NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034180038|ref|XP_016814601|]
View 

rho GTPase-activating protein 7 isoform X1 [Pan troglodytes]

Protein Classification

rho GTPase-activating protein 7( domain architecture ID 10176039)

rho GTPase-activating protein 7 (ARHGAP7), also called deleted in liver cancer 1 protein (DLC1), functions as a GTPase-activating protein for the small GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream signaling.

CATH:  3.30.530.20|1.10.555.10
Gene Ontology:  GO:0005488|GO:0007165|GO:0005096|GO:0051056
PubMed:  26427649|18922149|15246431|17222083|12480336|28163190|15928333|18831011
SCOP:  3000738|4001255

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
START_STARD12-like cd08908
C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also ...
 1315-1518 8.24e-149

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: 451.77  E-value: 8.24e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1315 NDDSADYQHFLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVSEGPPLRLWRSIIEVPAVPEEILKRLLKEQHLWDV 1394
Cdd:cd08908      1 NDEPADYHHFLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVSEGPPLRLWRTTIEVPAAPEEILKRLLKEQHLWDV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1395 DLLDSKVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWRTNLPKGACALLLTSVDHDRAPVVGVRVNVLLSRYLIEPCG 1474
Cdd:cd08908     81 DLLDSKVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWRTNLPKGACALLATSVDHDRAPVAGVRVNVLLSRYLIEPCG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1034180038 1475 PGKSKLTYMCRVDLRGHMPEWYTKSFGHLCAAEVVKIRDSFSNQ 1518
Cdd:cd08908    161 SGKSKLTYMCRIDLRGHMPEWYTKSFGHLCAAEVVKIRDSFSNQ 204
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1072-1290 2.04e-143

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: 438.00  E-value: 2.04e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1072 DRSVFGVPLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAIDCVNYEGQSAYDVADMLK 1151
Cdd:cd04375      1 DKNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1152 QYFRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAP 1231
Cdd:cd04375     81 QYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAP 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1232 SLFHLNTLKRENSSP-RVMQRKQSLGKPDQKDLNENLAATQGLAHMIAECKKLFQVPEEM 1290
Cdd:cd04375    161 SLFHLNTSRRENSSPaRRMQRKKSLGKPDQKELSENKAAHQCLAYMIEECNTLFMVPKEM 220
SAM_DLC1 cd09591
SAM domain of DLC1 subfamily; SAM (sterile alpha motif) domain of DLC1 (Deleted in liver ...
 454-513 2.07e-37

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: 134.76  E-value: 2.07e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038  454 KEACDWLRATGFPQYAQLYEDFLFPIDISLVKREHDFLDRDAIEALCRRLNTLNKCAVMK 513
Cdd:cd09591      1 KEACDWLRAAGFPQYAQLYEDLLFPIDIELVKREHDFLDRDAIEALCRRLNTLNKCAVMK 60
 
Name Accession Description Interval E-value
START_STARD12-like cd08908
C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also ...
 1315-1518 8.24e-149

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: 451.77  E-value: 8.24e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1315 NDDSADYQHFLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVSEGPPLRLWRSIIEVPAVPEEILKRLLKEQHLWDV 1394
Cdd:cd08908      1 NDEPADYHHFLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVSEGPPLRLWRTTIEVPAAPEEILKRLLKEQHLWDV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1395 DLLDSKVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWRTNLPKGACALLLTSVDHDRAPVVGVRVNVLLSRYLIEPCG 1474
Cdd:cd08908     81 DLLDSKVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWRTNLPKGACALLATSVDHDRAPVAGVRVNVLLSRYLIEPCG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1034180038 1475 PGKSKLTYMCRVDLRGHMPEWYTKSFGHLCAAEVVKIRDSFSNQ 1518
Cdd:cd08908    161 SGKSKLTYMCRIDLRGHMPEWYTKSFGHLCAAEVVKIRDSFSNQ 204
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1072-1290 2.04e-143

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: 438.00  E-value: 2.04e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1072 DRSVFGVPLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAIDCVNYEGQSAYDVADMLK 1151
Cdd:cd04375      1 DKNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1152 QYFRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAP 1231
Cdd:cd04375     81 QYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAP 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1232 SLFHLNTLKRENSSP-RVMQRKQSLGKPDQKDLNENLAATQGLAHMIAECKKLFQVPEEM 1290
Cdd:cd04375    161 SLFHLNTSRRENSSPaRRMQRKKSLGKPDQKELSENKAAHQCLAYMIEECNTLFMVPKEM 220
START pfam01852
START domain;
1323-1522 3.46e-58

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 199.55  E-value: 3.46e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1323 HFLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKV--SEGPPLRLWRSIIEVPA-VPEEILKRLLKeQHLWDVDLLDS 1399
Cdd:pfam01852    1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVepDHGEASRASGVVPMVAAlLVAELLKDMEY-RAQWDKDVRSA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1400 KVIEILDSQTEIYQYVQNSMA--PHPARDYVVLRTWRTnLPKGACALLLTSVDHDRAPVV--GVRVNVLLSRYLIEPCGP 1475
Cdd:pfam01852   80 ETLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWRR-LGGGVYVIVDRSVTHPQFPPSsgYVRAERLPSGYLIQPCGN 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034180038 1476 GKSKLTYMCRVDLRGHMPEWYTKSFGHLCAAEVVKIRDSFSNQNTET 1522
Cdd:pfam01852  159 GPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 1089-1252 1.40e-51

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: 179.38  E-value: 1.40e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038  1089 QPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQM-NEGAIDCVNYEGQSAYDVADMLKQYFRDLPEPLMTNKLS 1167
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAfDSGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038  1168 ETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSLFHLNTLKRENSSPR 1247
Cdd:smart00324   81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160


                    ....*
gi 1034180038  1248 VMQRK 1252
Cdd:smart00324  161 RHQNT 165
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 1092-1235 4.12e-49

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 171.19  E-value: 4.12e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1092 PQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQM-NEGAIDCVNYEGQSAYDVADMLKQYFRDLPEPLMTNKLSETF 1170
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAfDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034180038 1171 LQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSLFH 1235
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLR 145
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 1326-1510 2.06e-48

