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Conserved domains on  [gi|528479385|ref|XP_005171943|]
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stAR-related lipid transfer protein 8 isoform X3 [Danio rerio]

Protein Classification

Rho GTPase-activating protein; SRPBCC family protein( domain architecture ID 10175854)

Rho GTPase-activating protein for Rho/Rac/Cdc42-like small GTPases that act as molecular switches, active in their GTP-bound form but inactive when bound to GDP| SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) family protein may have a deep hydrophobic ligand-binding pocket

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
START_STARD8-like cd08907
C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also ...
 837-1041 4.23e-148

C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear.


:

Pssm-ID: 176916  Cd Length: 205  Bit Score: 439.36  E-value: 4.23e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  837 LGEPVDYRAYLEDNVQCLLREASERSKGWHHAHGPDNTELAYKKVGDGHPMRIWRVSVEIEAPPSVVLQRVLRERHLWDE 916
Cdd:cd08907     1 QGEGVDLRAYLEDNVQCLLREASERFKGWHSAPGPDNTELACKKVGDGHPLRLWKVSTEVEAPPSVVLQRVLRERHLWDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  917 DLLHSRVIETLENNTEVFHYITDSMAPHPRRNFITLRRWCSDLPKGVCVLVSSSVDHDNVQLEAGLRAVLLTSRMFIEPC 996
Cdd:cd08907    81 DLLHSQVIEALENNTEVYHYVTDSMAPHPRRDFVVLRMWRSDLPRGGCLLVSQSVDHDNPQLEAGVRAVLLTSQYLIEPC 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 528479385  997 GMGRSRLTHYCRADLRGRSPDWYNKVFGHLCAMEVARIRSSFPVL 1041
Cdd:cd08907   161 GMGRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVARIRDSFPTL 205
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 595-811 8.36e-122

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


:

Pssm-ID: 239840  Cd Length: 220  Bit Score: 371.37  E-value: 8.36e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  595 DKHVFGVPPIVNVQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYDVADLIK 674
Cdd:cd04375     1 DKNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  675 QYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAP 753
Cdd:cd04375    81 QYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAAnSQENQMTATNLAVCLAP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  754 SILHLNASKKDGASPRLISRKGGA--KPDHKDLSENMAATHCLSHMITECKKLFQIPHEM 811
Cdd:cd04375   161 SLFHLNTSRRENSSPARRMQRKKSlgKPDQKELSENKAAHQCLAYMIEECNTLFMVPKEM 220
SAM_DLC1,2-like cd09538
SAM domain of DLC1,2-like subfamily; SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted ...
 17-76 3.55e-35

SAM domain of DLC1,2-like subfamily; SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted in liver cancer) subfamily is a protein-protein interaction domain located at the N-terminus of the protein. Members of this subfamily do not form dimers/oligomers through their SAM domains. They participate in regulation of cell migration and lipid transfer. SAM domain of human DLC1 protein contains the EF1A1 (eukaryotic elongation factor) binding motif, thus SAM facilitates recruitment of EF1A1 to the membrane periphery and suppresses cell migration. Human Dlc2 gene is known as a tumor suppressor gene. It was found underexpressed in hepatocellular carcinoma.


:

Pssm-ID: 188937  Cd Length: 60  Bit Score: 127.53  E-value: 3.55e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385   17 KDACEWLRAAGFPQYAQLYEASLFPIEISAVRRDHEFLDQDSLKALCRRLTTLNKCAAMS 76
Cdd:cd09538     1 KEACKWLRAAGFPQYAQLYEDSQFPIDISAVKRDHDFLDRDSLQALIRRLNTLNKCASMK 60
 
Name Accession Description Interval E-value
START_STARD8-like cd08907
C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also ...
 837-1041 4.23e-148

C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176916  Cd Length: 205  Bit Score: 439.36  E-value: 4.23e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  837 LGEPVDYRAYLEDNVQCLLREASERSKGWHHAHGPDNTELAYKKVGDGHPMRIWRVSVEIEAPPSVVLQRVLRERHLWDE 916
Cdd:cd08907     1 QGEGVDLRAYLEDNVQCLLREASERFKGWHSAPGPDNTELACKKVGDGHPLRLWKVSTEVEAPPSVVLQRVLRERHLWDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  917 DLLHSRVIETLENNTEVFHYITDSMAPHPRRNFITLRRWCSDLPKGVCVLVSSSVDHDNVQLEAGLRAVLLTSRMFIEPC 996
Cdd:cd08907    81 DLLHSQVIEALENNTEVYHYVTDSMAPHPRRDFVVLRMWRSDLPRGGCLLVSQSVDHDNPQLEAGVRAVLLTSQYLIEPC 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 528479385  997 GMGRSRLTHYCRADLRGRSPDWYNKVFGHLCAMEVARIRSSFPVL 1041
Cdd:cd08907   161 GMGRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVARIRDSFPTL 205
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 595-811 8.36e-122

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239840  Cd Length: 220  Bit Score: 371.37  E-value: 8.36e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  595 DKHVFGVPPIVNVQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYDVADLIK 674
Cdd:cd04375     1 DKNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  675 QYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAP 753
Cdd:cd04375    81 QYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAAnSQENQMTATNLAVCLAP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  754 SILHLNASKKDGASPRLISRKGGA--KPDHKDLSENMAATHCLSHMITECKKLFQIPHEM 811
Cdd:cd04375   161 SLFHLNTSRRENSSPARRMQRKKSlgKPDQKELSENKAAHQCLAYMIEECNTLFMVPKEM 220
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 612-767 1.10e-43

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 156.27  E-value: 1.10e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385    612 QPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALR-QLNENSPDHVTYQGQSAYDVADLIKQYFRDLPEPVLTSKLT 690
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRdAFDSGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528479385    691 DTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAPSILHLNASKKDGAS 767
Cdd:smart00324   81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEhSEENKMTARNLAIVFGPTLLRPPDGEVASLK 158
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 615-757 2.23e-41

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 148.85  E-value: 2.23e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385   615 PQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQ-LNENSPDHVTYQGQSAYDVADLIKQYFRDLPEPVLTSKLTDTF 693
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREaFDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528479385   694 LHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAPSILH 757
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQnSDVNKMNAHNLAIVFGPTLLR 145
START pfam01852
START domain;
846-1035 1.57e-35

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 134.07  E-value: 1.57e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385   846 YLEDNVQCLLREASERSKGWHHAHGPDNTELAYKKV--GDGHPMRIWR-VSVEIEAPPSVVLQRVLReRHLWDEDLLHSR 922
Cdd:pfam01852    2 LAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVepDHGEASRASGvVPMVAALLVAELLKDMEY-RAQWDKDVRSAE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385   923 VIETLENNTEVFHYITDSMA--PHPRRNFITLRRWcSDLPKGVCVLVSSSVDH-DNVQLEAGLRAVLLTSRMFIEPCGMG 999
Cdd:pfam01852   81 TLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYW-RRLGGGVYVIVDRSVTHpQFPPSSGYVRAERLPSGYLIQPCGNG 159

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 528479385  1000 RSRLTHYCRADLRGRSPDWYNKVFGHLCAMEVARIR 1035
Cdd:pfam01852  160 PSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTW 195
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 848-1033 2.28e-35

