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Conserved domains on  [gi|2462568596|ref|XP_054178554|]
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rho guanine nucleotide exchange factor 1 isoform X4 [Homo sapiens]

Protein Classification

RGS_p115RhoGEF and PH_p115RhoGEF domain-containing protein( domain architecture ID 11580646)

protein containing domains RGS_p115RhoGEF, PHA03169, RhoGEF, and PH_p115RhoGEF

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RGS_p115RhoGEF cd08755
Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange ...
 67-259 1.41e-111

Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange factor (GEF), p115 RhoGEF; The RGS (Regulator of G-protein Signaling) domain is an essential part of the p115RhoGEF protein, a member of the RhoGEF (Rho guanine nucleotide exchange factor) subfamily of the RGS protein family. The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration, cell cycle progression of cells, and gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RhoGEF subfamily includes p115RhoGEF, LARG, PDZ-RhoGEF and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. In addition to being a G-alpha13/12 effector, the p115RhoGEF protein also functions as a GTPase-activating protein (GAP) for G-alpha13. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


:

Pssm-ID: 188709  Cd Length: 193  Bit Score: 342.26  E-value: 1.41e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  67 VKRRPAHLMALLQHVALQFEPGPLLCCLHADMLGSLGPKEAKKAFLDFYHSFLEKTAVLRVPVPPNVAFELDRTRADLIS 146
Cdd:cd08755     1 VKSRPAHLMVFLQHVMLQFDPAPLLCYLHADMLKNLNTKETKKHFGDFYNTFLEKGAVLKVSVPSNVAFELDRTRPELIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 147 EDVQRRFVQEVVQSQQVAVGRQLEDFRSKRLMGMTPWEQELAQLEAWVGRDRASYEARERHVAERLLMHLEEMQHTISTD 226
Cdd:cd08755    81 EEQQRRYVNEIQFAQSPAILRQLEDFRQKRMMGMTPNERELNDLESHRPTDRIPMEAKEKAVAESLLEKLVEMNPTIVPD 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462568596 227 EEKSAAVVNAIGLYMRHLGVRTKSGDKKSGRNF 259
Cdd:cd08755   161 EEKSNAIFGAIAYYMKHLGVKTKAFDNKKSKSG 193
PH_p115RhoGEF cd14679
Rho guanine nucleotide exchange factor Pleckstrin homology domain; p115RhoGEF (also called LSC, ...
 653-777 7.06e-71

Rho guanine nucleotide exchange factor Pleckstrin homology domain; p115RhoGEF (also called LSC, GEF1 or LBCL2) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. In addition to the Dbl homology (DH)-PH domain, p115RhoGEF contains an N-terminal RGS (Regulator of G-protein signalling) domain. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275429  Cd Length: 125  Bit Score: 230.50  E-value: 7.06e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 653 FKNLDITKKKLVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLKSHSRTLTPTPDGKTMLRPVLRLTSAMTRE 732
Cdd:cd14679     1 FKNIDITKKKLVHEGPLTWRVTKDKAIEVHVLLLDDLLVLLQKQDERLVLKCHSRTTTPTPDGKQMLSPIIKLNSAMTRE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462568596 733 VATDHKAFYVLFTWDQEAQIYELVAQTVSERKNWCALITETAGSL 777
Cdd:cd14679    81 VATDRKAFYVIFTWEQGAQIYELVAQTVSERKNWCALISETAGLL 125
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 435-619 7.20e-55

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: 188.28  E-value: 7.20e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  435 VISELLVTEAAHVRMLRVLHDLFFQPM-AECLFFPLEELQNIFPSLDELIEVHSLFLDRLMKRRQESGYLIEEIGDVLLA 513
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLkKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVERIGDVFLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  514 RfdgaegSWFQKISSRFCSRQSFALEQLKaKQRKDPRFCAFVQEAESRPRCRRLQLKDMIPTEMQRLTKYPLLLQSIGQN 593
Cdd:smart00325  81 L------EEFFKIYSEYCSNHPDALELLK-KLKKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKH 153

                          170       180
                   ....*....|....*....|....*..
gi 2462568596  594 TE-EPTEREKVELAAECCREILHHVNQ 619
Cdd:smart00325 154 TPeDHEDREDLKKALKAIKELANQVNE 180
PHA03169 super family cl27451
hypothetical protein; Provisional
 266-430 1.17e-03

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA03169:

Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.65  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 266 GNRRSDEPAKTKKGLSSIL-DAARWNRGEPQVPDfrhlkAEVDAEKPGATDRKGGVGMPSRDRNIGAPGQDTPGVSLHPL 344
Cdd:PHA03169   96 GSESVGSPTPSPSGSAEELaSGLSPENTSGSSPE-----SPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPS 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 345 SLDSPDR-EPGADAPLELGDSSPQGPMSLESLAPPESTDEGAETESPEPgDEGEPGRSGLELEPE-EPPGWRELVPPDTL 422
Cdd:PHA03169  171 HEDSPEEpEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTP-QQAPSPNTQQAVEHEdEPTEPEREGPPFPG 249


                  ....*...
gi 2462568596 423 HSLPKSQV 430
Cdd:PHA03169  250 HRSHSYTV 257
 
Name Accession Description Interval E-value
RGS_p115RhoGEF cd08755
Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange ...
 67-259 1.41e-111

Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange factor (GEF), p115 RhoGEF; The RGS (Regulator of G-protein Signaling) domain is an essential part of the p115RhoGEF protein, a member of the RhoGEF (Rho guanine nucleotide exchange factor) subfamily of the RGS protein family. The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration, cell cycle progression of cells, and gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RhoGEF subfamily includes p115RhoGEF, LARG, PDZ-RhoGEF and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. In addition to being a G-alpha13/12 effector, the p115RhoGEF protein also functions as a GTPase-activating protein (GAP) for G-alpha13. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188709  Cd Length: 193  Bit Score: 342.26  E-value: 1.41e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  67 VKRRPAHLMALLQHVALQFEPGPLLCCLHADMLGSLGPKEAKKAFLDFYHSFLEKTAVLRVPVPPNVAFELDRTRADLIS 146
Cdd:cd08755     1 VKSRPAHLMVFLQHVMLQFDPAPLLCYLHADMLKNLNTKETKKHFGDFYNTFLEKGAVLKVSVPSNVAFELDRTRPELIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 147 EDVQRRFVQEVVQSQQVAVGRQLEDFRSKRLMGMTPWEQELAQLEAWVGRDRASYEARERHVAERLLMHLEEMQHTISTD 226
Cdd:cd08755    81 EEQQRRYVNEIQFAQSPAILRQLEDFRQKRMMGMTPNERELNDLESHRPTDRIPMEAKEKAVAESLLEKLVEMNPTIVPD 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462568596 227 EEKSAAVVNAIGLYMRHLGVRTKSGDKKSGRNF 259
Cdd:cd08755   161 EEKSNAIFGAIAYYMKHLGVKTKAFDNKKSKSG 193
RGS-like pfam09128
Regulator of G protein signalling-like domain; Members of this family adopt a structure ...
 57-247 2.41e-84

Regulator of G protein signalling-like domain; Members of this family adopt a structure consisting of twelve helices that fold into a compact domain that contains the overall structural scaffold observed in other RGS proteins and three additional helical elements that pack closely to it. Helices 1-9 comprise the RGS (pfam00615) fold, in which helices 4-7 form a classic antiparallel bundle adjacent to the other helices. Like other RGS structures, helices 7 and 8 span the length of the folded domain and form essentially one continuous helix with a kink in the middle. Helices 10-12 form an apparently stable C-terminal extension of the structural domain, and although other RGS proteins lack this structure, these elements are intimately associated with the rest of the structural framework by hydrophobic interactions. Members of the family bind to active G-alpha proteins, promoting GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways.


Pssm-ID: 462687  Cd Length: 191  Bit Score: 269.75  E-value: 2.41e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  57 QNSQFQSLEQVKRRPAHLMALLQHVALQFEPGPLLCCLHADMLGSLGPKEAKKAFLDFYHSFLEKTAVLRVPVPPNVAFE 136
Cdd:pfam09128   1 QCSCFQSLEQLKSRPAHLAVFLHHVVSQFDPSPLLCYLYADLYQQTNSKETRRVFLDIHNFFLEKNAPLRVPVPESVAAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 137 LDRTRADLISEDVQRRFVQEVVQSQQVAVGRQLEDFRSKRLMGMTPWEQELAQLEAWVGRDRASYEaRERHVAERLLMHL 216
Cdd:pfam09128  81 LDRRRPELIPEDLHRRYIQTMQERAVPDIQRQLEDFRQKRSMGLTLAEGELSLLDAERDGDRGTLE-RERRVAEQILSKI 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462568596 217 EEMQHTIST-DEEKSAAVVNAIGLYMRHLGVR 247
Cdd:pfam09128 160 EEILSTSQTfDEERSATIQYVILTYMKHLGVR 191
PH_p115RhoGEF cd14679
Rho guanine nucleotide exchange factor Pleckstrin homology domain; p115RhoGEF (also called LSC, ...
 653-777 7.06e-71

Rho guanine nucleotide exchange factor Pleckstrin homology domain; p115RhoGEF (also called LSC, GEF1 or LBCL2) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. In addition to the Dbl homology (DH)-PH domain, p115RhoGEF contains an N-terminal RGS (Regulator of G-protein signalling) domain. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275429  Cd Length: 125  Bit Score: 230.50  E-value: 7.06e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 653 FKNLDITKKKLVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLKSHSRTLTPTPDGKTMLRPVLRLTSAMTRE 732
Cdd:cd14679     1 FKNIDITKKKLVHEGPLTWRVTKDKAIEVHVLLLDDLLVLLQKQDERLVLKCHSRTTTPTPDGKQMLSPIIKLNSAMTRE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462568596 733 VATDHKAFYVLFTWDQEAQIYELVAQTVSERKNWCALITETAGSL 777
Cdd:cd14679    81 VATDRKAFYVIFTWEQGAQIYELVAQTVSERKNWCALISETAGLL 125
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 435-619 7.20e-55

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: 188.28  E-value: 7.20e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  435 VISELLVTEAAHVRMLRVLHDLFFQPM-AECLFFPLEELQNIFPSLDELIEVHSLFLDRLMKRRQESGYLIEEIGDVLLA 513
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLkKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVERIGDVFLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  514 RfdgaegSWFQKISSRFCSRQSFALEQLKaKQRKDPRFCAFVQEAESRPRCRRLQLKDMIPTEMQRLTKYPLLLQSIGQN 593
Cdd:smart00325  81 L------EEFFKIYSEYCSNHPDALELLK-KLKKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKH 153

                          170       180
                   ....*....|....*....|....*..
gi 2462568596  594 TE-EPTEREKVELAAECCREILHHVNQ 619
Cdd:smart00325 154 TPeDHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 432-618 4.36e-52