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 171.46  E-value: 2.06e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038  1326 QDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVS----EGPPLRLWRSIIEVPA-VPEEILKRLlKEQHLWDVDLLDSK 1400
Cdd:smart00234    3 EEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSpgrkPGEAFRLVGVVPMVCAdLVEELMDDL-EYRPEWDKNVAKAE 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038  1401 VIEILDSQTEIYQYVQNSMA-PHPARDYVVLRTWRTNlPKGACALLLTSVDHDRAP--VVGVRVNVLLSRYLIEPCGPGK 1477
Cdd:smart00234   82 TLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWRED-EDGSYAVVDVSVTHPTSPpeSGYVRAENLPSGLLIEPLGNGP 160

                           170       180       190
                    ....*....|....*....|....*....|...
gi 1034180038  1478 SKLTYMCRVDLRGHMPEWYTKSFGHLCAAEVVK 1510
Cdd:smart00234  161 SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAK 193
SAM_DLC1 cd09591
SAM domain of DLC1 subfamily; SAM (sterile alpha motif) domain of DLC1 (Deleted in liver ...
 454-513 2.07e-37

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: 134.76  E-value: 2.07e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038  454 KEACDWLRATGFPQYAQLYEDFLFPIDISLVKREHDFLDRDAIEALCRRLNTLNKCAVMK 513
Cdd:cd09591      1 KEACDWLRAAGFPQYAQLYEDLLFPIDIELVKREHDFLDRDAIEALCRRLNTLNKCAVMK 60
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
452-513 1.41e-09

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 55.35  E-value: 1.41e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034180038  452 EAKEACDWLRATGFPQYAQLYEDFLFPIDISLVKREHDFLDRDAIEALCRRLNTLNKCAVMK 513
Cdd:pfam07647    5 SLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 454-513 5.28e-06

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 45.36  E-value: 5.28e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038   454 KEACDWLRATGFPQYAQLYEDFLFPIDISLVKREHDFLDRDAIEALCRRLNTLNKCAVMK 513
Cdd:smart00454    7 ESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
 
Name Accession Description Interval E-value
START_STARD12-like cd08908
C-terminal lipid-binding START domain of mammalian STARD12 and related proteins, which also ...
 1315-1518 8.24e-149

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: 451.77  E-value: 8.24e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1315 NDDSADYQHFLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVSEGPPLRLWRSIIEVPAVPEEILKRLLKEQHLWDV 1394
Cdd:cd08908      1 NDEPADYHHFLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVSEGPPLRLWRTTIEVPAAPEEILKRLLKEQHLWDV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1395 DLLDSKVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWRTNLPKGACALLLTSVDHDRAPVVGVRVNVLLSRYLIEPCG 1474
Cdd:cd08908     81 DLLDSKVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWRTNLPKGACALLATSVDHDRAPVAGVRVNVLLSRYLIEPCG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1034180038 1475 PGKSKLTYMCRVDLRGHMPEWYTKSFGHLCAAEVVKIRDSFSNQ 1518
Cdd:cd08908    161 SGKSKLTYMCRIDLRGHMPEWYTKSFGHLCAAEVVKIRDSFSNQ 204
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1072-1290 2.04e-143

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: 438.00  E-value: 2.04e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1072 DRSVFGVPLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAIDCVNYEGQSAYDVADMLK 1151
Cdd:cd04375      1 DKNVFGVPLLVNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1152 QYFRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAP 1231
Cdd:cd04375     81 QYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAP 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1232 SLFHLNTLKRENSSP-RVMQRKQSLGKPDQKDLNENLAATQGLAHMIAECKKLFQVPEEM 1290
Cdd:cd04375    161 SLFHLNTSRRENSSPaRRMQRKKSLGKPDQKELSENKAAHQCLAYMIEECNTLFMVPKEM 220
START_RhoGAP cd08869
C-terminal lipid-binding START domain of mammalian STARD8, -12, -13 and related proteins, ...
 1323-1518 3.87e-114

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: 357.77  E-value: 3.87e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1323 HFLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVSEGPPLRLWRSIIEVPAVPEEILKRLLKEQHLWDVDLLDSKVI 1402
Cdd:cd08869      1 SYLERCVQDLLREARDKSKGWVSVSSSDHVELAFKKVDDGHPLRLWRASTEVEAPPEEVLQRILRERHLWDDDLLQWKVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1403 EILDSQTEIYQYVQNSMAPHPARDYVVLRTWRTNLPKGACALLLTSVDH-DRAPVVGVRVNVLLSRYLIEPCGPGKSKLT 1481
Cdd:cd08869     81 ETLDEDTEVYQYVTNSMAPHPTRDYVVLRTWRTDLPKGACVLVETSVEHtEPVPLGGVRAVVLASRYLIEPCGSGKSRVT 160

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1034180038 1482 YMCRVDLRGHMPEWYTKSFGHLCAAEVVKIRDSFSNQ 1518
Cdd:cd08869    161 HICRVDLRGRSPEWYNKVYGHLCARELLRIRDSFRQL 197
START_STARD13-like cd08909
C-terminal lipid-binding START domain of mammalian STARD13 and related proteins, which also ...
 1316-1515 1.35e-94

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: 303.76  E-value: 1.35e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1316 DDSADYQHFLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVSEGPPLRLWRSIIEVPAVPEEILKRLLKEQHLWDVD 1395
Cdd:cd08909      2 EEGGTYQTYLESLIQNLQKEAKEKFKGWISCSSSDNTELAYKKVGDGNPLRLWKVSVEVEAPPSVVLNRVLRERHLWDED 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1396 LLDSKVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWRTNLPKGACALLLTSVDHDRAPVVG-VRVNVLLSRYLIEPCG 1474
Cdd:cd08909     82 FLQWKVVETLDKQTEVYQYVLNCMAPHPSRDFVVLRSWRTDLPKGACSLVSVSVEHEEAPLLGgVRAVVLDSQYLIEPCG 161

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1034180038 1475 PGKSKLTYMCRVDLRGHMPEWYTKSFGHLCAAEVVKIRDSF 1515
Cdd:cd08909    162 SGKSRLTHICRVDLKGHSPEWYNKGFGHLCAAEAARIRNSF 202
START_STARD8-like cd08907
C-terminal lipid-binding START domain of mammalian STARD8 and related proteins, which also ...
 1320-1515 2.16e-83

