeglliDVDQarLFSNVRAVCEANIKFWtlwlypmvaHSAITHEP 1102
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLppnsKPLSESEE-----EIKT--IFSNIEEIYELHRQLL---------LEELLKEW 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155  1103 LRCAFFQEGFLSFASIFAPYKIYCAEQSTCQFYCKELNHNNALFTSYLAWCESQKMCNRLRLADIVVRPMQRLTKYSLLL 1182
Cdd:pfam00621   65 ISIQRIGDIFLKFAPGFKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLL 144
                          170       180       190
                   ....*....|....*....|....*....|..
gi 221513155  1183 AAIKKHMS-DVEEIEAIDVMMHSVENFVGSVN 1213
Cdd:pfam00621  145 KELLKHTPpDHPDYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1027-1213 2.94e-23

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: 98.53  E-value: 2.94e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155   1027 AIWELVTTEVYYIHALQTVTDLFLACLeaVQEEGLLIDVDQARLFSNVRAVCEANIKFWTLwLYPMVAHSAITHEPLrca 1106
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPL--KKELKLLSPNELETLFGNIEEIYEFHRDFLDE-LEERIEEWDDSVERI--- 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155   1107 ffQEGFLSFASIFAPYKIYCAEQSTCQFYCKELNHNNALFTsYLAWCESQKMCNRLRLADIVVRPMQRLTKYSLLLAAIK 1186
Cdd:smart00325   75 --GDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQK-FLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELL 151
                           170       180
                    ....*....|....*....|....*...
gi 221513155   1187 KHMS-DVEEIEAIDVMMHSVENFVGSVN 1213
Cdd:smart00325  152 KHTPeDHEDREDLKKALKAIKELANQVN 179
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1027-1213 7.20e-23

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: 97.37  E-value: 7.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155 1027 AIWELVTTEVYYIHALQTVTDLFLACLeaVQEEGLLIDVDQARLFSNVRAVCEANIKFWTLwLYPMVAHSAITHEPLrca 1106
Cdd:cd00160     4 VIKELLQTERNYVRDLKLLVEVFLKPL--DKELLPLSPEEVELLFGNIEEIYEFHRIFLKS-LEERVEEWDKSGPRI--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155 1107 ffQEGFLSFASIFAPYKIYCAEQSTCQFYCKELNHNNALFTSYLAWCESQkmCNRLRLADIVVRPMQRLTKYSLLLAAIK 1186
Cdd:cd00160    78 --GDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESE--CGRLKLESLLLKPVQRLTKYPLLLKELL 153
                         170       180
                  ....*....|....*....|....*...
gi 221513155 1187 KHMSDV-EEIEAIDVMMHSVENFVGSVN 1213
Cdd:cd00160   154 KHTPDGhEDREDLKKALEAIKEVASQVN 181
RBD_PLEKHG5 cd17068
Ras-binding domain (RBD) found in pleckstrin homology (PH) and RhoGEF domain containing G5 ...
830-908 5.48e-09

Ras-binding domain (RBD) found in pleckstrin homology (PH) and RhoGEF domain containing G5 (PLEKHG5) and similar proteins; PLEKHG5, is also termed PH domain-containing family G member 5, or guanine nucleotide exchange factor 720 (GEF720), Syx, or Tech, is a novel Dbl-like protein related to p115Rho-GEF. It functions as a Rho guanine nucleotide exchange factor directly activating RhoA in vivo and potentially involved in the control of neuronal cell differentiation. It also regulates the balance of the RhoA downstream effector Dia and ROCK activities to promote polarized-cancer-cell migration. Moreover, PLEKHG5 activates the nuclear factor kappaB (NFkappaB) signaling pathway. Mutations in the PLEKHG5 gene are relevant with autosomal recessive intermediate Charcot-Marie-Tooth disease (CMT) and lower motor neuron disease (LMND).