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: 180.57  E-value: 4.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 432 RQEVISELLVTEAAHVRMLRVLHDLFFQPMAEC-LFFPLEELQNIFPSLDELIEVHSLFLDRLMKRRQESGYLIEEIGDV 510
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKElLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGPRIGDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 511 LLARFDgaegswFQKISSRFCSRQSFALEQLKAKQRKDPRFCAFVQEAESRprCRRLQLKDMIPTEMQRLTKYPLLLQSI 590
Cdd:cd00160    81 FLKLAP------FFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESE--CGRLKLESLLLKPVQRLTKYPLLLKEL 152

                         170       180
                  ....*....|....*....|....*....
gi 2462568596 591 GQNTEE-PTEREKVELAAECCREILHHVN 618
Cdd:cd00160   153 LKHTPDgHEDREDLKKALEAIKEVASQVN 181
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 435-618 2.23e-46

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: 164.01  E-value: 2.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 435 VISELLVTEAAHVRMLRVLHDLFFQPMAECLFFPLEELQNIFPSLDELIEVHSlflDRLMKRRQESGYLIEEIGDVLLAR 514
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHR---QLLLEELLKEWISIQRIGDIFLKF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 515 FDgaegswFQKISSRFCSRQSFALEQLKAKQRKDPRFCAFVQEAESRPRCRRLQLKDMIPTEMQRLTKYPLLLQSIGQNT 594
Cdd:pfam00621  78 AP------GFKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHT 151

                         170       180
                  ....*....|....*....|....*
gi 2462568596 595 EEPT-EREKVELAAECCREILHHVN 618
Cdd:pfam00621 152 PPDHpDYEDLKKALEAIKEVAKQIN 176
PH_16 pfam17838
PH domain;
647-775 3.10e-38

PH domain;


Pssm-ID: 436083  Cd Length: 127  Bit Score: 138.69  E-value: 3.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 647 DPMLSEFKNLDITKKKLVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLKSHSrTLTPTPDGKtMLRPVLRLT 726
Cdd:pfam17838   1 HPLGEEFKKLDLTTRKLIHEGPLTWRNSKGKLVEVHALLLEDILVLLQEKDQKLVLACLS-TGSENVDQK-TQSPIISLK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462568596 727 SAMTREVATDHKAFYVLFTWDQEAQIYELVAQTVSERKNWCALITETAG 775
Cdd:pfam17838  79 KLIVREVATDKKAFFLISTSPSDPQMYELHASTKSERNTWTKLIQDAIE 127
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 403-672 2.37e-16

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 84.56  E-value: 2.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  403 LELEPEEPPGWRELVPPDTLHSLPKSQVKRQEVISELLVTEAAHVRMLRVLHDLFFQPMAECLFFPLEELQN----IFPS 478
Cdd:COG5422    456 LDKFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIPENARRNfikhVFAN 535

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  479 LDELIEVHSLFLDRLmKRRQESGYLIEEIGDVLLARFdgaegSWFQKISSRFCSRQsfALEQLKAKQRK-DPRFCAFVQE 557
Cdd:COG5422    536 INEIYAVNSKLLKAL-TNRQCLSPIVNGIADIFLDYV-----PKFEPFIKYGASQP--YAKYEFEREKSvNPNFARFDHE 607

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  558 AESRPRCRRLQLKDMIPTEMQRLTKYPLLLQSIGQNTEE-PTEREKVELAAECCREILHHVNQAVRDMEDllrlkdyqrR 636
Cdd:COG5422    608 VERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPdNPDTEDIPKVIDMLREFLSRLNFESGKAEN---------R 678

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462568596  637 LDLSHLRQSSdPMLSEFKNLDI--TKKKLVHEGPLTWR 672
Cdd:COG5422    679 GDLFHLNQQL-LFKPEYVNLGLndEYRKIIFKGVLKRK 715
PHA03169 PHA03169
hypothetical protein; Provisional
 266-430 1.17e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.65  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 266 GNRRSDEPAKTKKGLSSIL-DAARWNRGEPQVPDfrhlkAEVDAEKPGATDRKGGVGMPSRDRNIGAPGQDTPGVSLHPL 344
Cdd:PHA03169   96 GSESVGSPTPSPSGSAEELaSGLSPENTSGSSPE-----SPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPS 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 345 SLDSPDR-EPGADAPLELGDSSPQGPMSLESLAPPESTDEGAETESPEPgDEGEPGRSGLELEPE-EPPGWRELVPPDTL 422
Cdd:PHA03169  171 HEDSPEEpEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTP-QQAPSPNTQQAVEHEdEPTEPEREGPPFPG 249


                  ....*...
gi 2462568596 423 HSLPKSQV 430
Cdd:PHA03169  250 HRSHSYTV 257
 
Name Accession Description Interval E-value
RGS_p115RhoGEF cd08755
Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange ...
 67-259 1.41e-111

Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange factor (GEF), p115 RhoGEF; The RGS (Regulator of G-protein Signaling) domain is an essential part of the p115RhoGEF protein, a member of the RhoGEF (Rho guanine nucleotide exchange factor) subfamily of the RGS protein family. The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration, cell cycle progression of cells, and gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RhoGEF subfamily includes p115RhoGEF, LARG, PDZ-RhoGEF and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. In addition to being a G-alpha13/12 effector, the p115RhoGEF protein also functions as a GTPase-activating protein (GAP) for G-alpha13. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188709  Cd Length: 193  Bit Score: 342.26  E-value: 1.41e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  67 VKRRPAHLMALLQHVALQFEPGPLLCCLHADMLGSLGPKEAKKAFLDFYHSFLEKTAVLRVPVPPNVAFELDRTRADLIS 146
Cdd:cd08755     1 VKSRPAHLMVFLQHVMLQFDPAPLLCYLHADMLKNLNTKETKKHFGDFYNTFLEKGAVLKVSVPSNVAFELDRTRPELIN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 147 EDVQRRFVQEVVQSQQVAVGRQLEDFRSKRLMGMTPWEQELAQLEAWVGRDRASYEARERHVAERLLMHLEEMQHTISTD 226
Cdd:cd08755    81 EEQQRRYVNEIQFAQSPAILRQLEDFRQKRMMGMTPNERELNDLESHRPTDRIPMEAKEKAVAESLLEKLVEMNPTIVPD 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2462568596 227 EEKSAAVVNAIGLYMRHLGVRTKSGDKKSGRNF 259
Cdd:cd08755   161 EEKSNAIFGAIAYYMKHLGVKTKAFDNKKSKSG 193
RGS-like pfam09128
Regulator of G protein signalling-like domain; Members of this family adopt a structure ...
 57-247 2.41e-84