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 133.71  E-value: 2.28e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385    848 EDNVQCLLREASERSKGWHHAHGPDNTELAYKKV----GDGHPMRIWRVSVEIEAPPSVVLQRVLRERHLWDEDLLHSRV 923
Cdd:smart00234    3 EEAAAELLKMAAASEEGWVLSSENENGDEVRSIFspgrKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKAET 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385    924 IETLENNTEVFHYITDSMA-PHPRRNFITLRRWCSDlPKGVCVLVSSSVDHDNVQLEAGL-RAVLLTSRMFIEPCGMGRS 1001
Cdd:smart00234   83 LEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWRED-EDGSYAVVDVSVTHPTSPPESGYvRAENLPSGLLIEPLGNGPS 161

                           170       180       190
                    ....*....|....*....|....*....|..
gi 528479385   1002 RLTHYCRADLRGRSPDWYNKVFGHLCAMEVAR 1033
Cdd:smart00234  162 KVTWVSHADLKGWLPHWLVRSLIKSGLAEFAK 193
SAM_DLC1,2-like cd09538
SAM domain of DLC1,2-like subfamily; SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted ...
 17-76 3.55e-35

SAM domain of DLC1,2-like subfamily; SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted in liver cancer) subfamily is a protein-protein interaction domain located at the N-terminus of the protein. Members of this subfamily do not form dimers/oligomers through their SAM domains. They participate in regulation of cell migration and lipid transfer. SAM domain of human DLC1 protein contains the EF1A1 (eukaryotic elongation factor) binding motif, thus SAM facilitates recruitment of EF1A1 to the membrane periphery and suppresses cell migration. Human Dlc2 gene is known as a tumor suppressor gene. It was found underexpressed in hepatocellular carcinoma.


Pssm-ID: 188937  Cd Length: 60  Bit Score: 127.53  E-value: 3.55e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385   17 KDACEWLRAAGFPQYAQLYEASLFPIEISAVRRDHEFLDQDSLKALCRRLTTLNKCAAMS 76
Cdd:cd09538     1 KEACKWLRAAGFPQYAQLYEDSQFPIDISAVKRDHDFLDRDSLQALIRRLNTLNKCASMK 60
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
12-75 2.70e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 45.72  E-value: 2.70e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528479385    12 HELEAKDACEWLRAAGFPQYAQLYEASLFPIEISAVRRDHEFLDQDSLKALCRRLTTLNKCAAM 75
Cdd:pfam07647    2 ESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
 
Name Accession Description Interval E-value
START_STARD8-like cd08907
C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also ...
 837-1041 4.23e-148

C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176916  Cd Length: 205  Bit Score: 439.36  E-value: 4.23e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  837 LGEPVDYRAYLEDNVQCLLREASERSKGWHHAHGPDNTELAYKKVGDGHPMRIWRVSVEIEAPPSVVLQRVLRERHLWDE 916
Cdd:cd08907     1 QGEGVDLRAYLEDNVQCLLREASERFKGWHSAPGPDNTELACKKVGDGHPLRLWKVSTEVEAPPSVVLQRVLRERHLWDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  917 DLLHSRVIETLENNTEVFHYITDSMAPHPRRNFITLRRWCSDLPKGVCVLVSSSVDHDNVQLEAGLRAVLLTSRMFIEPC 996
Cdd:cd08907    81 DLLHSQVIEALENNTEVYHYVTDSMAPHPRRDFVVLRMWRSDLPRGGCLLVSQSVDHDNPQLEAGVRAVLLTSQYLIEPC 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 528479385  997 GMGRSRLTHYCRADLRGRSPDWYNKVFGHLCAMEVARIRSSFPVL 1041
Cdd:cd08907   161 GMGRSRLTHICRADLRGRSPDWYNKVFGHLCAMEVARIRDSFPTL 205
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 595-811 8.36e-122

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239840  Cd Length: 220  Bit Score: 371.37  E-value: 8.36e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  595 DKHVFGVPPIVNVQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYDVADLIK 674
Cdd:cd04375     1 DKNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  675 QYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAP 753
Cdd:cd04375    81 QYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAAnSQENQMTATNLAVCLAP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  754 SILHLNASKKDGASPRLISRKGGA--KPDHKDLSENMAATHCLSHMITECKKLFQIPHEM 811
Cdd:cd04375   161 SLFHLNTSRRENSSPARRMQRKKSlgKPDQKELSENKAAHQCLAYMIEECNTLFMVPKEM 220
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 845-1041 2.07e-102

C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD8 (also known as deleted in liver cancer 3/DLC3, and Arhgap38), STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP), and STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. Some, including STARD12, -and -13, also have an N-terminal SAM (sterile alpha motif) domain; these have a SAM-RhoGAP-START domain organization. This subfamily is involved in cancer development. A large spectrum of cancers have dysregulated genes encoding these proteins. The precise function of the START domain in this subfamily is unclear.


Pssm-ID: 176878  Cd Length: 197  Bit Score: 319.25  E-value: 2.07e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  845 AYLEDNVQCLLREASERSKGWHHAHGPDNTELAYKKVGDGHPMRIWRVSVEIEAPPSVVLQRVLRERHLWDEDLLHSRVI 924
Cdd:cd08869     1 SYLERCVQDLLREARDKSKGWVSVSSSDHVELAFKKVDDGHPLRLWRASTEVEAPPEEVLQRILRERHLWDDDLLQWKVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  925 ETLENNTEVFHYITDSMAPHPRRNFITLRRWCSDLPKGVCVLVSSSVDHDNVQLEAGLRAVLLTSRMFIEPCGMGRSRLT 1004
Cdd:cd08869    81 ETLDEDTEVYQYVTNSMAPHPTRDYVVLRTWRTDLPKGACVLVETSVEHTEPVPLGGVRAVVLASRYLIEPCGSGKSRVT 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 528479385 1005 HYCRADLRGRSPDWYNKVFGHLCAMEVARIRSSFPVL 1041
Cdd:cd08869   161 HICRVDLRGRSPEWYNKVYGHLCARELLRIRDSFRQL 197
START_STARD13-like cd08909
C-terminal lipid-binding START domain of mammalian STARD13 and related proteins, which also ...
 843-1038 2.77e-98

C-terminal lipid-binding START domain of mammalian STARD13 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD13 (also known as DLC-2, Arhgap37, and SDCCAG13) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subfamily also have a RhoGAP domain. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176918  Cd Length: 205  Bit Score: 308.77  E-value: 2.77e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  843 YRAYLEDNVQCLLREASERSKGWHHAHGPDNTELAYKKVGDGHPMRIWRVSVEIEAPPSVVLQRVLRERHLWDEDLLHSR 922
Cdd:cd08909     7 YQTYLESLIQNLQKEAKEKFKGWISCSSSDNTELAYKKVGDGNPLRLWKVSVEVEAPPSVVLNRVLRERHLWDEDFLQWK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  923 VIETLENNTEVFHYITDSMAPHPRRNFITLRRWCSDLPKGVCVLVSSSVDHDNVQLEAGLRAVLLTSRMFIEPCGMGRSR 1002
Cdd:cd08909    87 VVETLDKQTEVYQYVLNCMAPHPSRDFVVLRSWRTDLPKGACSLVSVSVEHEEAPLLGGVRAVVLDSQYLIEPCGSGKSR 166

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 528479385 1003 LTHYCRADLRGRSPDWYNKVFGHLCAMEVARIRSSF 1038
Cdd:cd08909   167 LTHICRVDLKGHSPEWYNKGFGHLCAAEAARIRNSF 202
START_STARD12-like cd08908
C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also ...
 839-1038 3.35e-79

C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also have an N-terminal Rho GTPase-activating protein (RhoGAP) domain; This subgroup includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD12 (also known as DLC-1, Arhgap7, and p122-RhoGAP) and related proteins. It belongs to the START domain family, and in turn to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. Proteins belonging to this subgroup also have an N-terminal SAM (sterile alpha motif) domain and a RhoGAP domain, and have a SAM-RhoGAP-START domain organization. The precise function of the START domain in this subgroup is unclear.