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: 271.79  E-value: 2.16e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1320 DYQHFLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVSEGPPLRLWRSIIEVPAVPEEILKRLLKEQHLWDVDLLDS 1399
Cdd:cd08907      6 DLRAYLEDNVQCLLREASERFKGWHSAPGPDNTELACKKVGDGHPLRLWKVSTEVEAPPSVVLQRVLRERHLWDEDLLHS 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1400 KVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWRTNLPKGACALLLTSVDHDR-APVVGVRVNVLLSRYLIEPCGPGKS 1478
Cdd:cd08907     86 QVIEALENNTEVYHYVTDSMAPHPRRDFVVLRMWRSDLPRGGCLLVSQSVDHDNpQLEAGVRAVLLTSQYLIEPCGMGRS 165

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1034180038 1479 KLTYMCRVDLRGHMPEWYTKSFGHLCAAEVVKIRDSF 1515
Cdd:cd08907    166 RLTHICRADLRGRSPDWYNKVFGHLCAMEVARIRDSF 202
START pfam01852
START domain;
1323-1522 3.46e-58

START domain;


Pssm-ID: 426476  Cd Length: 205  Bit Score: 199.55  E-value: 3.46e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1323 HFLQDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKV--SEGPPLRLWRSIIEVPA-VPEEILKRLLKeQHLWDVDLLDS 1399
Cdd:pfam01852    1 ELAEEAAQELLKLALSDEPGWVLLSSNENGDVVLQIVepDHGEASRASGVVPMVAAlLVAELLKDMEY-RAQWDKDVRSA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1400 KVIEILDSQTEIYQYVQNSMA--PHPARDYVVLRTWRTnLPKGACALLLTSVDHDRAPVV--GVRVNVLLSRYLIEPCGP 1475
Cdd:pfam01852   80 ETLEVISSGGDLQYYVAALVApsPLSPRDFVFLRYWRR-LGGGVYVIVDRSVTHPQFPPSsgYVRAERLPSGYLIQPCGN 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034180038 1476 GKSKLTYMCRVDLRGHMPEWYTKSFGHLCAAEVVKIRDSFSNQNTET 1522
Cdd:pfam01852  159 GPSKVTWVSHADLKGWLPSWLLRSLYKSGMPEGAKTWVATLQRLCEK 205
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 1089-1252 1.40e-51

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: 179.38  E-value: 1.40e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038  1089 QPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQM-NEGAIDCVNYEGQSAYDVADMLKQYFRDLPEPLMTNKLS 1167
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAfDSGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038  1168 ETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSLFHLNTLKRENSSPR 1247
Cdd:smart00324   81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160


                    ....*
gi 1034180038  1248 VMQRK 1252
Cdd:smart00324  161 RHQNT 165
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 1092-1235 4.12e-49

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 171.19  E-value: 4.12e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1092 PQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQM-NEGAIDCVNYEGQSAYDVADMLKQYFRDLPEPLMTNKLSETF 1170
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAfDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034180038 1171 LQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSLFH 1235
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLR 145
START smart00234
in StAR and phosphatidylcholine transfer protein; putative lipid-binding domain in StAR and ...
 1326-1510 2.06e-48

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


Pssm-ID: 214575  Cd Length: 205  Bit Score: 171.46  E-value: 2.06e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038  1326 QDCVDGLFKEVKEKFKGWVSYSTSEQAELSYKKVS----EGPPLRLWRSIIEVPA-VPEEILKRLlKEQHLWDVDLLDSK 1400
Cdd:smart00234    3 EEAAAELLKMAAASEEGWVLSSENENGDEVRSIFSpgrkPGEAFRLVGVVPMVCAdLVEELMDDL-EYRPEWDKNVAKAE 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038  1401 VIEILDSQTEIYQYVQNSMA-PHPARDYVVLRTWRTNlPKGACALLLTSVDHDRAP--VVGVRVNVLLSRYLIEPCGPGK 1477
Cdd:smart00234   82 TLEVIDNGTVIYHYVSKFAAgPVSPRDFVFVRYWRED-EDGSYAVVDVSVTHPTSPpeSGYVRAENLPSGLLIEPLGNGP 160

                           170       180       190
                    ....*....|....*....|....*....|...
gi 1034180038  1478 SKLTYMCRVDLRGHMPEWYTKSFGHLCAAEVVK 1510
Cdd:smart00234  161 SKVTWVSHADLKGWLPHWLVRSLIKSGLAEFAK 193
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 1092-1245 4.33e-44

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: 157.85  E-value: 4.33e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1092 PQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAIDCVNYEGQSAYDVADMLKQYFRDLPEPLMTNKLSETFL 1171
Cdd:cd00159      1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034180038 1172 QIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSLFHLNTLKRENSS 1245
Cdd:cd00159     81 ELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELLE 154
SAM_DLC1 cd09591
SAM domain of DLC1 subfamily; SAM (sterile alpha motif) domain of DLC1 (Deleted in liver ...
 454-513 2.07e-37

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: 134.76  E-value: 2.07e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038  454 KEACDWLRATGFPQYAQLYEDFLFPIDISLVKREHDFLDRDAIEALCRRLNTLNKCAVMK 513
Cdd:cd09591      1 KEACDWLRAAGFPQYAQLYEDLLFPIDIELVKREHDFLDRDAIEALCRRLNTLNKCAVMK 60
SAM_DLC1,2-like cd09538
SAM domain of DLC1,2-like subfamily; SAM (sterile alpha motif) domain of DLC-1,2-like (Deleted ...
 454-513 9.54e-37

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: 132.54  E-value: 9.54e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038  454 KEACDWLRATGFPQYAQLYEDFLFPIDISLVKREHDFLDRDAIEALCRRLNTLNKCAVMK 513
Cdd:cd09538      1 KEACKWLRAAGFPQYAQLYEDSQFPIDISAVKRDHDFLDRDSLQALIRRLNTLNKCASMK 60
SAM_DLC2 cd09592
SAM domain of STARD13-like subfamily; SAM (sterile alpha motif) domain of DLC2 (Deleted in ...
 450-513 6.39e-35