Regulator of G protein signalling-like domain; Members of this family adopt a structure consisting of twelve helices that fold into a compact domain that contains the overall structural scaffold observed in other RGS proteins and three additional helical elements that pack closely to it. Helices 1-9 comprise the RGS (pfam00615) fold, in which helices 4-7 form a classic antiparallel bundle adjacent to the other helices. Like other RGS structures, helices 7 and 8 span the length of the folded domain and form essentially one continuous helix with a kink in the middle. Helices 10-12 form an apparently stable C-terminal extension of the structural domain, and although other RGS proteins lack this structure, these elements are intimately associated with the rest of the structural framework by hydrophobic interactions. Members of the family bind to active G-alpha proteins, promoting GTP hydrolysis by the alpha subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor signalling pathways.


Pssm-ID: 462687  Cd Length: 191  Bit Score: 269.75  E-value: 2.41e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  57 QNSQFQSLEQVKRRPAHLMALLQHVALQFEPGPLLCCLHADMLGSLGPKEAKKAFLDFYHSFLEKTAVLRVPVPPNVAFE 136
Cdd:pfam09128   1 QCSCFQSLEQLKSRPAHLAVFLHHVVSQFDPSPLLCYLYADLYQQTNSKETRRVFLDIHNFFLEKNAPLRVPVPESVAAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 137 LDRTRADLISEDVQRRFVQEVVQSQQVAVGRQLEDFRSKRLMGMTPWEQELAQLEAWVGRDRASYEaRERHVAERLLMHL 216
Cdd:pfam09128  81 LDRRRPELIPEDLHRRYIQTMQERAVPDIQRQLEDFRQKRSMGLTLAEGELSLLDAERDGDRGTLE-RERRVAEQILSKI 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462568596 217 EEMQHTIST-DEEKSAAVVNAIGLYMRHLGVR 247
Cdd:pfam09128 160 EEILSTSQTfDEERSATIQYVILTYMKHLGVR 191
PH_p115RhoGEF cd14679
Rho guanine nucleotide exchange factor Pleckstrin homology domain; p115RhoGEF (also called LSC, ...
 653-777 7.06e-71

Rho guanine nucleotide exchange factor Pleckstrin homology domain; p115RhoGEF (also called LSC, GEF1 or LBCL2) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. In addition to the Dbl homology (DH)-PH domain, p115RhoGEF contains an N-terminal RGS (Regulator of G-protein signalling) domain. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275429  Cd Length: 125  Bit Score: 230.50  E-value: 7.06e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 653 FKNLDITKKKLVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLKSHSRTLTPTPDGKTMLRPVLRLTSAMTRE 732
Cdd:cd14679     1 FKNIDITKKKLVHEGPLTWRVTKDKAIEVHVLLLDDLLVLLQKQDERLVLKCHSRTTTPTPDGKQMLSPIIKLNSAMTRE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462568596 733 VATDHKAFYVLFTWDQEAQIYELVAQTVSERKNWCALITETAGSL 777
Cdd:cd14679    81 VATDRKAFYVIFTWEQGAQIYELVAQTVSERKNWCALISETAGLL 125
RhoGEF smart00325
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Guanine nucleotide exchange ...
 435-619 7.20e-55

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: 188.28  E-value: 7.20e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  435 VISELLVTEAAHVRMLRVLHDLFFQPM-AECLFFPLEELQNIFPSLDELIEVHSLFLDRLMKRRQESGYLIEEIGDVLLA 513
Cdd:smart00325   1 VLKELLQTERNYVRDLKLLVEVFLKPLkKELKLLSPNELETLFGNIEEIYEFHRDFLDELEERIEEWDDSVERIGDVFLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  514 RfdgaegSWFQKISSRFCSRQSFALEQLKaKQRKDPRFCAFVQEAESRPRCRRLQLKDMIPTEMQRLTKYPLLLQSIGQN 593
Cdd:smart00325  81 L------EEFFKIYSEYCSNHPDALELLK-KLKKNPRFQKFLKEIESSPQCRRLTLESLLLKPVQRLTKYPLLLKELLKH 153

                          170       180
                   ....*....|....*....|....*..
gi 2462568596  594 TE-EPTEREKVELAAECCREILHHVNQ 619
Cdd:smart00325 154 TPeDHEDREDLKKALKAIKELANQVNE 180
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
 432-618 4.36e-52