Pssm-ID: 176917  Cd Length: 204  Bit Score: 257.25  E-value: 3.35e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  839 EPVDYRAYLEDNVQCLLREASERSKGWHHAHGPDNTELAYKKVGDGHPMRIWRVSVEIEAPPSVVLQRVLRERHLWDEDL 918
Cdd:cd08908     3 EPADYHHFLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVSEGPPLRLWRTTIEVPAAPEEILKRLLKEQHLWDVDL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  919 LHSRVIETLENNTEVFHYITDSMAPHPRRNFITLRRWCSDLPKGVCVLVSSSVDHDNVQLeAGLRAVLLTSRMFIEPCGM 998
Cdd:cd08908    83 LDSKVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWRTNLPKGACALLATSVDHDRAPV-AGVRVNVLLSRYLIEPCGS 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 528479385  999 GRSRLTHYCRADLRGRSPDWYNKVFGHLCAMEVARIRSSF 1038
Cdd:cd08908   162 GKSKLTYMCRIDLRGHMPEWYTKSFGHLCAAEVVKIRDSF 201
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 612-767 1.10e-43

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 156.27  E-value: 1.10e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385    612 QPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALR-QLNENSPDHVTYQGQSAYDVADLIKQYFRDLPEPVLTSKLT 690
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRdAFDSGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528479385    691 DTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAPSILHLNASKKDGAS 767
Cdd:smart00324   81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEhSEENKMTARNLAIVFGPTLLRPPDGEVASLK 158
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 615-757 2.23e-41

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 148.85  E-value: 2.23e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385   615 PQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQ-LNENSPDHVTYQGQSAYDVADLIKQYFRDLPEPVLTSKLTDTF 693
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREaFDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528479385   694 LHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAPSILH 757
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQnSDVNKMNAHNLAIVFGPTLLR 145
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 615-761 9.56e-41

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 147.83  E-value: 9.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  615 PQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYDVADLIKQYFRDLPEPVLTSKLTDTFL 694
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528479385  695 HVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIASAQE-NQMTADSLAVCLAPSILHLNAS 761
Cdd:cd00159    81 ELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEvNKMTASNLAIVFAPTLLRPPDS 148
START pfam01852
START domain;
846-1035 1.57e-35

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 134.07  E-value: 1.57e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385   846 YLEDNVQCLLREASERSKGWHHAHGPDNTELAYKKV--GDGHPMRIWR-VSVEIEAPPSVVLQRVLReRHLWDEDLLHSR 922
Cdd:pfam01852    2 LAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVepDHGEASRASGvVPMVAALLVAELLKDMEY-RAQWDKDVRSAE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385   923 VIETLENNTEVFHYITDSMA--PHPRRNFITLRRWcSDLPKGVCVLVSSSVDH-DNVQLEAGLRAVLLTSRMFIEPCGMG 999
Cdd:pfam01852   81 TLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYW-RRLGGGVYVIVDRSVTHpQFPPSSGYVRAERLPSGYLIQPCGNG 159

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 528479385  1000 RSRLTHYCRADLRGRSPDWYNKVFGHLCAMEVARIR 1035
Cdd:pfam01852  160 PSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTW 195
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 848-1033 2.28e-35

in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and phosphatidylcholine transfer protein


Pssm-ID: 214575  Cd Length: 205  Bit Score: 133.71  E-value: 2.28e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385    848 EDNVQCLLREASERSKGWHHAHGPDNTELAYKKV----GDGHPMRIWRVSVEIEAPPSVVLQRVLRERHLWDEDLLHSRV 923
Cdd:smart00234    3 EEAAAELLKMAAASEEGWVLSSENENGDEVRSIFspgrKPGEAFRLVGVVPMVCADLVEELMDDLEYRPEWDKNVAKAET 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385    924 IETLENNTEVFHYITDSMA-PHPRRNFITLRRWCSDlPKGVCVLVSSSVDHDNVQLEAGL-RAVLLTSRMFIEPCGMGRS 1001
Cdd:smart00234   83 LEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWRED-EDGSYAVVDVSVTHPTSPPESGYvRAENLPSGLLIEPLGNGPS 161

                           170       180       190
                    ....*....|....*....|....*....|..
gi 528479385   1002 RLTHYCRADLRGRSPDWYNKVFGHLCAMEVAR 1033
Cdd:smart00234  162 KVTWVSHADLKGWLPHWLVRSLIKSGLAEFAK 193
SAM_DLC1,2-like cd09538
SAM domain of DLC1,2-like subfamily; SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted ...
 17-76 3.55e-35

SAM domain of DLC1,2-like subfamily; SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted in liver cancer) subfamily is a protein-protein interaction domain located at the N-terminus of the protein. Members of this subfamily do not form dimers/oligomers through their SAM domains. They participate in regulation of cell migration and lipid transfer. SAM domain of human DLC1 protein contains the EF1A1 (eukaryotic elongation factor) binding motif, thus SAM facilitates recruitment of EF1A1 to the membrane periphery and suppresses cell migration. Human Dlc2 gene is known as a tumor suppressor gene. It was found underexpressed in hepatocellular carcinoma.


Pssm-ID: 188937  Cd Length: 60  Bit Score: 127.53  E-value: 3.55e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385   17 KDACEWLRAAGFPQYAQLYEASLFPIEISAVRRDHEFLDQDSLKALCRRLTTLNKCAAMS 76
Cdd:cd09538     1 KEACKWLRAAGFPQYAQLYEDSQFPIDISAVKRDHDFLDRDSLQALIRRLNTLNKCASMK 60
SAM_DLC2 cd09592
SAM domain of STARD13-like subfamily; SAM (sterile alpha motif) domain of DLC2 (Deleted in ...
 13-75 1.09e-31

SAM domain of STARD13-like subfamily; SAM (sterile alpha motif) domain of DLC2 (Deleted in liver cancer) protein is a lipid-binding and putative protein-protein interaction domain located at the N-terminus of the protein. Members of this subfamily do not form dimers/oligomers through their SAM domains. They participate in lipid transfer. Human Dlc2 gene is known as a tumor suppressor gene. It was found underexpressed in hepatocellular carcinoma.


Pssm-ID: 188991  Cd Length: 64  Bit Score: 117.82  E-value: 1.09e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528479385   13 ELEAKDACEWLRAAGFPQYAQLYEASLFPIEISAVRRDHEFLDQDSLKALCRRLTTLNKCAAM 75
Cdd:cd09592     1 EIEAKEACDWLRAAGFPQYAQLYEDSQFPIDIASVKRDHDFLDRDLVEPLCRRLNTLNKCASM 63
SAM_DLC1 cd09591
SAM domain of DLC1 subfamily; SAM (sterile alpha motif) domain of DLC1 (Deleted in liver ...
 17-75 4.81e-29

SAM domain of DLC1 subfamily; SAM (sterile alpha motif) domain of DLC1 (Deleted in liver cancer) protein is a protein-protein interaction domain located at the N-terminus. Proteins of this subfamily do not form dimers/oligomers through their SAM domains. They participate in regulation of cell migration. SAM domain of human DLC1 protein contains the EF1A1 (eukaryotic elongation factor) binding motif, thus SAM facilitates recruitment of EF1A1 to the membrane periphery and suppresses cell migration.