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: 127.45  E-value: 6.39e-35
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034180038  450 EIEAKEACDWLRATGFPQYAQLYEDFLFPIDISLVKREHDFLDRDAIEALCRRLNTLNKCAVMK 513
Cdd:cd09592      1 EIEAKEACDWLRAAGFPQYAQLYEDSQFPIDIASVKRDHDFLDRDLVEPLCRRLNTLNKCASMK 64
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1091-1290 6.80e-31

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: 121.39  E-value: 6.80e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1091 LPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAIDCVNYEGQSAYDVADMLKQYFRDLPEPLMTNKLSETF 1170
Cdd:cd04376      9 VPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAF 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1171 LQIYQYVPKDQrLQAIKAAIMLLPDENREVLQTLLYFLSDVTA-----------AVKENQMTPTNLAVCLAPSLfhlntL 1239
Cdd:cd04376     89 IGTALLEPDEQ-LEALQLLIYLLPPCNCDTLHRLLKFLHTVAEhaadsidedgqEVSGNKMTSLNLATIFGPNL-----L 162

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034180038 1240 KRENSSPRVMqRKQSLGkpdqkdLNENLAATQGLAHMIAECKKLFQVPEEM 1290
Cdd:cd04376    163 HKQKSGEREF-VQASLR------IEESTAIINVVQTMIDNYEELFMVSPEL 206
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1075-1287 7.67e-31

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: 121.68  E-value: 7.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1075 VFGVPLTVNVQRTGQPLPQS-----IQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAI--DCVNYEGQSAYDVA 1147
Cdd:cd04391      1 LFGVPLSTLLERDQKKVPGSkvpliFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKFyeGTFLWDQVKQHDAA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1148 DMLKQYFRDLPEPLMTNKLSETFLQIyQYVP-KDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLA 1226
Cdd:cd04391     81 SLLKLFIRELPQPLLTVEYLPAFYSV-QGLPsKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVA 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034180038 1227 VCLAPSLFhlntlkrensSPRVMQRKQSLGkpDQKDLNENLAATQGLAHMIAECKKLFQVP 1287
Cdd:cd04391    160 MIMAPNLF----------PPRGKHSKDNES--LQEEVNMAAGCANIMRLLIRYQDLLWTVP 208
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1076-1233 2.71e-30

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: 119.36  E-value: 2.71e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTVNVQRTG--QPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQM-NEGaiDCVNYegQSAYDV---ADM 1149
Cdd:cd04404      6 FGVSLQFLKEKNPeqEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKyNMG--EPVDF--DQYEDVhlpAVI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1150 LKQYFRDLPEPLMTNKLSETFLQIyQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCL 1229
Cdd:cd04404     82 LKTFLRELPEPLLTFDLYDDIVGF-LNVDKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVF 160


                   ....
gi 1034180038 1230 APSL 1233
Cdd:cd04404    161 GPNL 164
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1073-1233 1.97e-29

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: 117.17  E-value: 1.97e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1073 RSVFGVPLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRqmneGAIDC------VNYEGQSAYDV 1146
Cdd:cd04386      2 KPVFGTPLEEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLK----AALDAgtfslpLDEFYSDPHAV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1147 ADMLKQYFRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLA 1226
Cdd:cd04386     78 ASALKSYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIA 157


                   ....*..
gi 1034180038 1227 VCLAPSL 1233
Cdd:cd04386    158 IVLAPNL 164
START cd00177
Lipid-binding START domain of mammalian STARD1-STARD15 and related proteins; This family ...
 1333-1500 2.69e-29

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: 116.28  E-value: 2.69e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1333 FKEVKEKFKGWVSYSTSEQAELsYKKVSEGPPLRLWRSIIEVPAVPEEILKRL--LKEQHLWDVDLLDSKVIEILDSQTE 1410
Cdd:cd00177      7 LLELLEEPEGWKLVKEKDGVKI-YTKPYEDSGLKLLKAEGVIPASPEQVFELLmdIDLRKKWDKNFEEFEVIEEIDEHTD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1411 IYQYVQNSMAPHPARDYVVLRTWRtNLPKGACALLLTSVDHDRAPVVG--VRVNVLLSRYLIEPCGPGKSKLTYMCRVDL 1488
Cdd:cd00177     86 IIYYKTKPPWPVSPRDFVYLRRRR-KLDDGTYVIVSKSVDHDSHPKEKgyVRAEIKLSGWIIEPLDPGKTKVTYVLQVDP 164

                          170
                   ....*....|..
gi 1034180038 1489 RGHMPEWYTKSF 1500
Cdd:cd00177    165 KGSIPKSLVNSA 176
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1075-1254 5.15e-29

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: 115.65  E-value: 5.15e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1075 VFGVPLTV----NVQRTGQpLPQSIQQAMRYLRNHcLDQVGLFRKSGVKSRIQALRQMNEGAIDCVnyegqSAY---DVA 1147
Cdd:cd04394      1 VFGVPLHSlphsTVPEYGN-VPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEACL-----SSAlpcDVA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1148 DMLKQYFRDLPEPLMTNKLSETFLQIyQYVPKDQ-RLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLA 1226
Cdd:cd04394     74 GLLKQFFRELPEPLLPYDLHEALLKA-QELPTDEeRKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLA 152

                          170       180
                   ....*....|....*....|....*....
gi 1034180038 1227 VCLAPSLFHLNTLKRENSSPRVMQ-RKQS 1254
Cdd:cd04394    153 VIFAPNLFQSEEGGEKMSSSTEKRlRLQA 181
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1075-1250 1.29e-27

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: 111.40  E-value: 1.29e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1075 VFGVPLTvNVQRTGQP---LPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAIDCVNYEGQSAYDVADMLK 1151
Cdd:cd04393      2 VFGVPLQ-ELQQAGQPengVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1152 QYFRDLPEPLMTNKLSETFLQIYQ-YVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLA 1230
Cdd:cd04393     81 LFLQELPEGLIPASLQIRLMQLYQdYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAVFG 160

                          170       180
                   ....*....|....*....|....
gi 1034180038 1231 PSLFHLNT----LKRENSSPRVMQ 1250
Cdd:cd04393    161 PDVFHVYTdvedMKEQEICSRIMA 184
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1076-1252 2.35e-27