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: 180.57  E-value: 4.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 432 RQEVISELLVTEAAHVRMLRVLHDLFFQPMAEC-LFFPLEELQNIFPSLDELIEVHSLFLDRLMKRRQESGYLIEEIGDV 510
Cdd:cd00160     1 RQEVIKELLQTERNYVRDLKLLVEVFLKPLDKElLPLSPEEVELLFGNIEEIYEFHRIFLKSLEERVEEWDKSGPRIGDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 511 LLARFDgaegswFQKISSRFCSRQSFALEQLKAKQRKDPRFCAFVQEAESRprCRRLQLKDMIPTEMQRLTKYPLLLQSI 590
Cdd:cd00160    81 FLKLAP------FFKIYSEYCSNHPDALELLKKLKKFNKFFQEFLEKAESE--CGRLKLESLLLKPVQRLTKYPLLLKEL 152

                         170       180
                  ....*....|....*....|....*....
gi 2462568596 591 GQNTEE-PTEREKVELAAECCREILHHVN 618
Cdd:cd00160   153 LKHTPDgHEDREDLKKALEAIKEVASQVN 181
RGS_LARG cd08754
Regulator of G protein signaling (RGS) domain found in the leukemia-associated Rho guanine ...
 38-249 6.93e-52

Regulator of G protein signaling (RGS) domain found in the leukemia-associated Rho guanine nucleotide exchange factor (RhoGEF) protein (LARG); The RGS domain is an essential part of the leukemia-associated RhoGEF protein (LARG), a member of the RhoGEF (Rho guanine nucleotide exchange factor) subfamily of the RGS protein family. The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration, cell cycle progression of cells, and gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RhoGEF subfamily includes p115RhoGEF, LARG, PDZ-RhoGEF, and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. In addition to being a G-alpha13 effector, the LARG protein also functions as a GTPase-activating protein (GAP) for G-alpha13. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188708  Cd Length: 222  Bit Score: 181.35  E-value: 6.93e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  38 IIGAEDEDFENEletnSEEQNSQ---FQSLEQVKRRPAHLMALLQHVALQFEPGPLLCCLHADMLGSLGPKEAKKAFLDF 114
Cdd:cd08754     2 IIGAEDDDFPTE----SEQINGQcscFQNIELLKSRPAHLAVFLHHVVSQFDPAALLCYLYADLYKQTNSKETRRVFLEF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 115 YHSFLEKTAVLRVPVPPNVAFELDRTRADLISEDVQRRFVQEVVQSQQVAVGRQLEDFRSKRLMGMTPWEQELAQLEAWV 194
Cdd:cd08754    78 NQFFLDRAANLKVPVPDEVSLDLEKRRPELIPEELHRHYIQTMQERVSPEVQRNLEDFRQKRSMGLTLAEGELTKLDAER 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462568596 195 GRDRASYEaRERHVAERLLMHLEEMQHTIST-DEEKSAAVVNAIGLYMRHLGVRTK 249
Cdd:cd08754   158 FRDRNTIE-KERACAEQIVAKIEEVLMTSQTpEEDKSSTIQYVILTYMKHLGVKVK 212
RhoGEF pfam00621
RhoGEF domain; Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases Also called ...
 435-618 2.23e-46

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: 164.01  E-value: 2.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 435 VISELLVTEAAHVRMLRVLHDLFFQPMAECLFFPLEELQNIFPSLDELIEVHSlflDRLMKRRQESGYLIEEIGDVLLAR 514
Cdd:pfam00621   1 VIKELLQTERSYVRDLEILVEVFLPPNSKPLSESEEEIKTIFSNIEEIYELHR---QLLLEELLKEWISIQRIGDIFLKF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 515 FDgaegswFQKISSRFCSRQSFALEQLKAKQRKDPRFCAFVQEAESRPRCRRLQLKDMIPTEMQRLTKYPLLLQSIGQNT 594
Cdd:pfam00621  78 AP------GFKVYSTYCSNYPKALKLLKKLLKKNPKFRAFLEELEANPECRGLDLNSFLIKPVQRIPRYPLLLKELLKHT 151

                         170       180
                  ....*....|....*....|....*
gi 2462568596 595 EEPT-EREKVELAAECCREILHHVN 618
Cdd:pfam00621 152 PPDHpDYEDLKKALEAIKEVAKQIN 176
PH_LARG cd13390
Leukemia-associated Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; ...
 638-775 3.83e-46

Leukemia-associated Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; LARG (also called RhoGEF12) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. RhoGEFs activate Rho GTPases regulating cytoskeletal structure, gene transcription, and cell migration. LARG contains a N-terminal extension, followed by Dbl homology (DH)-PH domains which bind and catalyze the exchange of GDP for GTP on RhoA in addition to a RGS domain. The active site of RhoA adopts two distinct GDP-excluding conformations among the four unique complexes in the asymmetric unit. The LARG PH domain also contains a potential protein-docking site. LARG forms a homotetramer via its DH domains. 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: 275425  Cd Length: 138  Bit Score: 162.08  E-value: 3.83e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 638 DLSHLRQSSDPMLSEFKNLDITKKKLVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLKSHSRTLTPTPDGKT 717
Cdd:cd13390     1 DLSSLKQSEYPMIDELRNLDLTKRKMIHEGPLTWKVNRDKTIDLYTLLLEDILVLLQKQDDRLVLRCHSKILASTADSKH 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462568596 718 MLRPVLRLTSAMTREVATDHKAFYVLFTWDQEAQIYELVAQTVSERKNWCALITETAG 775
Cdd:cd13390    81 TFSPVIKLNTVLVRQVATDNKAFFVISMSENGAQIYELVAQTVSEKTVWQDLITRMAA 138
RGS_RhoGEF-like cd08736
Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange ...
 68-187 8.23e-46

Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange factor (RhoGEF) protein; The RGS domain found in the Rho guanine nucleotide exchange factor (RhoGEF) protein subfamily of the RGS domain containing protein family, which is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). RhoGEFs link signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RGS domain of the RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and therefore is often refered to as the RH (RGS Homology) domain. The RGS-GEFs subfamily includes the leukemia-associated RhoGEF (LARG), p115RhoGEF, and PDZ-RhoGEF. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188690  Cd Length: 120  Bit Score: 160.11  E-value: 8.23e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  68 KRRPAHLMALLQHVALQFEPGPLLCCLHADMLGSLGPKEAKKAFLDFYHSFLEKTAVLRVPVPPNVAFELDRTRADLISE 147
Cdd:cd08736     1 KSRPAHLAVFLHYVLSQFDPSPLLFYLITDLYKQGNPKDMRKWAYEIYSTFLEKNAPLKVKVPESLAAEIDKRLPNLIDE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462568596 148 DVQRRFVQEVVQSQQVAVGRQLEDFRSKRLMGMTPWEQEL 187
Cdd:cd08736    81 EDLRRVFQEAQERAMPEIQEQLEDFRQKRTMGLGSLEGEL 120
PH_PRG cd13391
PDZ Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; PRG (also called ...
 636-772 4.55e-45

PDZ Rho guanine nucleotide exchange factor Pleckstrin homology (PH) domain; PRG (also called RhoGEF11) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. RhoGEFs activate Rho GTPases regulating cytoskeletal structure, gene transcription, and cell migration. PRG contains an N-terminal PDZ domain, a regulators of G-protein signaling-like (RGSL) domain, a linker region, and a C-terminal Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. As is the case in p115-RhoGEF, it is thought that the PRG activated by relieving autoinhibition caused by the linker region. 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: 275426  Cd Length: 142  Bit Score: 159.04  E-value: 4.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 636 RLDLSHLRQSSDPMLSEFKNLDITKKKLVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLKSHSRTLTPTPDG 715
Cdd:cd13391     1 RLDATALERASNPLAAEFKNLDLTTRRMIHEGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLVLKCHSKTAVGSSDS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462568596 716 KTMLRPVLRLTSAMTREVATDHKAFYVLFTWDQEAQIYELVAQTVSERKNWCALITE 772
Cdd:cd13391    81 KQTFSPVLKLNSVLIRSVATDKRALFIICTSKLGPQIYELVALTSSEKNTWMELLEE 137
PH_16 pfam17838
PH domain;
647-775 3.10e-38

PH domain;


Pssm-ID: 436083  Cd Length: 127  Bit Score: 138.69  E-value: 3.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 647 DPMLSEFKNLDITKKKLVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLKSHSrTLTPTPDGKtMLRPVLRLT 726
Cdd:pfam17838   1 HPLGEEFKKLDLTTRKLIHEGPLTWRNSKGKLVEVHALLLEDILVLLQEKDQKLVLACLS-TGSENVDQK-TQSPIISLK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462568596 727 SAMTREVATDHKAFYVLFTWDQEAQIYELVAQTVSERKNWCALITETAG 775
Cdd:pfam17838  79 KLIVREVATDKKAFFLISTSPSDPQMYELHASTKSERNTWTKLIQDAIE 127
PH_RhoGEF cd13329
Rho guanine nucleotide exchange factor Pleckstrin homology domain; RhoGEFs belongs to ...
 663-774 7.52e-38

Rho guanine nucleotide exchange factor Pleckstrin homology domain; RhoGEFs belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. The members here all contain Dbl homology (DH)-PH domains. In addition some members contain N-terminal C1 (Protein kinase C conserved region 1) domains, PDZ (also called DHR/Dlg homologous regions) domains, ANK (ankyrin) domains, and RGS (Regulator of G-protein signalling) domains or C-terminal ATP-synthase B subunit. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. RhoGEF2/Rho guanine nucleotide exchange factor 2, p114RhoGEF/p114 Rho guanine nucleotide exchange factor, p115RhoGEF, p190RhoGEF, PRG/PDZ Rho guanine nucleotide exchange factor, RhoGEF 11, RhoGEF 12, RhoGEF 18, AKAP13/A-kinase anchoring protein 13, and LARG/Leukemia-associated Rho guanine nucleotide exchange factor are included in this CD. 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: 275411  Cd Length: 109  Bit Score: 137.01  E-value: 7.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 663 LVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLKSHsrtLTPTPDGKTMLRPVLRLTSAMTREVATDHKAFYV 742
Cdd:cd13329     1 LIHEGPLTWKVARGKLIEVHVLLLEDLLVLLQKQDDKYLLKLH---LTGSFDSKDTKSPVIKLSTLLVREVATDKKAFFL 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462568596 743 LFTWDQEAQIYELVAQTVSERKNWCALITETA 774
Cdd:cd13329    78 ISTSKNGPQMYELVANSSSERKTWIKHISDAV 109
RGS_PDZRhoGEF cd08753
Regulator of G protein signaling (RGS) domain found in the PDZ-Rho guanine nucleotide exchange ...
 38-180 2.62e-17