Pssm-ID: 188990  Cd Length: 60  Bit Score: 110.11  E-value: 4.81e-29
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 528479385   17 KDACEWLRAAGFPQYAQLYEASLFPIEISAVRRDHEFLDQDSLKALCRRLTTLNKCAAM 75
Cdd:cd09591     1 KEACDWLRAAGFPQYAQLYEDLLFPIDIELVKREHDFLDRDAIEALCRRLNTLNKCAVM 59
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 614-811 5.40e-29

RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP6-like proteins. ArhGAP6 shows GAP activity towards RhoA, but not towards Cdc42 and Rac1. ArhGAP6 is often deleted in microphthalmia with linear skin defects syndrome (MLS); MLS is a severe X-linked developmental disorder. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239841  Cd Length: 206  Bit Score: 115.23  E-value: 5.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  614 LPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYDVADLIKQYFRDLPEPVLTSKLTDTF 693
Cdd:cd04376     9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  694 LHVYQFVPAEQrLQAVQAAVILLPDENREVLQTLLYFLSDIA---------SAQE---NQMTADSLAVCLAPSILHLNAS 761
Cdd:cd04376    89 IGTALLEPDEQ-LEALQLLIYLLPPCNCDTLHRLLKFLHTVAehaadsideDGQEvsgNKMTSLNLATIFGPNLLHKQKS 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 528479385  762 KKdgasprlisRKGGAKPDHkdLSENMAATHCLSHMITECKKLFQIPHEM 811
Cdd:cd04376   168 GE---------REFVQASLR--IEESTAIINVVQTMIDNYEELFMVSPEL 206
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 598-816 7.27e-28

RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP18-like proteins. The function of ArhGAP18 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239856  Cd Length: 216  Bit Score: 112.44  E-value: 7.27e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  598 VFGVPPIVNVQRTGQPLPQS-----IQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQ-------LNENSPDHVTyqgqs 665
Cdd:cd04391     1 LFGVPLSTLLERDQKKVPGSkvpliFQKLINKLEERGLETEGILRIPGSAQRVKFLCQeleakfyEGTFLWDQVK----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  666 AYDVADLIKQYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIASAQE-NQMTA 744
Cdd:cd04391    76 QHDAASLLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEkNKMNL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528479385  745 DSLAVCLAPSILhlnaskkdgaSPRLIsrkgGAKPDHKDLSE-NMAATHC--LSHMITECKKLFQIPHEMMLQSR 816
Cdd:cd04391   156 WNVAMIMAPNLF----------PPRGK----HSKDNESLQEEvNMAAGCAniMRLLIRYQDLLWTVPSFLINQVR 216
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 878-1035 1.50e-26

Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, and related domains, such as the START domain of the Arabidopsis homeobox protein GLABRA 2. The mammalian STARDs are grouped into 8 subfamilies. This family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some members of this family, specific lipids that bind in this pocket are known; these include cholesterol (STARD1/STARD3/ STARD4/STARD5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2/ STARD7/STARD10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). The START domain is found either alone or in association with other domains. Mammalian STARDs participate in the control of various cellular processes including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease. The Arabidopsis homeobox protein GLABRA 2 suppresses root hair formation in hairless epidermal root cells.


Pssm-ID: 176851 [Multi-domain]  Cd Length: 193  Bit Score: 107.81  E-value: 1.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  878 YKKVGDGHPMRIWRVSVEIEAPPSVVLQRV--LRERHLWDEDLLHSRVIETLENNTEVFHYITDSMAPHPRRNFITLRRW 955
Cdd:cd00177    29 YTKPYEDSGLKLLKAEGVIPASPEQVFELLmdIDLRKKWDKNFEEFEVIEEIDEHTDIIYYKTKPPWPVSPRDFVYLRRR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  956 cSDLPKGVCVLVSSSVDHDNVQLEAGL-RAVLLTSRMFIEPCGMGRSRLTHYCRADLRGRSPDW-YNKVFGHLCAMEVAR 1033
Cdd:cd00177   109 -RKLDDGTYVIVSKSVDHDSHPKEKGYvRAEIKLSGWIIEPLDPGKTKVTYVLQVDPKGSIPKSlVNSAAKKQLASFLKD 187


                  ..
gi 528479385 1034 IR 1035
Cdd:cd00177   188 LR 189
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 599-756 9.81e-26

RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in class IX myosins. Class IX myosins contain a characteristic head domain, a neck domain, a tail domain which contains a C6H2-zinc binding motif and a RhoGAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239842  Cd Length: 186  Bit Score: 105.21  E-value: 9.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  599 FGVPpIVNVQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYDVADLIKQYFR 678
Cdd:cd04377     1 FGVS-LSSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528479385  679 DLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIASAQE-NQMTADSLAVCLAPSIL 756
Cdd:cd04377    80 ELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEvNRMSANALAIVFAPCIL 158
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 614-762 2.00e-25

RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239867  Cd Length: 192  Bit Score: 104.69  E-value: 2.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  614 LPQSIQQAMRYLRSQCLEKVGIFRKSGVKSriqALRQLNE--NSPDHVTYQGQSAYDVADLIKQYFRDLPEPVLTSKLTD 691
Cdd:cd04402    15 LPKPILDMLSLLYQKGPSTEGIFRRSANAK---ACKELKEklNSGVEVDLKAEPVLLLASVLKDFLRNIPGSLLSSDLYE 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528479385  692 TFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIA-SAQENQMTADSLAVCLAPSILHLNASK 762
Cdd:cd04402    92 EWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISqNSETNKMDAFNLAVCIAPSLLWPPASS 163
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 598-759 5.45e-24

RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP11A-like proteins. The mouse homolog of human ArhGAP11A has been detected as a gene exclusively expressed in immature ganglion cells, potentially playing a role in retinal development. The exact function of ArhGAP11A is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 100.62  E-value: 5.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  598 VFGVP----PIVNVQRTGQpLPQSIQQAMRYLRSQcLEKVGIFRKSGVKSRIQALRQLNENSPDHVtyqgqSAY---DVA 670
Cdd:cd04394     1 VFGVPlhslPHSTVPEYGN-VPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEACL-----SSAlpcDVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  671 DLIKQYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAV 749
Cdd:cd04394    74 GLLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQrCSENKMDSSNLAV 153

                         170
                  ....*....|
gi 528479385  750 CLAPSILHLN 759
Cdd:cd04394   154 IFAPNLFQSE 163
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 634-757 1.96e-23

RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239850  Cd Length: 184  Bit Score: 98.53  E-value: 1.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  634 GIFRKSGVKSRIQALrqLNENSPDHVTYQ----GQSAYDVADLIKQYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAV 709
Cdd:cd04385    35 GIYRKNGKNSSVKKL--LEAFRKDARSVQlregEYTVHDVADVLKRFLRDLPDPLLTSELHAEWIEAAELENKDERIARY 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 528479385  710 QAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAPSILH 757
Cdd:cd04385   113 KELIRRLPPINRATLKVLIGHLYRVQKhSDENQMSVHNLALVFGPTLFQ 161
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 597-756 3.23e-23

RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239869 [Multi-domain]  Cd Length: 195  Bit Score: 98.18  E-value: 3.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  597 HVFGVP--PIVNVQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLnENSPDHVTYQGQSAYDVADLI- 673
Cdd:cd04404     4 QQFGVSlqFLKEKNPEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQK-YNMGEPVDFDQYEDVHLPAVIl 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  674 KQYFRDLPEPVLTSKLTDtflHVYQF--VPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVC 750
Cdd:cd04404    83 KTFLRELPEPLLTFDLYD---DIVGFlnVDKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAhSDQNKMTNSNLAVV 159


                  ....*.
gi 528479385  751 LAPSIL 756
Cdd:cd04404   160 FGPNLL 165
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 599-756 1.66e-22

RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD1-like proteins. Yeast Rgd1 is a GAP protein for Rho3 and Rho4 and plays a role in low-pH response. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239863  Cd Length: 192  Bit Score: 96.32  E-value: 1.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  599 FGVPPIVNVQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYD-----VADLI 673
Cdd:cd04398     1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLISPEDYEsdihsVASLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  674 KQYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIASAQ-ENQMTADSLAVCLA 752
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHEsVNRMSVNNLAIIWG 160


                  ....
gi 528479385  753 PSIL 756
Cdd:cd04398   161 PTLM 164
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 599-800 1.75e-22

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 95.83  E-value: 1.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  599 FGVPpIVNVQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYDVADLIKQYFR 678
Cdd:cd04407     1 FGVR-VGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  679 DLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIASAQE-NQMTADSLAVCLAPSILH 757
Cdd:cd04407    80 ELPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDvNRMSPNALAIVFAPCLLR 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 528479385  758 LnaskKDGASPrLISRKGGAKpdhkdlsenmaATHCLSHMITE 800
Cdd:cd04407   160 C----PDSSDP-LTSMKDVAK-----------TTTCVEMLIKE 186
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 599-767 2.64e-20

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239862  Cd Length: 213  Bit Score: 90.50  E-value: 2.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  599 FGVPPIVNVQRTGQP-----------LPQSIQQAMRYLRSQCLEKVGIFRKSGvksRIQALRQLNE---NSPDHVT-YQG 663
Cdd:cd04397     1 FGVPLEILVEKFGADstlgvgpgklrIPALIDDIISAMRQMDMSVEGVFRKNG---NIRRLKELTEeidKNPTEVPdLSK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  664 QSAYDVADLIKQYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIASAQE---- 739
Cdd:cd04397    78 ENPVQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHidee 157

                         170       180       190
                  ....*....|....*....|....*....|
gi 528479385  740 --NQMTADSLAVCLAPSILHLNASKKDGAS 767
Cdd:cd04397   158 tgSKMDIHNLATVITPNILYSKTDNPNTGD 187
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 598-758 4.60e-20

RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of FAM13A1, isoform a-like proteins. The function of FAM13A1a is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by up several orders of magnitude.


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 89.06  E-value: 4.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  598 VFGVPpIVNVQRTGQP---LPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYDVADLIK 674
Cdd:cd04393     2 VFGVP-LQELQQAGQPengVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  675 QYFRDLPEPVLTSKLTDTFLHVYQFVPAEQrLQAVQAAVIL--LPDENREVLQTLLYFLSDIASA-QENQMTADSLAVCL 751
Cdd:cd04393    81 LFLQELPEGLIPASLQIRLMQLYQDYNGED-EFGRKLRDLLqqLPPVNYSLLKFLCHFLSNVASQhHENRMTAENLAAVF 159


                  ....*..
gi 528479385  752 APSILHL 758
Cdd:cd04393   160 GPDVFHV 166
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 596-756 5.83e-20

RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239851  Cd Length: 203  Bit Score: 89.05  E-value: 5.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  596 KHVFGVPPIVNVQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALR---QLNENSPDHVTYQgQSAYDVADL 672
Cdd:cd04386     2 KPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKaalDAGTFSLPLDEFY-SDPHAVASA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  673 IKQYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIA-SAQENQMTADSLAVCL 751
Cdd:cd04386    81 LKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAqKSDENKMSPSNIAIVL 160


                  ....*
gi 528479385  752 APSIL 756
Cdd:cd04386   161 APNLL 165
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 611-816 4.31e-19

RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP19-like proteins. The function of ArhGAP19 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239857  Cd Length: 208  Bit Score: 86.75  E-value: 4.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  611 GQPLPQS----IQQAMRYLrSQCLEKVGIFRKSGVKSRIQALR-QLNENSPDHVTYQGQSAYDVADLIKQYFRDLPEPVL 685
Cdd:cd04392     2 GAPLTEEgiaqIYQLIEYL-EKNLRVEGLFRKPGNSARQQELRdLLNSGTDLDLESGGFHAHDCATVLKGFLGELPEPLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  686 TSKLTDTFLHV---YQF--------VPAEQR-LQAVQAAVILLPDENREVLQTLLYFLSDIASAQE-NQMTADSLAVCLA 752
Cdd:cd04392    81 THAHYPAHLQIadlCQFdekgnktsAPDKERlLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDkNKMSADNLALLFT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528479385  753 PSILhlnaskkdgaSPRLISRkggakpdhKDLSENmaATHC---LSHMITECKKLFQIPHEMMLQSR 816
Cdd:cd04392   161 PHLI----------CPRNLTP--------EDLHEN--AQKLnsiVTFMIKHSQKLFKAPAYLREDAR 207
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 598-756 1.21e-17

RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 82.17  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  598 VFGVPPIVNVQRTGQPLPQSIQQAMRYLRSQCLEKvGIFRKSGVKSRIQALRQL--NENSPDHVTYQG-QSAYDVADLIK 674
Cdd:cd04384     2 VFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEfdSEQIPDLTKDVYiQDIHSVSSLCK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  675 QYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIASAQE-NQMTADSLAVCLAP 753
Cdd:cd04384    81 LYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSiTNMHAKNLAIVWAP 160


                  ...
gi 528479385  754 SIL 756
Cdd:cd04384   161 NLL 163
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 599-755 1.68e-17

RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in RalBP1 proteins, also known as RLIP, RLIP76 or cytocentrin. RalBP1 plays an important role in endocytosis during interphase. During mitosis, RalBP1 transiently associates with the centromere and has been shown to play an essential role in the proper assembly of the mitotic apparatus. RalBP1 is an effector of the Ral GTPase which itself is an effector of Ras. RalBP1 contains a RhoGAP domain, which shows weak activity towards Rac1 and Cdc42, but not towards Ral, and a Ral effector domain binding motif. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 81.33  E-value: 1.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  599 FGVPPIVNVQRT----GQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQL--NENSPDHVTYQgqsAYDVADL 672
Cdd:cd04381     1 FGASLSLAVERSrchdGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAynRRESPNLEEYE---PPTVASL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  673 IKQYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSD-IASAQENQMTADSLAVCL 751
Cdd:cd04381    78 LKQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHvIAQELETKMNIQNISIVL 157


                  ....
gi 528479385  752 APSI 755
Cdd:cd04381   158 SPTV 161
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 618-756 1.10e-16

RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase regulator associated with focal adhesion kinase); Graf is a multi-domain protein, containing SH3 and PH domains, that binds focal adhesion kinase and influences cytoskeletal changes mediated by Rho proteins. Graf exhibits GAP activity toward RhoA and Cdc42, but only weakly activates Rac1. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239839  Cd Length: 203  Bit Score: 79.74  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  618 IQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQL----NENSPDHVTYQgQSAYD---VADLIKQYFRDLPEPVLTSKLT 690
Cdd:cd04374    32 VRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLgldpKTSTPGDVDLD-NSEWEiktITSALKTYLRNLPEPLMTYELH 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528479385  691 DTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAPSIL 756
Cdd:cd04374   111 NDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDhSKKNLMTVSNLGVVFGPTLL 177
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 634-756 3.44e-16

RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein) and PARG1 (PTPL1-associated RhoGAP1). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239843  Cd Length: 203  Bit Score: 78.23  E-value: 3.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  634 GIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYDVADLIKQYFRDLPEPVLTSKLTDTFLHV---YQFVPAEQR----- 705
Cdd:cd04378    36 GIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLRQLPEPLILFRLYNDFIALakeIQRDTEEDKapntp 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528479385  706 ------LQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAPSIL 756
Cdd:cd04378   116 ievnriIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEqFEENKMSPNNLGIVFGPTLI 173
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 596-756 1.10e-15

RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal SAC7 and BAG7-like proteins. Both proteins are GTPase activating proteins of Rho1, but differ functionally in vivo: SAC7, but not BAG7, is involved in the control of Rho1-mediated activation of the PKC-MPK1 pathway. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239861  Cd Length: 225  Bit Score: 77.45  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  596 KHVFGVPPIVnVQRTGQplpqsiqqamrYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDH---VTYQGQSAYDVADL 672
Cdd:cd04396    26 QYVYGYIPVV-VAKCGV-----------YLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDYgksFDWDGYTVHDAASV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  673 IKQYFRDLPEPVLTSKLTDTFLHVYQFVPA-----------------EQRLQAVQAAVILLPDENREVLQTLLYFLSDIA 735
Cdd:cd04396    94 LRRYLNNLPEPLVPLDLYEEFRNPLRKRPRilqymkgrineplntdiDQAIKEYRDLITRLPNLNRQLLLYLLDLLAVFA 173

                         170       180
                  ....*....|....*....|..
gi 528479385  736 S-AQENQMTADSLAVCLAPSIL 756
Cdd:cd04396   174 RnSDKNLMTASNLAAIFQPGIL 195
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 612-773 1.89e-15

RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXA. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239871  Cd Length: 186  Bit Score: 75.81  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  612 QPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYDVADLIKQYFRDLPEPVLTSKLTD 691
Cdd:cd04406    13 RSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  692 TFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIASAQE-NQMTADSLAVCLAPSILHLNASKKDGASPRL 770
Cdd:cd04406    93 EFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEEtNRMSANALAIVFAPCILRCPDTTDPLQSVQD 172


                  ...
gi 528479385  771 ISR 773
Cdd:cd04406   173 ISK 175
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 608-757 2.94e-15

RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15, 12 and 9-like proteins; This subgroup of ARHGAPs are multidomain proteins that contain RhoGAP, PH, SH3 and WW domains. Most members that are studied show GAP activity towards Rac1, some additionally show activity towards Cdc42. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 75.12  E-value: 2.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  608 QRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQL--NENSPDHVTYQGQSAYDVADLIKQYFRDLPEPVL 685
Cdd:cd04403    10 QRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAvdHDEKLDLDDSKWEDIHVITGALKLFFRELPEPLF 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528479385  686 TSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSD-IASAQENQMTADSLAVCLAPSILH 757
Cdd:cd04403    90 PYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRvIEHGEKNRMTTQNLAIVFGPTLLR 162
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 599-765 2.07e-14

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 73.04  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  599 FGVPPIVNVQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALR-QLNENSPDHVTYqgQSAYDV---ADLIK 674
Cdd:cd04387     1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKaAFDTNNKDVSVM--LSEMDVnaiAGTLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  675 QYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIASAQE-NQMTADSLAVCLAP 753
Cdd:cd04387    79 LYFRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEvNKMSLHNLATVFGP 158

                         170
                  ....*....|..
gi 528479385  754 SILHLNASKKDG 765
Cdd:cd04387   159 TLLRPSEKESKI 170
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 607-757 8.22e-14

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239848  Cd Length: 188  Bit Score: 70.91  E-value: 8.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  607 VQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQgQSAYD---VADLIKQYFRDLPEP 683
Cdd:cd04383    11 IQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADD-QNDHDinsVAGVLKLYFRGLENP 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528479385  684 VLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAPSILH 757
Cdd:cd04383    90 LFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQfSDENMMDPYNLAICFGPTLMP 164
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 599-756 8.68e-14

RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p190-like proteins. p190, also named RhoGAP5, plays a role in neuritogenesis and axon branch stability. p190 shows a preference for Rho, over Rac and Cdc42, and consists of an N-terminal GTPase domain and a C-terminal GAP domain. The central portion of p190 contains important regulatory phosphorylation sites. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239838  Cd Length: 185  Bit Score: 70.95  E-value: 8.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  599 FGVPpIVNVQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQAL-RQLNENSPDHVTYQGQSAYDVADLIKQYF 677
Cdd:cd04373     1 FGVP-LANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLqKQFDQDHNLDLVSKDFTVNAVAGALKSFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  678 RDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIA-SAQENQMTADSLAVCLAPSIL 756
Cdd:cd04373    80 SELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSqNSKVNLMTSENLSICFWPTLM 159
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 614-756 4.03e-13

RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239873  Cd Length: 200  Bit Score: 69.46  E-value: 4.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  614 LPQSIQQAMRYLRSQCLEKV--------GIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYDVADLIKQYFRDLPEPVL 685
Cdd:cd04408     8 LPRDFPEEVPFVVVRCTAEIenralgvqGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLKELPEPVL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  686 TSKLTDTFLHVYQFV------------PAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIASA-QENQMTADSLAVCLA 752
Cdd:cd04408    88 PFQLYDDFIALAKELqrdsekaaespsIVENIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERfEDNKMSPNNLGIVFG 167


                  ....
gi 528479385  753 PSIL 756
Cdd:cd04408   168 PTLL 171
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 630-755 9.36e-13

RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239860  Cd Length: 196  Bit Score: 68.20  E-value: 9.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  630 LEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYD---VADLIKQYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRL 706
Cdd:cd04395    34 LETVGIYRVPGNNAAISALQEELNRGGFDIDLQDPRWRDvnvVSSLLKSFFRKLPEPLFTNELYPDFIEANRIEDPVERL 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 528479385  707 QAVQAAVILLPDENREVLQTLLYFLSDIA-SAQENQMTADSLAVCLAPSI 755
Cdd:cd04395   114 KELRRLIHSLPDHHYETLKHLIRHLKTVAdNSEVNKMEPRNLAIVFGPTL 163
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 607-756 1.37e-12

RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239837 [Multi-domain]  Cd Length: 194  Bit Score: 67.54  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  607 VQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHvTYQGQSAYDVADLI----KQYFRDLPE 682
Cdd:cd04372     9 VKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEK-ADISATVYPDINVItgalKLYFRDLPI 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528479385  683 PVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAPSIL 756
Cdd:cd04372    88 PVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLhEKDNKMNAENLGIVFGPTLM 162
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 599-794 4.51e-12

RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in SYD-1_like proteins. Syd-1, first identified and best studied in C.elegans, has been shown to play an important role in neuronal development by specifying axonal properties. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239844  Cd Length: 207  Bit Score: 66.34  E-value: 4.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  599 FGVP--PIVNVQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYDV---ADLI 673
Cdd:cd04379     1 FGVPlsRLVEREGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEELYPDInviTGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  674 KQYFRDLPEPVLTSKLTDTFLHVYQFVPAEQRLQAVQAAVIL---LPDENREVLQTLLYFLSDIASAQE-NQMTADSLAV 749
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHLTLSIidcLPLSAKATLLLLLDHLSLVLSNSErNKMTPQNLAV 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 528479385  750 CLAPSIL-HLNASKKDGASPRLISRKGGAKpDHKDLSENMaatHCL 794
Cdd:cd04379   161 CFGPVLMfCSQEFSRYGISPTSKMAAVSTV-DFKQHIEVL---HYL 202
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 599-756 1.89e-11

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239874  Cd Length: 211  Bit Score: 64.83  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  599 FGVPPIVNVQRTGQPLPQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNENSPDHVTYQGQSAYDVADLIKQYFR 678
Cdd:cd04409     1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  679 DLPEPVLTSKLTDTF-------LHVYQFVPAEQRLQAVQAAV------IL---------LPDENREVLQTLLYFLSDIAS 736
Cdd:cd04409    81 QLPEPLILFRLYNEFiglakesQHVNETQEAKKNSDKKWPNMctelnrILlkskdllrqLPAPNYNTLQFLIVHLHRVSE 160

                         170       180
                  ....*....|....*....|.
gi 528479385  737 -AQENQMTADSLAVCLAPSIL 756
Cdd:cd04409   161 qAEENKMSASNLGIIFGPTLI 181
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 608-756 3.40e-11

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 63.62  E-value: 3.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  608 QRTGQPL-PQSIQQAMRYLRSQCLEKVGIFRKSGVKSRIQALRQLNEnSPDHVTYQGQS-AYDVADLIKQYFRDLPEPVL 685
Cdd:cd04390    15 RKFGPRLvPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFD-AGERPSFDSDTdVHTVASLLKLYLRELPEPVI 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528479385  686 TSKLTDTFLHVYQFVPA--EQRLQAVQAAVILLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAPSIL 756
Cdd:cd04390    94 PWAQYEDFLSCAQLLSKdeEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSnSSVNKMSVQNLATVFGPNIL 167
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 598-755 1.75e-10

RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 61.22  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  598 VFGVP-----PIVNVQRTGQPLPQSIQQAMRYLRSQ-CLEKVGIFRKSGVKSRIQALR-QLNENSpDHVTYQGQSAYD-- 668
Cdd:cd04400     1 IFGSPleeavELSSHKYNGRDLPSVVYRCIEYLDKNrAIYEEGIFRLSGSASVIKQLKeRFNTEY-DVDLFSSSLYPDvh 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  669 -VADLIKQYFRDLPEPVLTSKLTDTFLHVyqfvpAEQRLQAVQAAVIL------LPDENREVLQTLLYFLSDI-ASAQEN 740
Cdd:cd04400    80 tVAGLLKLYLRELPTLILGGELHNDFKRL-----VEENHDRSQRALELkdlvsqLPQANYDLLYVLFSFLRKIiEHSDVN 154

                         170
                  ....*....|....*
gi 528479385  741 QMTADSLAVCLAPSI 755
Cdd:cd04400   155 KMNLRNVCIVFSPTL 169
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 630-755 9.33e-10

RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in MgcRacGAP proteins. MgcRacGAP plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling. ii) after phosphorylation by aurora B MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain a N-terminal C1-like domain, and a C-terminal RhoGAP domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239847  Cd Length: 193  Bit Score: 59.23  E-value: 9.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  630 LEKVGIFRKSGVKSRIQALRQ--LNENSPDHVtyqgqSAYDVADL---IKQYFRDLPEPVLTSKLTDTFLHVYQFVPAEQ 704
Cdd:cd04382    33 LTEEGLYRVSGSEREVKALKEkfLRGKTVPNL-----SKVDIHVIcgcLKDFLRSLKEPLITFALWKEFMEAAEILDEDN 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528479385  705 RLQAVQAAVILLPDENREVLQTLLYFLSDIASAQENQMTADSLAVCLAPSI 755
Cdd:cd04382   108 SRAALYQAISELPQPNRDTLAFLILHLQRVAQSPECKMDINNLARVFGPTI 158
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 634-756 6.85e-08

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239854  Cd Length: 187  Bit Score: 53.55  E-value: 6.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  634 GIFRKSGVKSRIQALR-QLNE-NSPDHVTyqgQSAYDVADLIKQYFRDLPEPVLTSKLTDTFLHVYqfvpaEQRLQAVqA 711
Cdd:cd04389    42 GIFRVPGDIDEVNELKlRVDQwDYPLSGL---EDPHVPASLLKLWLRELEEPLIPDALYQQCISAS-----EDPDKAV-E 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 528479385  712 AVILLPDENREVLQTLLYFLSDIA---SAQENQMTADSLAVCLAPSIL 756
Cdd:cd04389   113 IVQKLPIINRLVLCYLINFLQVFAqpeNVAHTKMDVSNLAMVFAPNIL 160
RhoGAP_BRCC3-like cd04405
RhoGAP_BRCC3-like: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 597-739 1.43e-07

RhoGAP_BRCC3-like: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of BRCC3-like proteins. This subgroup also contains two groups of closely related proteins, BRCC3 and DEPDC7, which both contain a C-terminal RhoGAP-like domain and an N-terminal DEP (Disheveled, Egl-10, and Pleckstrin) domain. The function(s) of BRCC3 and DEPDC7 are unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239870  Cd Length: 235  Bit Score: 53.49  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  597 HVFGVPPIVNVQRTGQPLPQSIQQAMR--YLRSQCL--EKVGIFRKSGVKSRIQALRQLNENSPDHV-------TYQGQS 665
Cdd:cd04405    20 QLVGLPLLEELLDPALVNPKHISYNMDpdVYTSNYLdrEVVKLFSKSQLDHWLLSAMDCLANWPDQLvvdvsrpLYSQHD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  666 AY-----DVADLIKQYFRDLPEPVLTSKLTDTF---LHVYQFVPAEQRLQAVQAAVILLPDENREVLQTLLYFLSDIASA 737
Cdd:cd04405   100 MLsgfkrLLFKTIAKYYGQLKEPLLTFHLFDIFvgiLELLGNGKEEVALEALQLCLLLLPPASRRELRRLLRFMARAAKN 179


                  ..
gi 528479385  738 QE 739
Cdd:cd04405   180 DM 181
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 842-1016 1.50e-07

Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD4, -5, and -6. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD4 plays an important role in steroidogenesis, trafficking cholesterol into mitochondria. It specifically binds cholesterol, and demonstrates limited binding to another sterol, 7a-hydroxycholesterol. STARD4 and STARD5 are ubiquitously expressed, with highest levels in liver and kidney. STRAD5 functions in the kidney within the proximal tubule cells where it is associated with the Endoplasmic Reticulum (ER), and may participate in ER-associated cholesterol transport. It binds cholesterol and 25-hydroxycholesterol. Expression of the gene encoding STARD5 is increased by ER stress, and its mRNA and protein levels are elevated in a type I diabetic mouse model of human diabetic nephropathy. STARD6 is expressed in male germ cells of normal rats, and in the steroidogenic Leydig cells of perinatal hypothyroid testes. It may play a pivotal role in the steroidogenesis as well as in the spermatogenesis of normal rats. STARD6 has also been detected in the rat nervous system, and may participate in neurosteroid synthesis.