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: 110.61  E-value: 2.35e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLtVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAIDCVNYEGQSAYDVADMLKQYFR 1155
Cdd:cd04377      1 FGVSL-SSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1156 DLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSLfh 1235
Cdd:cd04377     80 ELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCI-- 157

                          170
                   ....*....|....*..
gi 1034180038 1236 lntLKRENSSPRVMQRK 1252
Cdd:cd04377    158 ---LRCPDTADPLQSLQ 171
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 1079-1235 2.29e-24

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: 101.62  E-value: 2.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1079 PLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALrqMNEGAIDCVNYE----GQSAYDVADMLKQYF 1154
Cdd:cd04385      3 PALEDQQLTDNDIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKL--LEAFRKDARSVQlregEYTVHDVADVLKRFL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1155 RDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSLF 1234
Cdd:cd04385     81 RDLPDPLLTSELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLF 160


                   .
gi 1034180038 1235 H 1235
Cdd:cd04385    161 Q 161
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1076-1238 3.87e-24

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: 101.33  E-value: 3.87e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQM---NEGAIDCVNYEGQSA--YDVADML 1150
Cdd:cd04398      1 FGVPLEDLILREGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELfdkDPLNVLLISPEDYESdiHSVASLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1151 KQYFRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLA 1230
Cdd:cd04398     81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160


                   ....*...
gi 1034180038 1231 PSLFHLNT 1238
Cdd:cd04398    161 PTLMNAAP 168
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1076-1234 4.39e-23

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: 98.14  E-value: 4.39e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTvNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAIDCVNYEGQSAYDVADMLKQYFR 1155
Cdd:cd04407      1 FGVRVG-SLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLR 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034180038 1156 DLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSLF 1234
Cdd:cd04407     80 ELPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLL 158
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1076-1246 5.85e-22

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: 95.06  E-value: 5.85e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTVNVQRTGqpLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALR-QMNEGAIdcVNYEGQSAYDVADMLKQYF 1154
Cdd:cd04402      2 FGQPLSNICEDDN--LPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKeKLNSGVE--VDLKAEPVLLLASVLKDFL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1155 RDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSLF 1234
Cdd:cd04402     78 RNIPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLL 157

                          170
                   ....*....|..
gi 1034180038 1235 HLNTLKRENSSP 1246
Cdd:cd04402    158 WPPASSELQNED 169
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1074-1234 8.53e-22

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: 94.88  E-value: 8.53e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1074 SVFGVPLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQvGLFRKSGVKSRIQALRQ-MNEGAI-DCVNYEG-QSAYDVADML 1150
Cdd:cd04384      1 RVFGCDLTEHLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHeFDSEQIpDLTKDVYiQDIHSVSSLC 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1151 KQYFRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLA 1230
Cdd:cd04384     80 KLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWA 159


                   ....
gi 1034180038 1231 PSLF 1234
Cdd:cd04384    160 PNLL 163
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 1095-1233 5.33e-21

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: 92.84  E-value: 5.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1095 IQQAMRYLRNHCLDQVGLFRKSGVKSRIQAL-------RQMNEGAIDCVNYEGQSAyDVADMLKQYFRDLPEPLMTNKLS 1167
Cdd:cd04374     32 VRKCIEAVETRGINEQGLYRVVGVNSKVQKLlslgldpKTSTPGDVDLDNSEWEIK-TITSALKTYLRNLPEPLMTYELH 110

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034180038 1168 ETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSL 1233
Cdd:cd04374    111 NDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTL 176
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1076-1233 5.85e-21

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: 92.11  E-value: 5.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTVNVQRT----GQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQM--NEGaidCVNYEGQSAYDVADM 1149
Cdd:cd04381      1 FGASLSLAVERSrchdGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAynRRE---SPNLEEYEPPTVASL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1150 LKQYFRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCL 1229
Cdd:cd04381     78 LKQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVL 157


                   ....
gi 1034180038 1230 APSL 1233
Cdd:cd04381    158 SPTV 161
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1076-1248 1.18e-20

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: 91.30  E-value: 1.18e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALR-QMN-EGAIDCVNYEGQSAYDVADMLKQY 1153
Cdd:cd04403      1 FGCHLEALCQRENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRfAVDhDEKLDLDDSKWEDIHVITGALKLF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1154 FRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSL 1233
Cdd:cd04403     81 FRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPTL 160

                          170
                   ....*....|....*
gi 1034180038 1234 FHlntLKRENSSPRV 1248
Cdd:cd04403    161 LR---PEQETGNIAV 172
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1076-1234 1.20e-20

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: 90.98  E-value: 1.20e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLtVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQAL-RQMNE-GAIDCVNYEgQSAYDVADMLKQY 1153
Cdd:cd04373      1 FGVPL-ANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLqKQFDQdHNLDLVSKD-FTVNAVAGALKSF 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1154 FRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSL 1233
Cdd:cd04373     79 FSELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTL 158


                   .
gi 1034180038 1234 F 1234
Cdd:cd04373    159 M 159
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1076-1233 1.30e-20

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: 91.72  E-value: 1.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAIDCVNYEGQSAYDVADMLKQYFR 1155
Cdd:cd04378      1 FGVDFSQVPRDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1156 DLPEPLMTNKLSETFLQI---YQYVPKDQR-----------LQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMT 1221
Cdd:cd04378     81 QLPEPLILFRLYNDFIALakeIQRDTEEDKapntpievnriIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMS 160

                          170
                   ....*....|..
gi 1034180038 1222 PTNLAVCLAPSL 1233
Cdd:cd04378    161 PNNLGIVFGPTL 172
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1074-1235 5.55e-20

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: 89.40  E-value: 5.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1074 SVFGVPLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAIDCVNYEgQSAYD---VADML 1150
Cdd:cd04383      1 KLFNGSLEEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADD-QNDHDinsVAGVL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1151 KQYFRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLA 1230
Cdd:cd04383     80 KLYFRGLENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFG 159