Regulator of G protein signaling (RGS) domain found in the PDZ-Rho guanine nucleotide exchange factor (RhoGEF) protein; The RGS domain is an essential part of the PDZ-RhoGEF (PDZ:Postsynaptic density 95, Disk large, Zona occludens-1; RhoGEF: Rho guanine nucleotide exchange factor; alias PRG) protein, a member of RhoGEFs subfamily of the RGS protein family. The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration, and cell cycle progression, as well as gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. RhoGEFs subfamily includes leukemia-associated RhoGEF protein (LARG), p115RhoGEF, PDZ-RhoGEF and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. In contrast to p115RhoGEF and LARG, PDZ-RhoGEF cannot serve as a GTPase-activating protein (GAP), due to the mutation of sites in the RGS domain region that are crucial for GAP activity. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188707  Cd Length: 145  Bit Score: 79.53  E-value: 2.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  38 IIGAEdEDFENELETNseEQNSQFQSLEQVKRRPAHLMALLQHVALQFEPGPLLCCLHADMLGSLGPKEAKKAFLDFYHS 117
Cdd:cd08753     2 IIGPE-EDYDPGYFNN--ESDIIFQDLEKLKSRPAHLVVFLRYIFSQADPGPLLFYLCSEVYQQTSPKDSRSLGKDIWNI 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462568596 118 FLEKTAVLRVPVPPNVAFELD-RTRAdliSEDVqRRFVQEVVQSQQVAVGRQLEDFRSKRLMGM 180
Cdd:cd08753    79 FLEKNAPLRVKIPEMLQAEIDlRLRN---NEDP-RGVLCEAQEAVMPEIQEQIQDYRSKRTLGL 138
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 403-672 2.37e-16

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


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 84.56  E-value: 2.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  403 LELEPEEPPGWRELVPPDTLHSLPKSQVKRQEVISELLVTEAAHVRMLRVLHDLFFQPMAECLFFPLEELQN----IFPS 478
Cdd:COG5422    456 LDKFDEEKNLWTLSVPKEVWESLPKQEIKRQEAIYEVIYTERDFVKDLEYLRDTWIKPLEESNIIPENARRNfikhVFAN 535

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  479 LDELIEVHSLFLDRLmKRRQESGYLIEEIGDVLLARFdgaegSWFQKISSRFCSRQsfALEQLKAKQRK-DPRFCAFVQE 557
Cdd:COG5422    536 INEIYAVNSKLLKAL-TNRQCLSPIVNGIADIFLDYV-----PKFEPFIKYGASQP--YAKYEFEREKSvNPNFARFDHE 607

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  558 AESRPRCRRLQLKDMIPTEMQRLTKYPLLLQSIGQNTEE-PTEREKVELAAECCREILHHVNQAVRDMEDllrlkdyqrR 636
Cdd:COG5422    608 VERLDESRKLELDGYLTKPTTRLARYPLLLEEVLKFTDPdNPDTEDIPKVIDMLREFLSRLNFESGKAEN---------R 678

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2462568596  637 LDLSHLRQSSdPMLSEFKNLDI--TKKKLVHEGPLTWR 672
Cdd:COG5422    679 GDLFHLNQQL-LFKPEYVNLGLndEYRKIIFKGVLKRK 715
RGS_GEF_like cd08756
Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange ...
 68-182 7.36e-05

Regulator of G protein signaling (RGS) domain found in the Rho guanine nucleotide exchange factor (RhoGEF) protein; The RGS domain found in the Rho guanine nucleotide exchange factor (RhoGEF) protein subfamily of the RGS domain containing protein family, which is a diverse group of multifunctional proteins that regulate cellular signaling events downstream of G-protein coupled receptors (GPCRs). The RhoGEFs are peripheral membrane proteins that regulate essential cellular processes, including cell shape, cell migration and cell cycle progression as well as gene transcription by linking signals from heterotrimeric G-alpha12/13 protein-coupled receptors to Rho GTPase activation, leading to various cellular responses, such as actin reorganization and gene expression. The RhoGEF subfamily includes the leukemia-associated RhoGEF protein (LARG), p115RhoGEF, PDZ-RhoGEF, and its rat specific splice variant GTRAP48. The RGS domain of RhoGEFs has very little sequence similarity with the canonical RGS domain of the RGS proteins and is often refered to as RH (RGS Homology) domain. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins play critical regulatory role as GTPase activating proteins (GAPs) of the heterotrimeric G-protein G-alpha-subunits. RGS proteins regulate many aspects of embryonic development such as glial differentiation, embryonic axis formation, skeletal and muscle development, cell migration during early embryogenesis, as well as apoptosis, cell proliferation, and modulation of cardiac development.


Pssm-ID: 188710  Cd Length: 122  Bit Score: 43.15  E-value: 7.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596  68 KRRPAHLMALLQHVALQFEPGPLLCCLHADMLGSLGPKEAKKAFLDFYHSFLEKTA-VLRVPVPPNVAFELDRT-RADLI 145
Cdd:cd08756     1 KTHPAHLAVFLNYLLSNSDPSSLFFYLITDLYKSGNIKDMRKWAYEIFSTFLVPNApLLWPNIDESLIQEIDKIlQNEQD 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462568596 146 SEDVQRRFVQEVVQSQQVAVGRQLEDFRSKRLMGMTP 182
Cdd:cd08756    81 DEEILRRVFLKAREKARDEINDQLADFRQKRTLGLGS 117
PH_ARHGEF18 cd15794
Rho guanine nucleotide exchange factor 18 Pleckstrin homology (PH) domain; ARHGEF18, also ...
 660-770 2.02e-04

Rho guanine nucleotide exchange factor 18 Pleckstrin homology (PH) domain; ARHGEF18, also called p114RhoGEF, is a key regulator of RhoA-Rock2 signaling that is crucial for maintenance of polarity in the vertebrate retinal epithelium, and consequently is essential for cellular differentiation, morphology and eventually organ function. ARHGEF18 contains Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275437  Cd Length: 119  Bit Score: 41.81  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 660 KKKLVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLKShsrtltptPDGKTmlrPVLRLTSAMTREVATDHKA 739
Cdd:cd15794     1 RRQLLLEGMLYWKAASGRLKDILALLLTDVLLLLQEKDQKYVFAS--------VDSKP---PVISLQKLIVREVANEEKA 69