Pssm-ID: 340588  Cd Length: 75  Bit Score: 54.12  E-value: 5.48e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221513155  830 DSSQQPDEEFIPATKGVTLLNALSHALRRRNLSFTQITItdnnptpsFLDAGPSLLPvsvdEQTDVESLAGHHLCITER 908
Cdd:cd17068     9 DDDDDDDVEIVPAVKGKTLRDVLEPLLERRGLDLDRVNV--------FLDSSNTPLP----LEFDTYFLGGHTLRVKAK 75
 
Name Accession Description Interval E-value
PH_PLEKHG5_G6 cd13244
Pleckstrin homology domain-containing family G member 5 and 6 pleckstrin homology (PH) domain; ...
1271-1366 8.42e-40

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: 142.75  E-value: 8.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155 1271 RHLFMEGDHKFKDNLG-KSDVHCFLLTDLLLVCKTIaKRGLGALKVIRQPYLTDQLIVQ-LAPNNTLNCVYLNEFQVATT 1348
Cdd:cd13244     1 RRLLLEGDLRLKEGKGsKVDVHCFLFTDMLLICKPV-KRKKDRLKVIRPPYLVDKLVVQeLKDPGGFLLVYLNEFHTAVA 79
                          90       100
                  ....*....|....*....|.
gi 221513155 1349 AFTLQCTEA---KNWYDALWR 1366
Cdd:cd13244    80 AYTFQTSSQedtRRWLDAIRK 100
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
1027-1213 1.11e-28

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: 113.93  E-value: 1.11e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155  1027 AIWELVTTEVYYIHALQTVTDLFL----ACLEAVQEeglliDVDQarLFSNVRAVCEANIKFWtlwlypmvaHSAITHEP 1102
Cdd:pfam00621    1 VIKELLQTERSYVRDLEILVEVFLppnsKPLSESEE-----EIKT--IFSNIEEIYELHRQLL---------LEELLKEW 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155  1103 LRCAFFQEGFLSFASIFAPYKIYCAEQSTCQFYCKELNHNNALFTSYLAWCESQKMCNRLRLADIVVRPMQRLTKYSLLL 1182
Cdd:pfam00621   65 ISIQRIGDIFLKFAPGFKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLL 144
                          170       180       190
                   ....*....|....*....|....*....|..
gi 221513155  1183 AAIKKHMS-DVEEIEAIDVMMHSVENFVGSVN 1213
Cdd:pfam00621  145 KELLKHTPpDHPDYEDLKKALEAIKEVAKQIN 176
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
1027-1213 2.94e-23

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: 98.53  E-value: 2.94e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155   1027 AIWELVTTEVYYIHALQTVTDLFLACLeaVQEEGLLIDVDQARLFSNVRAVCEANIKFWTLwLYPMVAHSAITHEPLrca 1106
Cdd:smart00325    1 VLKELLQTERNYVRDLKLLVEVFLKPL--KKELKLLSPNELETLFGNIEEIYEFHRDFLDE-LEERIEEWDDSVERI--- 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155   1107 ffQEGFLSFASIFAPYKIYCAEQSTCQFYCKELNHNNALFTsYLAWCESQKMCNRLRLADIVVRPMQRLTKYSLLLAAIK 1186
Cdd:smart00325   75 --GDVFLKLEEFFKIYSEYCSNHPDALELLKKLKKNPRFQK-FLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELL 151
                           170       180
                    ....*....|....*....|....*...
gi 221513155   1187 KHMS-DVEEIEAIDVMMHSVENFVGSVN 1213
Cdd:smart00325  152 KHTPeDHEDREDLKKALKAIKELANQVN 179
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
1027-1213 7.20e-23

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: 97.37  E-value: 7.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155 1027 AIWELVTTEVYYIHALQTVTDLFLACLeaVQEEGLLIDVDQARLFSNVRAVCEANIKFWTLwLYPMVAHSAITHEPLrca 1106
Cdd:cd00160     4 VIKELLQTERNYVRDLKLLVEVFLKPL--DKELLPLSPEEVELLFGNIEEIYEFHRIFLKS-LEERVEEWDKSGPRI--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155 1107 ffQEGFLSFASIFAPYKIYCAEQSTCQFYCKELNHNNALFTSYLAWCESQkmCNRLRLADIVVRPMQRLTKYSLLLAAIK 1186
Cdd:cd00160    78 --GDVFLKLAPFFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESE--CGRLKLESLLLKPVQRLTKYPLLLKELL 153
                         170       180
                  ....*....|....*....|....*...
gi 221513155 1187 KHMSDV-EEIEAIDVMMHSVENFVGSVN 1213
Cdd:cd00160   154 KHTPDGhEDREDLKKALEAIKEVASQVN 181
RBD_PLEKHG5 cd17068
Ras-binding domain (RBD) found in pleckstrin homology (PH) and RhoGEF domain containing G5 ...
830-908 5.48e-09

Ras-binding domain (RBD) found in pleckstrin homology (PH) and RhoGEF domain containing G5 (PLEKHG5) and similar proteins; PLEKHG5, is also termed PH domain-containing family G member 5, or guanine nucleotide exchange factor 720 (GEF720), Syx, or Tech, is a novel Dbl-like protein related to p115Rho-GEF. It functions as a Rho guanine nucleotide exchange factor directly activating RhoA in vivo and potentially involved in the control of neuronal cell differentiation. It also regulates the balance of the RhoA downstream effector Dia and ROCK activities to promote polarized-cancer-cell migration. Moreover, PLEKHG5 activates the nuclear factor kappaB (NFkappaB) signaling pathway. Mutations in the PLEKHG5 gene are relevant with autosomal recessive intermediate Charcot-Marie-Tooth disease (CMT) and lower motor neuron disease (LMND).


Pssm-ID: 340588  Cd Length: 75  Bit Score: 54.12  E-value: 5.48e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221513155  830 DSSQQPDEEFIPATKGVTLLNALSHALRRRNLSFTQITItdnnptpsFLDAGPSLLPvsvdEQTDVESLAGHHLCITER 908
Cdd:cd17068     9 DDDDDDDVEIVPAVKGKTLRDVLEPLLERRGLDLDRVNV--------FLDSSNTPLP----LEFDTYFLGGHTLRVKAK 75
PH1_FGD5_FGD6 cd13389
FYVE, RhoGEF and PH domain containing/faciogenital dysplasia proteins 5 and 6, N-terminal ...
1271-1376 6.78e-04

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: 41.10  E-value: 6.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155 1271 RHLFMEGdhkfkdNLGKS------DVHCFLLTDLLLVCKTIakRGLGALKVIRQ---PYLTDQLIVQLApnntlncvYLN 1341
Cdd:cd13389    12 RKLIKEG------ELMKVsrkemqPRYFFLFNDCLLYTTPV--QSSGMLKLNNElplSGMKVKLPEDEE--------YSN 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 221513155 1342 EFQVATTA--FTL---QCTEAKNWYDALWRAKTIYQRLKR 1376
Cdd:cd13389    76 EFQIISTKrsFTLiasSEEERDEWVKALSRAIEEHTKKQR 115
PH_RalBD_exo84 cd01226
Exocyst complex 84-kDa subunit Ral-binding domain/Pleckstrin Homology (PH) domain; The Sec6/8 ...
1271-1315 5.46e-03

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: 38.41  E-value: 5.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 221513155 1271 RHLFMEGDHKFKD---NLGKSDVHCFLLTDLLLVCKTIA-KRGLGALKV 1315
Cdd:cd01226     6 RYLLHEGDLLELDpddYKPIQKVHLFLLNDVLLIASWLPnRRGPVRYKF 54
PH_PLEKHG7 cd13245
Pleckstrin homology domain-containing family G member 7 pleckstrin homology (PH) domain; ...
1286-1354 7.54e-03

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: 38.41  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221513155 1286 GKS-DVHCFLLTDLLLVCKTiaKRGLGALK------------------------VIRQPYLTDQLIV------QLAPNNT 1334
Cdd:cd13245    14 GKTlDVYLFLFDDMLLITKM--KKNLKKKKssdsensmpsleltplikeggsytVYKQPIPLDRLCLhdvdpnEATANGL 91
                          90       100
                  ....*....|....*....|...
gi 221513155 1335 LNC---VYLNEFQVATTAFTLQC 1354
Cdd:cd13245    92 KHAfvlVHLNRYQQVIGVYTLQA 114
 
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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