                   ....*
gi 1034180038 1231 PSLFH 1235
Cdd:cd04383    160 PTLMP 164
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1076-1293 4.48e-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: 87.13  E-value: 4.48e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTvnvqrtgQPLPQSIQQAMRYLRNHcLDQVGLFRKSGVKSRIQALR-QMNEGAIDCVNYEGQSAYDVADMLKQYF 1154
Cdd:cd04392      1 FGAPLT-------EEGIAQIYQLIEYLEKN-LRVEGLFRKPGNSARQQELRdLLNSGTDLDLESGGFHAHDCATVLKGFL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1155 RDLPEPLMTNKLSETFLQI---YQY---------VPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTP 1222
Cdd:cd04392     73 GELPEPLLTHAHYPAHLQIadlCQFdekgnktsaPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSA 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034180038 1223 TNLAVCLAPSLfhlntlkrenssprVMQRKQSlgkpdQKDLNENLAA-TQGLAHMIAECKKLFQVPEEMSRC 1293
Cdd:cd04392    153 DNLALLFTPHL--------------ICPRNLT-----PEDLHENAQKlNSIVTFMIKHSQKLFKAPAYLRED 205
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1076-1233 1.69e-18

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: 85.26  E-value: 1.69e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQmnegAIDcvnYEG------QSAYD---- 1145
Cdd:cd04372      1 YGCDLTTLVKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKM----AFD---RDGekadisATVYPdinv 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1146 VADMLKQYFRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNL 1225
Cdd:cd04372     74 ITGALKLYFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENL 153


                   ....*...
gi 1034180038 1226 AVCLAPSL 1233
Cdd:cd04372    154 GIVFGPTL 161
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 1076-1247 1.85e-17

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: 82.51  E-value: 1.85e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTVNVQRTGQPL--PQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNE--GAIDCVNYEGQSAYDV-ADML 1150
Cdd:cd04379      1 FGVPLSRLVEREGESRdvPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFErnSAAVELSEELYPDINViTGVL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1151 KQYFRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIML---LPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAV 1227
Cdd:cd04379     81 KDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHLTLSIidcLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160

                          170       180
                   ....*....|....*....|.
gi 1034180038 1228 CLAPSLF-HLNTLKRENSSPR 1247
Cdd:cd04379    161 CFGPVLMfCSQEFSRYGISPT 181
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1076-1234 1.18e-16

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: 79.66  E-value: 1.18e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTvNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAIDCVNYEGQSAYDVADMLKQYFR 1155
Cdd:cd04406      1 FGVELS-RLTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLR 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034180038 1156 DLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSLF 1234
Cdd:cd04406     80 DLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCIL 158
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 1076-1233 2.34e-16

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: 79.09  E-value: 2.34e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAIDCVNYEGQSAYDVADMLKQYFR 1155
Cdd:cd04408      1 FGVDFSQLPRDFPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1156 DLPEPLMTNKLSETFLQI---YQYVPKDQR---------LQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPT 1223
Cdd:cd04408     81 ELPEPVLPFQLYDDFIALakeLQRDSEKAAespsiveniIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPN 160

                          170
                   ....*....|
gi 1034180038 1224 NLAVCLAPSL 1233
Cdd:cd04408    161 NLGIVFGPTL 170
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1076-1246 3.41e-16

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: 78.95  E-value: 3.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTVNVQRTGQP-----------LPQSIQQAMRYLRNHCLDQVGLFRKSGvksRIQALRQMNEgAID-----CVNYE 1139
Cdd:cd04397      1 FGVPLEILVEKFGADstlgvgpgklrIPALIDDIISAMRQMDMSVEGVFRKNG---NIRRLKELTE-EIDknpteVPDLS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1140 GQSAYDVADMLKQYFRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVT--AAVKE 1217
Cdd:cd04397     77 KENPVQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSsfSHIDE 156

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1034180038 1218 ---NQMTPTNLAVCLAPslfhlNTLKRENSSP 1246
Cdd:cd04397    157 etgSKMDIHNLATVITP-----NILYSKTDNP 183
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1075-1234 4.29e-16

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: 78.99  E-value: 4.29e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1075 VFGVPL-----TVNVQ-----RTGQPL-----PQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAID---CV 1136
Cdd:cd04396      1 VFGVSLeeslkYASVAisivdEDGEQYvygyiPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPDygkSF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1137 NYEGQSAYDVADMLKQYFRDLPEPLMTNKLSETFLQ-------IYQYVP----------KDQRLQAIKAAIMLLPDENRE 1199
Cdd:cd04396     81 DWDGYTVHDAASVLRRYLNNLPEPLVPLDLYEEFRNplrkrprILQYMKgrineplntdIDQAIKEYRDLITRLPNLNRQ 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1034180038 1200 VLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSLF 1234
Cdd:cd04396    161 LLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGIL 195
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1076-1233 3.97e-15

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: 76.00  E-value: 3.97e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQMNEGAIDCVNYEGQSAYDVADMLKQYFR 1155
Cdd:cd04409      1 FGADFAQVAKKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1156 DLPEPLMTNKLSETFLQI---YQYVPKDQR-------------------LQAIKAAIMLLPDENREVLQTLLYFLSDVTA 1213
Cdd:cd04409     81 QLPEPLILFRLYNEFIGLakeSQHVNETQEakknsdkkwpnmctelnriLLKSKDLLRQLPAPNYNTLQFLIVHLHRVSE 160

                          170       180
                   ....*....|....*....|
gi 1034180038 1214 AVKENQMTPTNLAVCLAPSL 1233
Cdd:cd04409    161 QAEENKMSASNLGIIFGPTL 180
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1075-1255 5.55e-15

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: 75.17  E-value: 5.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1075 VFGVPLTVNV---QRTGQPL-PQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRQmnegAIDC---VNYEGQS-AYDV 1146
Cdd:cd04390      2 VFGQRLEDTVayeRKFGPRLvPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQD----AFDAgerPSFDSDTdVHTV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1147 ADMLKQYFRDLPEPLMTNKLSETFLQIYQYVPKDQR--LQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTN 1224
Cdd:cd04390     78 ASLLKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEkgLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQN 157

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1034180038 1225 LAVCLAPslfhlNTLKRENSSPRVMQRKQSL 1255
Cdd:cd04390    158 LATVFGP-----NILRPKVEDPATIMEGTPQ 183
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1075-1233 5.84e-15