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462568596 740 FYVLFTWDQEAQIYELVAQTVSERKNWCALI 770
Cdd:cd15794    70 MFLISASLNGPEMYEIHTNSKEDRNTWMAHI 100
PH_AKAP13 cd13392
A-kinase anchoring protein 13 Pleckstrin homology (PH) domain; The Rho-specific GEF activity ...
 663-773 5.89e-04

A-kinase anchoring protein 13 Pleckstrin homology (PH) domain; The Rho-specific GEF activity of AKAP13 (also called Brx-1, AKAP-Lbc, and proto-Lbc) mediates signaling downstream of G-protein coupled receptors and Toll-like receptor 2. It plays a role in cell growth, cell development and actin fiber formation. Protein kinase A (PKA) binds and phosphorylates AKAP13, regulating its Rho-GEF activity. Alternative splicing of this gene in humans has at least 3 transcript variants encoding different isoforms (i.e. proto-/onco-Lymphoid blast crisis, Lbc and breast cancer nuclear receptor-binding auxiliary protein, Brx) containing a dbl oncogene homology (DH) domain and PH domain which are required for full transforming activity. The DH domain is associated with guanine nucleotide exchange activation while the PH domain has multiple functions including determine protein sub-cellular localisation via phosphoinositide interactions, while others bind protein partners. Other ligands include protein kinase C which is bound by the PH domain of AKAP13, serving to activate protein kinase D and mobilize a cardiac hypertrophy signaling pathway. 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: 275427  Cd Length: 103  Bit Score: 40.28  E-value: 5.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 663 LVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLKSHSRTLTptpdgktmlrpVLRLTSAMTREVATDHKAFYV 742
Cdd:cd13392     1 LVRDGPVSLKNTAGRLKEVQAVLLSDVLVFLQEKDQKYVFASLDQKST-----------VISLKKLIVREVAHEEKGLFL 69

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2462568596 743 LFTWDQEAQIYELVAQTVSERKNWCALITET 773
Cdd:cd13392    70 ISMGIADPEMVEVHASSKEERNSWMQIIQDT 100
PH_p190RhoGEF cd14680
Rho guanine nucleotide exchange factor Pleckstrin homology domain; p190RhoGEF (also called ...
 663-772 7.82e-04

Rho guanine nucleotide exchange factor Pleckstrin homology domain; p190RhoGEF (also called RIP2 or ARHGEF28) belongs to regulator of G-protein signaling (RGS) domain-containing RhoGEFs that are RhoA-selective and directly activated by the Galpha12/13 family of heterotrimeric G proteins. In addition to the Dbl homology (DH)-PH domain, p190RhoGEF contains an N-terminal C1 (Protein kinase C conserved region 1) domain. The DH-PH domains bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275430  Cd Length: 101  Bit Score: 39.98  E-value: 7.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 663 LVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLKshsrtltpTPDGKTmlrPVLRLTSAMTREVATDHKAFYV 742
Cdd:cd14680     1 LLHEGLVYWKTATGRFKDILALLLTDVLLFLQEKDQKYIFA--------AVDQKP---PVICLQKLIVREVANEERGMFL 69

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462568596 743 LFTWDQEAQIYELVAQTVSERKNWCALITE 772
Cdd:cd14680    70 ISASSAGPEMYEIHTSSKEERNNWMRLIQE 99
PHA03169 PHA03169
hypothetical protein; Provisional
 266-430 1.17e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.65  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 266 GNRRSDEPAKTKKGLSSIL-DAARWNRGEPQVPDfrhlkAEVDAEKPGATDRKGGVGMPSRDRNIGAPGQDTPGVSLHPL 344
Cdd:PHA03169   96 GSESVGSPTPSPSGSAEELaSGLSPENTSGSSPE-----SPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPS 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 345 SLDSPDR-EPGADAPLELGDSSPQGPMSLESLAPPESTDEGAETESPEPgDEGEPGRSGLELEPE-EPPGWRELVPPDTL 422
Cdd:PHA03169  171 HEDSPEEpEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTP-QQAPSPNTQQAVEHEdEPTEPEREGPPFPG 249


                  ....*...
gi 2462568596 423 HSLPKSQV 430
Cdd:PHA03169  250 HRSHSYTV 257
PH_ARHGEF2 cd13393
Rho guanine nucleotide exchange factor 2 Pleckstrin homology (PH) domain; ARHGEF2, also called ...
 660-776 1.75e-03

Rho guanine nucleotide exchange factor 2 Pleckstrin homology (PH) domain; ARHGEF2, also called GEF-H1, acts as guanine nucleotide exchange factor (GEF) for RhoA GTPases. It is thought to play a role in actin cytoskeleton reorganization in different tissues since its activation induces formation of actin stress fibers. ARHGEF2 contains a C1 domain followed by Dbl-homology (DH) and pleckstrin-homology (PH) domains which bind and catalyze the exchange of GDP for GTP on RhoA. 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: 275428  Cd Length: 116  Bit Score: 39.10  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462568596 660 KKKLVHEGPLTWRVTKDKAVEVHVLLLDDLLLLLQRQDERLLLkshsrtltPTPDGKtmlrPVLRLTSAMTREVATDHKA 739
Cdd:cd13393     1 RRKLIHDGCLLWKTASGRFKDVQVLLMTDVLVFLQEKDQKYIF--------PTLDKP----AVISLQNLIVRDIANQEKG 68

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462568596 740 FYVLFTWDQEaqIYELVAQTVSERKNWCALITETAGS 776
Cdd:cd13393    69 MFLISAAPPE--MYEVHAASRDDRNTWMRLIQQTVKT 103
 
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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