Pssm-ID: 176876  Cd Length: 206  Bit Score: 53.23  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  842 DYRAYLEDNVQCLLREASERSkGWHHAHGPDNTELAYKKVG--DGHpmrIWRVSVEIEAPPS----VVLQRVLRERHLWD 915
Cdd:cd08867     2 DFKVIAEKLANEALQYINDTD-GWKVLKTVKNITVSWKPSTefTGH---LYRAEGIVDALPEkvidVIIPPCGGLRLKWD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  916 EDLLHSRVIETLENNTEVFHYITDS--MAPHPRRNFITLrRWCSDLPKGVCVLVSSSVDHDNVQLEAGLravlltSRMFI 993
Cdd:cd08867    78 KSLKHYEVLEKISEDLCVGRTITPSaaMGLISPRDFVDL-VYVKRYEDNQWSSSGKSVDIPERPPTPGF------VRGYN 150

                         170       180       190
                  ....*....|....*....|....*....|..
gi 528479385  994 EPCGMG---------RSRLTHYCRADLRGRSP 1016
Cdd:cd08867   151 HPCGYFcsplkgspdKSFLVLYVQTDLRGMIP 182
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 855-1022 2.22e-07

Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD10 (also known as CGI-52, PTCP-like, and SDCCAG28). The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD10 binds phophatidylcholine and phosphatidylethanolamine. This protein is widely expressed and is synthesized constitutively in many organs. It may function in the liver in the export of phospholipids into bile. It is concentrated in the sperm flagellum, and may play a role in energy metabolism. In the mammary gland it may participate in the enrichment of lipids in milk, and be a potential marker of differentiation. Its expression is induced in this gland during gestation and lactation. It is overexpressed in mammary tumors from Neu/ErbB2 transgenic mice, in several breast carcinoma cell lines, and in 35% of primary human breast cancers, and may cooperate with c-erbB receptor signaling in breast oncogenesis. It is a potential marker of disease outcome in breast cancer; loss of STARD10 expression in breast cancer strongly predicts an aggressive disease course. The lipid transfer activity of STRAD10 is downregulated by phosphorylation of its Ser284 by CK2 (casein kinase 2).


Pssm-ID: 176880  Cd Length: 222  Bit Score: 52.64  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  855 LREASERSKGWHHAHGPDNTELAYKKVgDGHPMRIWRVSVEIEAPPSVVLQRVLRE---RHLWDEDLLHSRVIETLENNT 931
Cdd:cd08871    15 FKKLCDSTDGWKLKYNKNNVKVWTKNP-ENSSIKMIKVSAIFPDVPAETLYDVLHDpeyRKTWDSNMIESFDICQLNPNN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  932 EVFHYITDSMAPHPRRNFITLRRW-CSDlpkGVCVLVSSSVDHDNVQLEAGL-RAVLLTSRMFIEPCGMGRSRLTHYCRA 1009
Cdd:cd08871    94 DIGYYSAKCPKPLKNRDFVNLRSWlEFG---GEYIIFNHSVKHKKYPPRKGFvRAISLLTGYLIRPTGPKGCTLTYVTQN 170

                         170
                  ....*....|....
gi 528479385 1010 DLRGRSPDWY-NKV 1022
Cdd:cd08871   171 DPKGSLPKWVvNKA 184
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
12-75 2.70e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 45.72  E-value: 2.70e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528479385    12 HELEAKDACEWLRAAGFPQYAQLYEASLFPIEISAVRRDHEFLDQDSLKALCRRLTTLNKCAAM 75
Cdd:pfam07647    2 ESWSLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQEL 65
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 624-773 6.13e-06

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239845  Cd Length: 220  Bit Score: 48.49  E-value: 6.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  624 YLRSQCLEKVGIFRKSGVKS----RIQALRQ-LNENSPDHVTYqgqSAYDVADLIKQYFRDLPEPVLTSKLTDTfLHVYQ 698
Cdd:cd04380    60 YLYTRGLAQEGLFEEPGLPSepgeLLAEIRDaLDTGSPFNSPG---SAESVAEALLLFLESLPDPIIPYSLYER-LLEAV 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  699 FVPAEQRLQAVQAAvilLPDENREVLQTLLYFLSDIAS-AQENQMTADSLAVCLAPSILH----LNASKKDGASPRLISR 773
Cdd:cd04380   136 ANNEEDKRQVIRIS---LPPVHRNVFVYLCSFLRELLSeSADRGLDENTLATIFGRVLLRdpprAGGKERRAERDRKRAF 212
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 669-756 1.74e-03

RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239864  Cd Length: 212  Bit Score: 41.16  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  669 VADLIKQYFRDLPEPVLTSKLTDTFLHVYQFVPA------EQRLQAVQAAVILLPDEN---REVLQTLLYFLSDIASAQE 739
Cdd:cd04399    81 VASVLKLYLLELPDSLIPHDIYDLIRSLYSAYPPsqedsdTARIQGLQSTLSQLPKSHiatLDAIITHFYRLIEITKMGE 160

                          90
                  ....*....|....*...
gi 528479385  740 NQMT-ADSLAVCLAPSIL 756
Cdd:cd04399   161 SEEEyADKLATSLSREIL 178
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 867-1022 5.37e-03

Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain family; Functionally uncharacterized subgroup of the START domain family. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. For some mammalian members of the START family (STARDs), it is known which lipids bind in this pocket; these include cholesterol (STARD1, -3, -4, and -5), 25-hydroxycholesterol (STARD5), phosphatidylcholine (STARD2, -7, and -10), phosphatidylethanolamine (STARD10) and ceramides (STARD11). Mammalian STARDs participate in the control of various cellular processes, including lipid trafficking between intracellular compartments, lipid metabolism, and modulation of signaling events. Mutation or altered expression of STARDs is linked to diseases such as cancer, genetic disorders, and autoimmune disease.


Pssm-ID: 176885  Cd Length: 195  Bit Score: 39.18  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  867 HAHGPDNT-ELAYKKVG--------DGHPMRIWRVSVEIEAPPSVVLQrVLR--ER-HLWDEDLLHSRVIETLENNTEVF 934
Cdd:cd08876    11 AALAPDGDwQLVKDKDGikvytrdvEGSPLKEFKAVAEVDASIEAFLA-LLRdtESyPQWMPNCKESRVLKRTDDNERSV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479385  935 HYITDsmAPHP--RRNFITLRRWCSDLPKGVCVLVSSSVDHDNVQLEAGLRAVLLTSRMFIEPCGMGRSRLTHYCRADLR 1012
Cdd:cd08876    90 YTVID--LPWPvkDRDMVLRSTTEQDADDGSVTITLEAAPEALPEQKGYVRIKTVEGQWTFTPLGNGKTRVTYQAYADPG 167

                         170
                  ....*....|.
gi 528479385 1013 GRSPDW-YNKV 1022
Cdd:cd08876   168 GSIPGWlANAF 178
 
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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