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: 75.13  E-value: 5.84e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1075 VFGVPL-TVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALR-QMNEG--AIDCVNYEGQSAYDVADML 1150
Cdd:cd04395      1 TFGVPLdDCPPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQeELNRGgfDIDLQDPRWRDVNVVSSLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1151 KQYFRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLA 1230
Cdd:cd04395     81 KSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFG 160


                   ...
gi 1034180038 1231 PSL 1233
Cdd:cd04395    161 PTL 163
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 1076-1233 6.17e-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: 72.27  E-value: 6.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1076 FGVPLTVNVQRTGQPLPQSIQQAMRYLRNHCLDQVGLFRKSGVKSRIQALRqmneGAIDCVNYEGQ---SAYDV---ADM 1149
Cdd:cd04387      1 FGVKISTVTKRERSKVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALK----AAFDTNNKDVSvmlSEMDVnaiAGT 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1150 LKQYFRDLPEPLMTNKLSETFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCL 1229
Cdd:cd04387     77 LKLYFRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVF 156


                   ....
gi 1034180038 1230 APSL 1233
Cdd:cd04387    157 GPTL 160
START_STARD10-like cd08871
Lipid-binding START domain of mammalian STARD10 and related proteins; This subfamily includes ...
 1330-1495 2.50e-13

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: 70.75  E-value: 2.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1330 DGLFKEVKEKFK---GW-VSYSTSEQAELSykKVSEGPPLRLWRSIIEVPAVPEEILKRLLkeqH------LWDVDLLDS 1399
Cdd:cd08871      9 DADFEEFKKLCDstdGWkLKYNKNNVKVWT--KNPENSSIKMIKVSAIFPDVPAETLYDVL---HdpeyrkTWDSNMIES 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1400 KVIEILDSQTEIYQYVQNSMAPHPARDYVVLRTWrtnLPKGACALLL-TSVDHDRAPVVG--VRVNVLLSRYLIEPCGPG 1476
Cdd:cd08871     84 FDICQLNPNNDIGYYSAKCPKPLKNRDFVNLRSW---LEFGGEYIIFnHSVKHKKYPPRKgfVRAISLLTGYLIRPTGPK 160

                          170
                   ....*....|....*....
gi 1034180038 1477 KSKLTYMCRVDLRGHMPEW 1495
Cdd:cd08871    161 GCTLTYVTQNDPKGSLPKW 179
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 1075-1233 3.77e-13

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: 69.69  E-value: 3.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1075 VFGVPLTVNVQRT-----GQPLPQSIQQAMRYL-RNHCLDQVGLFRKSGVKSRIQALR-QMN-EGAIDCVNYEGQsaYD- 1145
Cdd:cd04400      1 IFGSPLEEAVELSshkynGRDLPSVVYRCIEYLdKNRAIYEEGIFRLSGSASVIKQLKeRFNtEYDVDLFSSSLY--PDv 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1146 --VADMLKQYFRDLPEPLMTNKLSETFLQIYQYVPKD-QRLQAIKAAIMLLPDENREVLQTLLYFLSDVTAAVKENQMTP 1222
Cdd:cd04400     79 htVAGLLKLYLRELPTLILGGELHNDFKRLVEENHDRsQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNL 158

                          170
                   ....*....|.
gi 1034180038 1223 TNLAVCLAPSL 1233
Cdd:cd04400    159 RNVCIVFSPTL 169
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1105-1251 1.07e-12

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: 68.47  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1105 HC--------LDQVGLFRKSGVKSRIQALRQM--------NEGAIDcvnyegqsAYDVADMLKQYFRDLPEPLMTNKLSE 1168
Cdd:cd04382     23 HCvneieargLTEEGLYRVSGSEREVKALKEKflrgktvpNLSKVD--------IHVICGCLKDFLRSLKEPLITFALWK 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1169 TFLQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFLSDVtAAVKENQMTPTNLAVCLAPSLF--------HLNTLK 1240
Cdd:cd04382     95 EFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRV-AQSPECKMDINNLARVFGPTIVgysvpnpdPMTILQ 173

                          170
                   ....*....|.
gi 1034180038 1241 RENSSPRVMQR 1251
Cdd:cd04382    174 DTVRQPRVVER 184
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1111-1249 7.92e-12

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: 65.88  E-value: 7.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1111 GLFRKSGVKSRIQALR-QMNEGAIDCVNYEgqSAYDVADMLKQYFRDLPEPLMTNKLSETFLQIYqyvpkDQRLQAIkAA 1189
Cdd:cd04389     42 GIFRVPGDIDEVNELKlRVDQWDYPLSGLE--DPHVPASLLKLWLRELEEPLIPDALYQQCISAS-----EDPDKAV-EI 113

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034180038 1190 IMLLPDENREVLQTLLYFLSDVT--AAVKENQMTPTNLAVCLAPslfhlNTLKRENSSPRVM 1249
Cdd:cd04389    114 VQKLPIINRLVLCYLINFLQVFAqpENVAHTKMDVSNLAMVFAP-----NILRCTSDDPRVI 170
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
452-513 1.41e-09

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 55.35  E-value: 1.41e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034180038  452 EAKEACDWLRATGFPQYAQLYEDFLFPIDISLVKREHDFLDRDAIEALCRRLNTLNKCAVMK 513
Cdd:pfam07647    5 SLESVADWLRSIGLEQYTDNFRDQGITGAELLLRLTLEDLKRLGITSVGHRRKILKKIQELK 66
START_1 cd08876
Uncharacterized subgroup of the steroidogenic acute regulatory protein (StAR)-related lipid ...
 1342-1495 4.09e-09

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: 58.05  E-value: 4.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1342 GWVSYSTSEQAELSYKKVsEGPPLRLWRSIIEVPAVPEEILKRLLKEQH--LWDVDLLDSKVIEILDSQtEIYQYVQNSM 1419
Cdd:cd08876     18 DWQLVKDKDGIKVYTRDV-EGSPLKEFKAVAEVDASIEAFLALLRDTESypQWMPNCKESRVLKRTDDN-ERSVYTVIDL 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034180038 1420 aPHPA--RDYVVLRTWRTNLPKGACALLLTSVDHDRAPVVG-VRVNVLLSRYLIEPCGPGKSKLTYMCRVDLRGHMPEW 1495
Cdd:cd08876     96 -PWPVkdRDMVLRSTTEQDADDGSVTITLEAAPEALPEQKGyVRIKTVEGQWTFTPLGNGKTRVTYQAYADPGGSIPGW 173
RhoGAP_BRCC3-like cd04405
RhoGAP_BRCC3-like: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1075-1222 5.35e-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: 52.33  E-value: 5.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1075 VFGVPLTVNVQRTGQPLPQSIQQAMR--YLRNHCLDQ--VGLFRKSGVKSRIQAlrqmnegAIDC--------VNYEGQS 1142
Cdd:cd04405     21 LVGLPLLEELLDPALVNPKHISYNMDpdVYTSNYLDRevVKLFSKSQLDHWLLS-------AMDClanwpdqlVVDVSRP 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1143 AYDVADMLK-----------QYFRDLPEPLMTNKLSETF---LQIYQYVPKDQRLQAIKAAIMLLPDENREVLQTLLYFL 1208
Cdd:cd04405     94 LYSQHDMLSgfkrllfktiaKYYGQLKEPLLTFHLFDIFvgiLELLGNGKEEVALEALQLCLLLLPPASRRELRRLLRFM 173

                          170
                   ....*....|....
gi 1034180038 1209 sdvtAAVKENQMTP 1222
Cdd:cd04405    174 ----ARAAKNDMPR 183
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1101-1255 1.05e-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: 51.19  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1101 YLRNHCLDQVGLFRKSGVKSriQALRQMNEgAIDCVNYEGQ-----SAYDVADMLKQYFRDLPEPLMTNKLSETFLQiYQ 1175
Cdd:cd04380     60 YLYTRGLAQEGLFEEPGLPS--EPGELLAE-IRDALDTGSPfnspgSAESVAEALLLFLESLPDPIIPYSLYERLLE-AV 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1176 YVPKDQRLQAIKAAimlLPDENREVLQTLLYFLSDVTAAVKENQMTPTNLAVCLAPSLFHLNTLKRENSSPRVMQRKQSL 1255
Cdd:cd04380    136 ANNEEDKRQVIRIS---LPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRAGGKERRAERDRKRAF 212
START_STARD4_5_6-like cd08867
Lipid-binding START domain of mammalian STARD4, -5, -6, and related proteins; This subfamily ...
 1342-1494 1.14e-06

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: 50.92  E-value: 1.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1342 GWVSYSTSEQAELSYKKVSEGPPlRLWRSIIEVPAVPEEILKRLL----KEQHLWDVDLLDSKVIEILDSQTEIYQYVQN 1417
Cdd:cd08867     23 GWKVLKTVKNITVSWKPSTEFTG-HLYRAEGIVDALPEKVIDVIIppcgGLRLKWDKSLKHYEVLEKISEDLCVGRTITP 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1418 S--MAPHPARDYVVLRTWRTnLPKGACALLLTSVDH-DRAPVVG-VR-VNvllsryliEPCG---------PGKSKLTYM 1483
Cdd:cd08867    102 SaaMGLISPRDFVDLVYVKR-YEDNQWSSSGKSVDIpERPPTPGfVRgYN--------HPCGyfcsplkgsPDKSFLVLY 172

                          170
                   ....*....|.
gi 1034180038 1484 CRVDLRGHMPE 1494
Cdd:cd08867    173 VQTDLRGMIPQ 183
SAM smart00454
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ...
 454-513 5.28e-06

Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation.


Pssm-ID: 197735  Cd Length: 68  Bit Score: 45.36  E-value: 5.28e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038   454 KEACDWLRATGFPQYAQLYEDFLFPIDISLVKREHDFLDRDAIEALCRRLNTLNKCAVMK 513
Cdd:smart00454    7 ESVADWLESIGLEQYADNFRKNGIDGALLLLLTSEEDLKELGITKLGHRKKILKAIQKLK 66
START_STARD1_3_like cd08868
Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily ...
 1341-1493 3.88e-03

Cholesterol-binding START domain of mammalian STARD1, -3 and related proteins; This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of STARD1 (also known as StAR) and STARD3 (also known as metastatic lymph node 64/MLN64). 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. This STARD1-like subfamily has a high affinity for cholesterol. STARD1/StAR can reduce macrophage lipid content and inflammatory status. It plays an essential role in steroidogenic tissues: transferring the steroid precursor, cholesterol, from the outer to the inner mitochondrial membrane, across the aqueous space. Mutations in the gene encoding STARD1/StAR can cause lipid congenital adrenal hyperplasia (CAH), an autosomal recessive disorder characterized by a steroid synthesis deficiency and an accumulation of cholesterol in the adrenal glands and the gonads. STARD3 may function in trafficking endosomal cholesterol to a cytosolic acceptor or membrane. In addition to having a cytoplasmic START cholesterol-binding domain, STARD3 also contains an N-terminal MENTAL cholesterol-binding and protein-protein interaction domain. The MENTAL domain contains transmembrane helices and anchors MLN64 to endosome membranes. The gene encoding STARD3 is overexpressed in about 25% of breast cancers.


Pssm-ID: 176877  Cd Length: 208  Bit Score: 40.42  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1341 KGWVSYSTSEQAELSYKKVSEGPP--LRLwRSIIEVPA--VPEEILKRLlKEQHLWDVDLLDSKVIEILDSQTEI-YQYV 1415
Cdd:cd08868     24 PGWKLEKNTTWGDVVYSRNVPGVGkvFRL-TGVLDCPAefLYNELVLNV-ESLPSWNPTVLECKIIQVIDDNTDIsYQVA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034180038 1416 QNSMAPH-PARDYVVLRTWRtnLPKGACALLLTSVDHDRAPVVG--VRVNVLLSRYLIEPCG--PGKSKLTYMCRVDLRG 1490
Cdd:cd08868    102 AEAGGGLvSPRDFVSLRHWG--IRENCYLSSGVSVEHPAMPPTKnyVRGENGPGCWILRPLPnnPNKCNFTWLLNTDLKG 179


                   ...
gi 1034180038 1491 HMP 1493
Cdd:cd08868    180 WLP 182
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH