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Conserved domains on  [gi|71834861|ref|NP_001164|]
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rho GTPase-activating protein 5 isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGAP_pG1_pG2 pfam19518
p190RhoGAP, pG1 and pG2 domains; The p190RhoGAP (GTPase-activating protein) proteins, ...
 556-1263 0e+00

p190RhoGAP, pG1 and pG2 domains; The p190RhoGAP (GTPase-activating protein) proteins, p190RhoGAP-A (ARHGAP35) and p190RhoGAP-B (ARHGAP5)4-6, regulates Rho GTP hydrolysis and are important for proper Rho signalling. They share a domain organization containing a GTP-binding GTPase domain, four FF domains, two GTPase-like folds (pG1 and pG2) in the middle domain and a C-terminal GAP domain. This entry represents pG1 and pG2 which are important for GAP activity toward RhoA and were classified as pseudoGTPases as they lack nucleotide-binding activity. Crystal structures revealed a small GTPase fold in both cases with a central 6-stranded beta-sheet surrounded by four alpha-helices.


:

Pssm-ID: 466111  Cd Length: 699  Bit Score: 1100.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    556 TCLSGQNCTDIKVEQLLASSLLQLDHGRLRLYHDSTNIDKVNLFILGKDGLAQELANEIRTQST-DDEYALDGKIYELDL 634
Cdd:pfam19518    1 TCPSGPNCVDSKIEQLLASRFPQPYPRRLKSYHDDANIDRINLVILGKDGLARELANEIRALCTnDDKYVLDGKMYELSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    635 RPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLSFIGEFIGKIRTEASQiRKDKYMANLPFTLILANQR-DSISKNLPI 713
Cdd:pfam19518   81 RPIEGNVRLPVNSFQTPTFKPHGCLCLYNSKESLSYVVESIEKSRESTLG-RRDNHLAHLPLTLILVNKRgDIGGETLQS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    714 LRHQGQQLANKLQCPFVDVP--AGTYPRKFNETQIKQALRGVLESVKHNLDVVSPIPANKDLSEADLRIVMCAMCGDPFS 791
Cdd:pfam19518  160 LIQQGQQVANKLQCPFLDPAspGGGYGRNFNEKQINQVLRGLLESKRHNLNVVSPAPSIKDLSEADLRIVMCLMCGDPFS 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    792 VDLILSPFLDSHSCSAAQAGQNNSLMLDKIIGEKRRRIQITILSYHSSIGVRKDELVHGYILVYSAKRKASMGMLRAFLS 871
Cdd:pfam19518  240 VDLILSPFLQSQHCRPAQPGSGNSVLLELIIGGQRRRIELSILSYHSSFGVRKSRLVHGYILVYSAKRKASMAMLRAFLC 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    872 EVQDTIPVQLVAVTDSQADFFENEAIKELMTEGEHIATEITAKFTALYSLSQYHRQTEVFTLFFSDVLEKKNMIENSYLS 951
Cdd:pfam19518  320 EVQDIIPVQLVAVTDSQADFFESEVSREQLTEGEEIAHEIEAKFTALYCGSGYQHQTEVFTPFFKEVLEKKTIIEASHMY 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    952 DNTRESTHQsEDVFLPSPRDC--FPYNNYPDSDDDTEAPPPYSPIGDDVQLLptPSDRSRYRLDLEGNEYPIHSTPNCHD 1029
Cdd:pfam19518  400 DNTAEACST-EEEFFSSPRAGspSPNSNLPDSEDDTEPPPPYSPIRDDVQLL--PSDRSKFSLDLEGNDYSVISTPSSFE 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   1030 HERNHkVPPPIKPKPVVPKTNVKKLDPNLLktIEAGIGKNPRKQTSRVPLAHPEDMDPSDnYAEPIDTIFKQKGYSDEIY 1109
Cdd:pfam19518  477 SKLNN-KVPPPVKPKPPVKFDVRKLDPNLY--IDGGNRDGPRSLPSRVTWAPGEGYDPSD-YAEPMDAVVKPRGEEENIY 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   1110 VVPDDS-QNRI-KIRNSFVNNTQGdEENGFSDRTSKSHGERR--------PSKYKYKSKTLfSKAKSyYRRTHSDASDDE 1179
Cdd:pfam19518  553 SVPHDStQGKIiTIRNSNKTQSNG-EGNGSDSEADSSSLERRkksalgvkPRLYRDRSKRL-GKFSS-YRTSFSVGSDDE 629

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   1180 AFTTSKTKRKGRHRGSEEDPLLSPVEtwkGGIDNPAITSDQElddkkmkkkthKVKEDKKKKKTKNFNPPTRRNWESNYF 1259
Cdd:pfam19518  630 LGPIRKKKREDDHGGSKGDNLLNPYE---GGIEDPKRRNILR-----------SLRRTTKKPKPKPRPSISKPTWESNYF 695


                   ....
gi 71834861   1260 GMPL 1263
Cdd:pfam19518  696 GVPL 699
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1443 7.63e-113

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: 353.30  E-value: 7.63e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFA 1338
Cdd:cd04373    1 FGVPLANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDFTVNAVAGALKSFFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1339 DLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMR 1418
Cdd:cd04373   81 ELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR 160

                        170       180
                 ....*....|....*....|....*
gi 71834861 1419 PDFENREFLSTTKIHQSVVETFIQQ 1443
Cdd:cd04373  161 PDFTSMEALSATRIYQTIIETFIQQ 185
RhoGAP-FF1 pfam16512
p190-A and -B Rho GAPs FF domain; RhoGAP-FF1 is the FF domain of the Rho GTPase activating ...
 260-338 3.42e-36

p190-A and -B Rho GAPs FF domain; RhoGAP-FF1 is the FF domain of the Rho GTPase activating proteins (GAPs). These are the key proteins that make the switch between the active guanosine-triphosphate-bound form of Rho guanosine triphosphatases (GTPases) and the inactive guanosine-diphosphate-bound form. Rho guanosine triphosphatases (GTPases) are a family of proteins with key roles in the regulation of actin cytoskeleton dynamics. The RhoGAP-FF1 region contains the FF domain that has been implicated in binding to the transcription factor TFII-I; and phosphorylation of Tyr308 within the first FF domain inhibits this interaction. The RhoGAPFF1 domain constitutes the first solved structure of an FF domain that lacks the first of the two highly conserved Phe residues, but the substitution of Phe by Tyr does not affect the domain fold.


:

Pssm-ID: 465153  Cd Length: 80  Bit Score: 131.56  E-value: 3.42e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    260 DAYKTQRQLVVTATDKFEKLV-QTVRDYHATWKTVSNKLKNHPDYEEYINLEGTRKARNTFSKHIEQLKQEHIRKRREEY 338
Cdd:pfam16512    1 EAAKVRKELLDSATDAFERLIrSQVTDYRALWKTVSKKLSQHPEYQEYVELFGTDKAKRLFRKHIKKLKDEHIRKRRQGY 80
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 429-481 4.42e-09

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


:

Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 53.73  E-value: 4.42e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 71834861     429 EMKEKFKKTLEKIQFISPGQPWEEVMCFVMEDEAYKYITEADSKEVYGRHQRE 481
Cdd:smart00441    2 EAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 31-246 1.56e-08

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd00876:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 160  Bit Score: 55.22  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   31 GVGKSCLCNRFVRSKADEYY---PEHTSVlSTIDFggrvvnndhflywgdiiqnseDGVECKIHVI---EQTEFiddqtf 104
Cdd:cd00876    9 GVGKSALTIRFVSGEFVEEYdptIEDSYR-KQIVV---------------------DGETYTLDILdtaGQEEF------ 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  105 lphrSTNLQPYIKraaasklqsaeklmyictdqlgleqdfeqkqmpegklNVDGFLLCIDVsqgCNRK-FDDQLKFVNNL 183
Cdd:cd00876   61 ----SAMRDQYIR-------------------------------------NGDGFILVYSI---TSREsFEEIKNIREQI 96

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71834861  184 FVQLSKSKKPVIIAATKCDEcvDHYlREV-----QAFAsNKKNLLVVETSARFNVNIETCFTALVQML 246
Cdd:cd00876   97 LRVKDKEDVPIVLVGNKCDL--ENE-RQVsteegEALA-EEWGCPFLETSAKTNINIDELFNTLVREI 160
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 484-533 2.26e-05

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


:

Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 43.33  E-value: 2.26e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 71834861     484 EKAKEEFQEMLFEHSELFYDLDLNATPSSDKMSEIH-TVLSEEPRYKALQK 533
Cdd:smart00441    1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYkALLSESEREQLFED 51
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 368-420 6.39e-04

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


:

Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 39.09  E-value: 6.39e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 71834861     368 MEKRADFQLCFVVLEK----TPWDETDHIDKINDRRIpfDLLSTLEAEKVYQNHVQH 420
Cdd:smart00441    1 EEAKEAFKELLKEHEVitpdTTWSEARKKLKNDPRYK--ALLSESEREQLFEDHIEE 55
 
Name Accession Description Interval E-value
RhoGAP_pG1_pG2 pfam19518
p190RhoGAP, pG1 and pG2 domains; The p190RhoGAP (GTPase-activating protein) proteins, ...
 556-1263 0e+00

p190RhoGAP, pG1 and pG2 domains; The p190RhoGAP (GTPase-activating protein) proteins, p190RhoGAP-A (ARHGAP35) and p190RhoGAP-B (ARHGAP5)4-6, regulates Rho GTP hydrolysis and are important for proper Rho signalling. They share a domain organization containing a GTP-binding GTPase domain, four FF domains, two GTPase-like folds (pG1 and pG2) in the middle domain and a C-terminal GAP domain. This entry represents pG1 and pG2 which are important for GAP activity toward RhoA and were classified as pseudoGTPases as they lack nucleotide-binding activity. Crystal structures revealed a small GTPase fold in both cases with a central 6-stranded beta-sheet surrounded by four alpha-helices.


Pssm-ID: 466111  Cd Length: 699  Bit Score: 1100.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    556 TCLSGQNCTDIKVEQLLASSLLQLDHGRLRLYHDSTNIDKVNLFILGKDGLAQELANEIRTQST-DDEYALDGKIYELDL 634
Cdd:pfam19518    1 TCPSGPNCVDSKIEQLLASRFPQPYPRRLKSYHDDANIDRINLVILGKDGLARELANEIRALCTnDDKYVLDGKMYELSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    635 RPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLSFIGEFIGKIRTEASQiRKDKYMANLPFTLILANQR-DSISKNLPI 713
Cdd:pfam19518   81 RPIEGNVRLPVNSFQTPTFKPHGCLCLYNSKESLSYVVESIEKSRESTLG-RRDNHLAHLPLTLILVNKRgDIGGETLQS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    714 LRHQGQQLANKLQCPFVDVP--AGTYPRKFNETQIKQALRGVLESVKHNLDVVSPIPANKDLSEADLRIVMCAMCGDPFS 791
Cdd:pfam19518  160 LIQQGQQVANKLQCPFLDPAspGGGYGRNFNEKQINQVLRGLLESKRHNLNVVSPAPSIKDLSEADLRIVMCLMCGDPFS 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    792 VDLILSPFLDSHSCSAAQAGQNNSLMLDKIIGEKRRRIQITILSYHSSIGVRKDELVHGYILVYSAKRKASMGMLRAFLS 871
Cdd:pfam19518  240 VDLILSPFLQSQHCRPAQPGSGNSVLLELIIGGQRRRIELSILSYHSSFGVRKSRLVHGYILVYSAKRKASMAMLRAFLC 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    872 EVQDTIPVQLVAVTDSQADFFENEAIKELMTEGEHIATEITAKFTALYSLSQYHRQTEVFTLFFSDVLEKKNMIENSYLS 951
Cdd:pfam19518  320 EVQDIIPVQLVAVTDSQADFFESEVSREQLTEGEEIAHEIEAKFTALYCGSGYQHQTEVFTPFFKEVLEKKTIIEASHMY 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    952 DNTRESTHQsEDVFLPSPRDC--FPYNNYPDSDDDTEAPPPYSPIGDDVQLLptPSDRSRYRLDLEGNEYPIHSTPNCHD 1029
Cdd:pfam19518  400 DNTAEACST-EEEFFSSPRAGspSPNSNLPDSEDDTEPPPPYSPIRDDVQLL--PSDRSKFSLDLEGNDYSVISTPSSFE 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   1030 HERNHkVPPPIKPKPVVPKTNVKKLDPNLLktIEAGIGKNPRKQTSRVPLAHPEDMDPSDnYAEPIDTIFKQKGYSDEIY 1109
Cdd:pfam19518  477 SKLNN-KVPPPVKPKPPVKFDVRKLDPNLY--IDGGNRDGPRSLPSRVTWAPGEGYDPSD-YAEPMDAVVKPRGEEENIY 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   1110 VVPDDS-QNRI-KIRNSFVNNTQGdEENGFSDRTSKSHGERR--------PSKYKYKSKTLfSKAKSyYRRTHSDASDDE 1179
Cdd:pfam19518  553 SVPHDStQGKIiTIRNSNKTQSNG-EGNGSDSEADSSSLERRkksalgvkPRLYRDRSKRL-GKFSS-YRTSFSVGSDDE 629

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   1180 AFTTSKTKRKGRHRGSEEDPLLSPVEtwkGGIDNPAITSDQElddkkmkkkthKVKEDKKKKKTKNFNPPTRRNWESNYF 1259
Cdd:pfam19518  630 LGPIRKKKREDDHGGSKGDNLLNPYE---GGIEDPKRRNILR-----------SLRRTTKKPKPKPRPSISKPTWESNYF 695


                   ....
gi 71834861   1260 GMPL 1263
Cdd:pfam19518  696 GVPL 699
pseudoGTPaseD_p190RhoGAP-B cd22220
pseudoGTPase domain found in p190RhoGAP-B and similar proteins; p190RhoGAP protein B ...
 592-762 1.48e-120

pseudoGTPase domain found in p190RhoGAP-B and similar proteins; p190RhoGAP protein B (p190RhoGAP-B), also called ARHGAP5, or p190-B, or Rho-type GTPase-activating protein 5 (RHOGAP5), is a Rho family GTPase-activating protein (GAP) that acts as a key regulator of Rho GTPase signaling and is essential for actin cytoskeletal structure and contractility. This model corresponds to the GTPase-like domain called pseudoGTPase domain that is located at the middle region of p190RhoGAP-B. Rho family GTPase-activating proteins normally have five highly conserved sequence motifs, termed 'G-motifs', required for nucleotide-binding and catalytic activity. PseudoGTPases consist of a GTPase fold lacking one or more of these G motifs.


Pssm-ID: 412065  Cd Length: 171  Bit Score: 373.80  E-value: 1.48e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  592 NIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLSFI 671
Cdd:cd22220    1 NIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDANSPYLLSQLWTSAFKPHGCFCVFNSIESLNFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  672 GEFIGKIRTEASQIRKDKYMANLPFTLILANQRDSISKNLPILRHQGQQLANKLQCPFVDVPAGTYPRKFNETQIKQALR 751
Cdd:cd22220   81 GECIGKIRAEASQIRRDRYIANLPFTLILANQRDSVSKNLPILRHQGQQLANKLQCPFVDVPAGTYPRKFNETQIKQALR 160

                        170
                 ....*....|.
gi 71834861  752 GVLESVKHNLD 762
Cdd:cd22220  161 GVLESVKHNLD 171
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1443 7.63e-113

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: 353.30  E-value: 7.63e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFA 1338
Cdd:cd04373    1 FGVPLANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDFTVNAVAGALKSFFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1339 DLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMR 1418
Cdd:cd04373   81 ELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR 160

                        170       180
                 ....*....|....*....|....*
gi 71834861 1419 PDFENREFLSTTKIHQSVVETFIQQ 1443
Cdd:cd04373  161 PDFTSMEALSATRIYQTIIETFIQQ 185
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 1271-1444 5.91e-67

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: 223.30  E-value: 5.91e-67
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    1271 KPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFADLPDPLIPYSLH 1350
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    1351 PELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMRPDFENREFLSTT 1430
Cdd:smart00324   81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160

                           170
                    ....*....|....
gi 71834861    1431 KIHQSVVETFIQQC 1444
Cdd:smart00324  161 RHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 1274-1420 9.85e-60

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 201.62  E-value: 9.85e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   1274 PLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFADLPDPLIPYSLHPEL 1353
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71834861   1354 LEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMRPD 1420
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147
RhoGAP-FF1 pfam16512
p190-A and -B Rho GAPs FF domain; RhoGAP-FF1 is the FF domain of the Rho GTPase activating ...
 260-338 3.42e-36

p190-A and -B Rho GAPs FF domain; RhoGAP-FF1 is the FF domain of the Rho GTPase activating proteins (GAPs). These are the key proteins that make the switch between the active guanosine-triphosphate-bound form of Rho guanosine triphosphatases (GTPases) and the inactive guanosine-diphosphate-bound form. Rho guanosine triphosphatases (GTPases) are a family of proteins with key roles in the regulation of actin cytoskeleton dynamics. The RhoGAP-FF1 region contains the FF domain that has been implicated in binding to the transcription factor TFII-I; and phosphorylation of Tyr308 within the first FF domain inhibits this interaction. The RhoGAPFF1 domain constitutes the first solved structure of an FF domain that lacks the first of the two highly conserved Phe residues, but the substitution of Phe by Tyr does not affect the domain fold.


Pssm-ID: 465153  Cd Length: 80  Bit Score: 131.56  E-value: 3.42e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    260 DAYKTQRQLVVTATDKFEKLV-QTVRDYHATWKTVSNKLKNHPDYEEYINLEGTRKARNTFSKHIEQLKQEHIRKRREEY 338
Cdd:pfam16512    1 EAAKVRKELLDSATDAFERLIrSQVTDYRALWKTVSKKLSQHPEYQEYVELFGTDKAKRLFRKHIKKLKDEHIRKRRQGY 80
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 429-481 4.42e-09

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 53.73  E-value: 4.42e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 71834861     429 EMKEKFKKTLEKIQFISPGQPWEEVMCFVMEDEAYKYITEADSKEVYGRHQRE 481
Cdd:smart00441    2 EAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
 31-246 1.56e-08

Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206642 [Multi-domain]  Cd Length: 160  Bit Score: 55.22  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   31 GVGKSCLCNRFVRSKADEYY---PEHTSVlSTIDFggrvvnndhflywgdiiqnseDGVECKIHVI---EQTEFiddqtf 104
Cdd:cd00876    9 GVGKSALTIRFVSGEFVEEYdptIEDSYR-KQIVV---------------------DGETYTLDILdtaGQEEF------ 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  105 lphrSTNLQPYIKraaasklqsaeklmyictdqlgleqdfeqkqmpegklNVDGFLLCIDVsqgCNRK-FDDQLKFVNNL 183
Cdd:cd00876   61 ----SAMRDQYIR-------------------------------------NGDGFILVYSI---TSREsFEEIKNIREQI 96

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71834861  184 FVQLSKSKKPVIIAATKCDEcvDHYlREV-----QAFAsNKKNLLVVETSARFNVNIETCFTALVQML 246
Cdd:cd00876   97 LRVKDKEDVPIVLVGNKCDL--ENE-RQVsteegEALA-EEWGCPFLETSAKTNINIDELFNTLVREI 160
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 28-244 3.04e-07

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 51.75  E-value: 3.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861     28 GNCGVGKSCLCNRFVRSKADEYYpehtsvLSTIdfggrvvnndhflywgdiiqnsedGVECKIHVIEqtefIDDQTflph 107
Cdd:pfam00071    6 GDGGVGKSSLLIRFTQNKFPEEY------IPTI------------------------GVDFYTKTIE----VDGKT---- 47

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    108 rstnlqpyikraaaSKLQsaeklmyIcTDQLGLEqDFE---QKQMPegklNVDGFLLCIDVSqgcNRK-FDDQLKFVNNL 183
Cdd:pfam00071   48 --------------VKLQ-------I-WDTAGQE-RFRalrPLYYR----GADGFLLVYDIT---SRDsFENVKKWVEEI 97

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71834861    184 FVQLSKSKkPVIIAATKCD----ECVDhyLREVQAFAsNKKNLLVVETSARFNVNIETCFTALVQ 244
Cdd:pfam00071   98 LRHADENV-PIVLVGNKCDledqRVVS--TEEGEALA-KELGLPFMETSAKTNENVEEAFEELAR 158
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 271-325 3.33e-06

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 45.64  E-value: 3.33e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 71834861     271 TATDKFEKLVQTVRD--YHATWKTVSNKLKNHPdyeEYINLEGTRKARNTFSKHIEQ 325
Cdd:smart00441    2 EAKEAFKELLKEHEVitPDTTWSEARKKLKNDP---RYKALLSESEREQLFEDHIEE 55
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
 28-244 8.30e-06

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 47.50  E-value: 8.30e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861      28 GNCGVGKSCLCNRFVRskaDEYYPEHTSvlsTIdfggrvvnndhflywgdiiqnsedGVECKIHVIEqtefIDDQTFlph 107
Cdd:smart00175    7 GDSGVGKSSLLSRFTD---GKFSEQYKS---TI------------------------GVDFKTKTIE----VDGKRV--- 49

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861     108 rstnlqpyikraaasKLQsaeklmyICtDQLGLE------QDFEQkqmpegklNVDGFLLCIDVSqgcNRK-FDDQLKFV 180
Cdd:smart00175   50 ---------------KLQ-------IW-DTAGQErfrsitSSYYR--------GAVGALLVYDIT---NREsFENLENWL 95

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71834861     181 NNLfVQLSKSKKPVIIAATKCDEcvDHyLREV-----QAFASnKKNLLVVETSARFNVNIETCFTALVQ 244
Cdd:smart00175   96 KEL-REYASPNVVIMLVGNKSDL--EE-QRQVsreeaEAFAE-EHGLPFFETSAKTNTNVEEAFEELAR 159
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 484-533 2.26e-05

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 43.33  E-value: 2.26e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 71834861     484 EKAKEEFQEMLFEHSELFYDLDLNATPSSDKMSEIH-TVLSEEPRYKALQK 533
Cdd:smart00441    1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYkALLSESEREQLFED 51
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 485-545 4.46e-05

FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.


Pssm-ID: 426471 [Multi-domain]  Cd Length: 50  Bit Score: 42.06  E-value: 4.46e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71834861    485 KAKEEFQEMLFEHselfydldlNATPSSdKMSEIHTVLSEEPRYKALQKLApDRESLLLKH 545
Cdd:pfam01846    1 KAREAFKELLKEH---------KITPYS-TWSEIKKKIENDPRYKALLDGS-EREELFEDY 50
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
28-246 2.17e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 43.82  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   28 GNCGVGKSCLCNRFVRSK--ADEYYPEHTSVLSTIDFggrvvnndhflywgdiiqnSEDGVECKIHVIE---QTEFIDDQ 102
Cdd:COG1100   10 GTGGVGKTSLVNRLVGDIfsLEKYLSTNGVTIDKKEL-------------------KLDGLDVDLVIWDtpgQDEFRETR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  103 TFLphrstnlqpyikraaASKLQSAeklmyictdqlgleqdfeqkqmpegklnvDGFLLCIDVSQgcnRKFDDQLKFVNN 182
Cdd:COG1100   71 QFY---------------ARQLTGA-----------------------------SLYLFVVDGTR---EETLQSLYELLE 103

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71834861  183 LFVQLSKsKKPVIIAATKCDECVDHYLRE---VQAFASNKKNLLVVETSARFNVNIETCFTALVQML 246
Cdd:COG1100  104 SLRRLGK-KSPIILVLNKIDLYDEEEIEDeerLKEALSEDNIVEVVATSAKTGEGVEELFAALAEIL 169
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 368-420 6.39e-04

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 39.09  E-value: 6.39e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 71834861     368 MEKRADFQLCFVVLEK----TPWDETDHIDKINDRRIpfDLLSTLEAEKVYQNHVQH 420
Cdd:smart00441    1 EEAKEAFKELLKEHEVitpdTTWSEARKKLKNDPRYK--ALLSESEREQLFEDHIEE 55
 
Name Accession Description Interval E-value
RhoGAP_pG1_pG2 pfam19518
p190RhoGAP, pG1 and pG2 domains; The p190RhoGAP (GTPase-activating protein) proteins, ...
 556-1263 0e+00

p190RhoGAP, pG1 and pG2 domains; The p190RhoGAP (GTPase-activating protein) proteins, p190RhoGAP-A (ARHGAP35) and p190RhoGAP-B (ARHGAP5)4-6, regulates Rho GTP hydrolysis and are important for proper Rho signalling. They share a domain organization containing a GTP-binding GTPase domain, four FF domains, two GTPase-like folds (pG1 and pG2) in the middle domain and a C-terminal GAP domain. This entry represents pG1 and pG2 which are important for GAP activity toward RhoA and were classified as pseudoGTPases as they lack nucleotide-binding activity. Crystal structures revealed a small GTPase fold in both cases with a central 6-stranded beta-sheet surrounded by four alpha-helices.


Pssm-ID: 466111  Cd Length: 699  Bit Score: 1100.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    556 TCLSGQNCTDIKVEQLLASSLLQLDHGRLRLYHDSTNIDKVNLFILGKDGLAQELANEIRTQST-DDEYALDGKIYELDL 634
Cdd:pfam19518    1 TCPSGPNCVDSKIEQLLASRFPQPYPRRLKSYHDDANIDRINLVILGKDGLARELANEIRALCTnDDKYVLDGKMYELSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    635 RPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLSFIGEFIGKIRTEASQiRKDKYMANLPFTLILANQR-DSISKNLPI 713
Cdd:pfam19518   81 RPIEGNVRLPVNSFQTPTFKPHGCLCLYNSKESLSYVVESIEKSRESTLG-RRDNHLAHLPLTLILVNKRgDIGGETLQS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    714 LRHQGQQLANKLQCPFVDVP--AGTYPRKFNETQIKQALRGVLESVKHNLDVVSPIPANKDLSEADLRIVMCAMCGDPFS 791
Cdd:pfam19518  160 LIQQGQQVANKLQCPFLDPAspGGGYGRNFNEKQINQVLRGLLESKRHNLNVVSPAPSIKDLSEADLRIVMCLMCGDPFS 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    792 VDLILSPFLDSHSCSAAQAGQNNSLMLDKIIGEKRRRIQITILSYHSSIGVRKDELVHGYILVYSAKRKASMGMLRAFLS 871
Cdd:pfam19518  240 VDLILSPFLQSQHCRPAQPGSGNSVLLELIIGGQRRRIELSILSYHSSFGVRKSRLVHGYILVYSAKRKASMAMLRAFLC 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    872 EVQDTIPVQLVAVTDSQADFFENEAIKELMTEGEHIATEITAKFTALYSLSQYHRQTEVFTLFFSDVLEKKNMIENSYLS 951
Cdd:pfam19518  320 EVQDIIPVQLVAVTDSQADFFESEVSREQLTEGEEIAHEIEAKFTALYCGSGYQHQTEVFTPFFKEVLEKKTIIEASHMY 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    952 DNTRESTHQsEDVFLPSPRDC--FPYNNYPDSDDDTEAPPPYSPIGDDVQLLptPSDRSRYRLDLEGNEYPIHSTPNCHD 1029
Cdd:pfam19518  400 DNTAEACST-EEEFFSSPRAGspSPNSNLPDSEDDTEPPPPYSPIRDDVQLL--PSDRSKFSLDLEGNDYSVISTPSSFE 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   1030 HERNHkVPPPIKPKPVVPKTNVKKLDPNLLktIEAGIGKNPRKQTSRVPLAHPEDMDPSDnYAEPIDTIFKQKGYSDEIY 1109
Cdd:pfam19518  477 SKLNN-KVPPPVKPKPPVKFDVRKLDPNLY--IDGGNRDGPRSLPSRVTWAPGEGYDPSD-YAEPMDAVVKPRGEEENIY 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   1110 VVPDDS-QNRI-KIRNSFVNNTQGdEENGFSDRTSKSHGERR--------PSKYKYKSKTLfSKAKSyYRRTHSDASDDE 1179
Cdd:pfam19518  553 SVPHDStQGKIiTIRNSNKTQSNG-EGNGSDSEADSSSLERRkksalgvkPRLYRDRSKRL-GKFSS-YRTSFSVGSDDE 629

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   1180 AFTTSKTKRKGRHRGSEEDPLLSPVEtwkGGIDNPAITSDQElddkkmkkkthKVKEDKKKKKTKNFNPPTRRNWESNYF 1259
Cdd:pfam19518  630 LGPIRKKKREDDHGGSKGDNLLNPYE---GGIEDPKRRNILR-----------SLRRTTKKPKPKPRPSISKPTWESNYF 695


                   ....
gi 71834861   1260 GMPL 1263
Cdd:pfam19518  696 GVPL 699
pseudoGTPaseD_p190RhoGAP-B cd22220
pseudoGTPase domain found in p190RhoGAP-B and similar proteins; p190RhoGAP protein B ...
 592-762 1.48e-120

pseudoGTPase domain found in p190RhoGAP-B and similar proteins; p190RhoGAP protein B (p190RhoGAP-B), also called ARHGAP5, or p190-B, or Rho-type GTPase-activating protein 5 (RHOGAP5), is a Rho family GTPase-activating protein (GAP) that acts as a key regulator of Rho GTPase signaling and is essential for actin cytoskeletal structure and contractility. This model corresponds to the GTPase-like domain called pseudoGTPase domain that is located at the middle region of p190RhoGAP-B. Rho family GTPase-activating proteins normally have five highly conserved sequence motifs, termed 'G-motifs', required for nucleotide-binding and catalytic activity. PseudoGTPases consist of a GTPase fold lacking one or more of these G motifs.


Pssm-ID: 412065  Cd Length: 171  Bit Score: 373.80  E-value: 1.48e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  592 NIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLSFI 671
Cdd:cd22220    1 NIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDANSPYLLSQLWTSAFKPHGCFCVFNSIESLNFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  672 GEFIGKIRTEASQIRKDKYMANLPFTLILANQRDSISKNLPILRHQGQQLANKLQCPFVDVPAGTYPRKFNETQIKQALR 751
Cdd:cd22220   81 GECIGKIRAEASQIRRDRYIANLPFTLILANQRDSVSKNLPILRHQGQQLANKLQCPFVDVPAGTYPRKFNETQIKQALR 160

                        170
                 ....*....|.
gi 71834861  752 GVLESVKHNLD 762
Cdd:cd22220  161 GVLESVKHNLD 171
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1443 7.63e-113

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: 353.30  E-value: 7.63e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFA 1338
Cdd:cd04373    1 FGVPLANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDFTVNAVAGALKSFFS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1339 DLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMR 1418
Cdd:cd04373   81 ELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR 160

                        170       180
                 ....*....|....*....|....*
gi 71834861 1419 PDFENREFLSTTKIHQSVVETFIQQ 1443
Cdd:cd04373  161 PDFTSMEALSATRIYQTIIETFIQQ 185
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 1271-1444 5.91e-67

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: 223.30  E-value: 5.91e-67
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    1271 KPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFADLPDPLIPYSLH 1350
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    1351 PELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMRPDFENREFLSTT 1430
Cdd:smart00324   81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160

                           170
                    ....*....|....
gi 71834861    1431 KIHQSVVETFIQQC 1444
Cdd:smart00324  161 RHQNTVIEFLIENA 174
pseudoGTPaseD_p190RhoGAP cd22207
pseudoGTPase domain found in the family of p190RhoGAP; This family includes two p190RhoGAP ...
 596-759 1.40e-64

pseudoGTPase domain found in the family of p190RhoGAP; This family includes two p190RhoGAP proteins, A and B, which are Rho family GTPase-activating proteins (GAPs) that act as key regulators of Rho GTPase signaling and are essential for actin cytoskeletal structure and contractility. Rho family is one of five Ras superfamily subgroups (Ras, Rho, Rab, Ran and Arf). Each contains five highly conserved sequence motifs, termed 'G-motifs', required for nucleotide-binding and catalytic activity. PseudoGTPases consist of a GTPase fold lacking one or more of these G motifs. This model corresponds to the GTPase-like domain called pseudoGTPase domain that is located at the middle region of p190RhoGAP proteins.


Pssm-ID: 412064  Cd Length: 166  Bit Score: 216.36  E-value: 1.40e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  596 VNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLSFIGEFI 675
Cdd:cd22207    1 LNLVLLGSDGLADELANEIRALCEDDEYELDGVVYSLDLRTIDGDVSLPQNSFQTTDFKPHGCLCVYSSRESLEYIKTSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  676 GKIRTEASQIRKDKYMANLPFTLILANQRDSISKNLPILRHQGQQLANKLQCPFVDVPAGTYP--RKFNETQIKQALRGV 753
Cdd:cd22207   81 EKTLLSDLEEEDKLPFQGLPIVLLFARDPSISEKEVSQLREEGQELADRLQCVFIDVPSSGEAmgRKFHESQIDDALRSL 160


                 ....*.
gi 71834861  754 LESVKH 759
Cdd:cd22207  161 IESIKH 166
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 1274-1420 9.85e-60

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 201.62  E-value: 9.85e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   1274 PLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFADLPDPLIPYSLHPEL 1353
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71834861   1354 LEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMRPD 1420
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147
pseudoGTPaseD_p190RhoGAP-A cd22221
pseudoGTPase domain found in p190RhoGAP-A and similar proteins; p190RhoGAP protein A ...
 592-760 5.61e-55

pseudoGTPase domain found in p190RhoGAP-A and similar proteins; p190RhoGAP protein A (p190RhoGAP-A), also called Rho GTPase-activating protein 35(RHOGAP35), glucocorticoid receptor DNA-binding factor 1, or glucocorticoid receptor repression factor 1 (GRF-1), or Rho GAP p190A, or p190-A, is a Rho family GTPase-activating protein (GAP) that acts as a key regulator of Rho GTPase signaling and is essential for actin cytoskeletal structure and contractility. It binds several acidic phospholipids which inhibits the Rho GAP activity to promote the Rac GAP activity. This model corresponds to the GTPase-like domain called pseudoGTPase domain that is located at the middle region of p190RhoGAP-A. Rho family GTPase-activating proteins normally have five highly conserved sequence motifs, termed 'G-motifs', required for nucleotide-binding and catalytic activity. PseudoGTPases would consist of a GTPase fold lacking one or more of these G motifs.


Pssm-ID: 412066  Cd Length: 172  Bit Score: 189.31  E-value: 5.61e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  592 NIDKVNLFILGKDGLAQELANEIRTQST-DDEYALDGKIYELDLRPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLSF 670
Cdd:cd22221    1 NVDRINLVILGKDGLARELANEIRALCTnDDKYVLDGKMYELSLRPIEGNVRLPVNSFQTPTFQPHGCLCLYNSKESLSY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  671 IGEFIGKIRtEASQIRKDKYMANLPFTLILANQR-DSISKNLPILRHQGQQLANKLQCPFVDvPAGT---YPRKFNETQI 746
Cdd:cd22221   81 VVESIEKSR-ESTLGRRDNHLAHLPLTLILVNKRgDTSGETLQSLIQQGQQVASKLQCVFLD-PASTgigYGRNINEKQI 158

                        170
                 ....*....|....
gi 71834861  747 KQALRGVLESVKHN 760
Cdd:cd22221  159 SQILKGLLDSKRNL 172
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 1274-1442 1.44e-54

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: 187.89  E-value: 1.44e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1274 PLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSmEVTVNAVAGALKAFFADLPDPLIPYSLHPEL 1353
Cdd:cd00159    1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLE-DYDVHDVASLLKLYLRELPEPLIPFELYDEF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1354 LEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMRPDFENREFLSTTKIH 1433
Cdd:cd00159   80 IELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELLEDIKKL 159


                 ....*....
gi 71834861 1434 QSVVETFIQ 1442
Cdd:cd00159  160 NEIVEFLIE 168
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1448 1.05e-44

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: 160.38  E-value: 1.05e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAEK-PIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEV--TVNAVAGALKA 1335
Cdd:cd04372    1 YGCDLTTLVKAHNtQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADISATVypDINVITGALKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1336 FFADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPT 1415
Cdd:cd04372   81 YFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPT 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 71834861 1416 LMRPDFENREFLSTTKIHQS-VVETFIQQCQFFF 1448
Cdd:cd04372  161 LMRPPEDSALTTLNDMRYQIlIVQLLITNEDVLF 194
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1448 3.40e-41

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: 150.63  E-value: 3.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTA--EKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQfdqdhnINLVSMEVT--------VNA 1328
Cdd:cd04395    2 FGVPLDDCPPSseNPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEE------LNRGGFDIDlqdprwrdVNV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1329 VAGALKAFFADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNL 1408
Cdd:cd04395   76 VSSLLKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNL 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 71834861 1409 SICFWPTLMRPDFENREFLSTTKIHQ-SVVETFIQQCQFFF 1448
Cdd:cd04395  156 AIVFGPTLVRTSDDNMETMVTHMPDQcKIVETLIQHYDWFF 196
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1259-1443 1.96e-40

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: 147.92  E-value: 1.96e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAEKP-IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTdqdNIQK---QFDQDHNINL-VSMEVTVNAVAGAL 1333
Cdd:cd04403    1 FGCHLEALCQRENStVPKFVRLCIEAVEKRGLDVDGIYRVSGNLA---VIQKlrfAVDHDEKLDLdDSKWEDIHVITGAL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1334 KAFFADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFW 1413
Cdd:cd04403   78 KLFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFG 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 71834861 1414 PTLMRPDFENREfLSTTKIHQS-VVETFIQQ 1443
Cdd:cd04403  158 PTLLRPEQETGN-IAVHMVYQNqIVELILLE 187
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1448 2.59e-40

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: 147.94  E-value: 2.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAEKP-IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQD-HNINLVSMEVT---VNAVAGAL 1333
Cdd:cd04398    1 FGVPLEDLILREGDnVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDpLNVLLISPEDYesdIHSVASLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1334 KAFFADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFW 1413
Cdd:cd04398   81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 71834861 1414 PTLMRPDFENREFLSttkiHQS-VVETFIQQCQFFF 1448
Cdd:cd04398  161 PTLMNAAPDNAADMS----FQSrVIETLLDNAYQIF 192
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 1273-1420 6.72e-40

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: 146.30  E-value: 6.72e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1273 IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQD-HNINLVSMEVTVNAVAGALKAFFADLPDPLIPYSLHP 1351
Cdd:cd04385   15 IPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDaRSVQLREGEYTVHDVADVLKRFLRDLPDPLLTSELHA 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71834861 1352 ELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMRPD 1420
Cdd:cd04385   95 EWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQTD 163
RhoGAP-FF1 pfam16512
p190-A and -B Rho GAPs FF domain; RhoGAP-FF1 is the FF domain of the Rho GTPase activating ...
 260-338 3.42e-36

p190-A and -B Rho GAPs FF domain; RhoGAP-FF1 is the FF domain of the Rho GTPase activating proteins (GAPs). These are the key proteins that make the switch between the active guanosine-triphosphate-bound form of Rho guanosine triphosphatases (GTPases) and the inactive guanosine-diphosphate-bound form. Rho guanosine triphosphatases (GTPases) are a family of proteins with key roles in the regulation of actin cytoskeleton dynamics. The RhoGAP-FF1 region contains the FF domain that has been implicated in binding to the transcription factor TFII-I; and phosphorylation of Tyr308 within the first FF domain inhibits this interaction. The RhoGAPFF1 domain constitutes the first solved structure of an FF domain that lacks the first of the two highly conserved Phe residues, but the substitution of Phe by Tyr does not affect the domain fold.


Pssm-ID: 465153  Cd Length: 80  Bit Score: 131.56  E-value: 3.42e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    260 DAYKTQRQLVVTATDKFEKLV-QTVRDYHATWKTVSNKLKNHPDYEEYINLEGTRKARNTFSKHIEQLKQEHIRKRREEY 338
Cdd:pfam16512    1 EAAKVRKELLDSATDAFERLIrSQVTDYRALWKTVSKKLSQHPEYQEYVELFGTDKAKRLFRKHIKKLKDEHIRKRRQGY 80
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1453 1.23e-35

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: 134.89  E-value: 1.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQD-LVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDH-NINLVSMEVTVNAVAGALKAF 1336
Cdd:cd04386    5 FGTPLEEhLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTfSLPLDEFYSDPHAVASALKSY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1337 FADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTL 1416
Cdd:cd04386   85 LRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAPNL 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 71834861 1417 --MRPDFENREFLSTTKIH-QSVVETFIQQCQFFFyNGEI 1453
Cdd:cd04386  165 lwAKNEGSLAEMAAGTSVHvVAIVELIISHADWFF-PGEV 203
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1259-1420 1.74e-32

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: 125.24  E-value: 1.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQD-HNINLvsMEVTVNAVAGALKAFF 1337
Cdd:cd04377    1 FGVSLSSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDpDSVNL--EDYPIHVITSVLKQWL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1338 ADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLM 1417
Cdd:cd04377   79 RELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCIL 158


                 ....
gi 71834861 1418 R-PD 1420
Cdd:cd04377  159 RcPD 162
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 1276-1442 1.42e-31

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: 123.27  E-value: 1.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1276 FVEKCVEFIEDTGLCTEGLYRVSGNKTdqdNIQKQ----FDQ----DHNINLVSMEVTVNAVAGALKAFFADLPDPLIPY 1347
Cdd:cd04374   31 FVRKCIEAVETRGINEQGLYRVVGVNS---KVQKLlslgLDPktstPGDVDLDNSEWEIKTITSALKTYLRNLPEPLMTY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1348 SLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMRPDFENREFL 1427
Cdd:cd04374  108 ELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEETVAAI 187

                        170
                 ....*....|....*
gi 71834861 1428 STTKIHQSVVETFIQ 1442
Cdd:cd04374  188 MDIKFQNIVVEILIE 202
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1263-1438 3.40e-29

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: 115.85  E-value: 3.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1263 LQDLVTAEKP-IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSmEVTVNAVAGALKAFFADLP 1341
Cdd:cd04382    6 LADFDPSTSPmIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLS-KVDIHVICGCLKDFLRSLK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1342 DPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQhKINLMTADNLSICFWPTLM---R 1418
Cdd:cd04382   85 EPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQS-PECKMDINNLARVFGPTIVgysV 163

                        170       180
                 ....*....|....*....|
gi 71834861 1419 PDFENREFLSTTKIHQSVVE 1438
Cdd:cd04382  164 PNPDPMTILQDTVRQPRVVE 183
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1419 1.71e-28

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: 113.97  E-value: 1.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVT---AEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLvSMEVTVNAVAGALKA 1335
Cdd:cd04404    6 FGVSLQFLKEknpEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEPVDF-DQYEDVHLPAVILKT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1336 FFADLPDPLIPYSLHPELLEAAKIpDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPT 1415
Cdd:cd04404   85 FLRELPEPLLTFDLYDDIVGFLNV-DKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGPN 163


                 ....
gi 71834861 1416 LMRP 1419
Cdd:cd04404  164 LLWA 167
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 1273-1449 4.29e-28

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: 113.10  E-value: 4.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1273 IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSM-EVTVNAVAGALKAFFADLPDPLIPYSLHP 1351
Cdd:cd04387   16 VPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLsEMDVNAIAGTLKLYFRELPEPLFTDELYP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1352 ELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMRPDfENREFLSTTK 1431
Cdd:cd04387   96 NFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPS-EKESKIPTNT 174

                        170
                 ....*....|....*...
gi 71834861 1432 IHQSVVETFIQQCQFFFY 1449
Cdd:cd04387  175 MTDSWSLEVMSQVQVLLY 192
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1273-1419 3.47e-27

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: 110.59  E-value: 3.47e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1273 IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDqdHNINLVSM-EVTVNAVAGALKAFFADLPDPLIPYSLHP 1351
Cdd:cd04378   16 VPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFE--NGKDLVELsELSPHDISSVLKLFLRQLPEPLILFRLYN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1352 ELLEAAK-------------IPDKTER-LHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLM 1417
Cdd:cd04378   94 DFIALAKeiqrdteedkapnTPIEVNRiIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTLI 173


                 ..
gi 71834861 1418 RP 1419
Cdd:cd04378  174 RP 175
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1438 7.92e-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: 109.09  E-value: 7.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAEKP---IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLvSMEVTVNAVAGALKA 1335
Cdd:cd04393    3 FGVPLQELQQAGQPengVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDL-SKEADVCSAASLLRL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1336 FFADLPDPLIPYSLHPELLEA-AKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWP 1414
Cdd:cd04393   82 FLQELPEGLIPASLQIRLMQLyQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAVFGP 161

                        170       180
                 ....*....|....*....|....*..
gi 71834861 1415 TL--MRPDFEN-REFLSTTKIHQSVVE 1438
Cdd:cd04393  162 DVfhVYTDVEDmKEQEICSRIMAKLLE 188
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1259-1420 1.17e-26

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: 108.54  E-value: 1.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNiNLVSMEVTVNAVAGALKAFFA 1338
Cdd:cd04407    1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPE-NVKLENYPIHAITGLLKQWLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1339 DLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMR 1418
Cdd:cd04407   80 ELPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLR 159


                 ...
gi 71834861 1419 -PD 1420
Cdd:cd04407  160 cPD 162
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1259-1416 1.42e-26

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: 107.91  E-value: 1.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAEK-----PIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVnaVAGAL 1333
Cdd:cd04381    1 FGASLSLAVERSRchdgiDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLEEYEPPT--VASLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1334 KAFFADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFW 1413
Cdd:cd04381   79 KQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLS 158


                 ...
gi 71834861 1414 PTL 1416
Cdd:cd04381  159 PTV 161
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1447 3.20e-26

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: 107.59  E-value: 3.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQD-LVTAEKPIPLFVEKCVEFIEDTGLCTeGLYRVSGNktdQDNIQK---QFDQDHNINLVS--MEVTVNAVAGA 1332
Cdd:cd04384    3 FGCDLTEhLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGI---ASNIQRlrhEFDSEQIPDLTKdvYIQDIHSVSSL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1333 LKAFFADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICF 1412
Cdd:cd04384   79 CKLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVW 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 71834861 1413 WPTLMR-PDFENREFLSTTKIHQSVVETFIQQCQFF 1447
Cdd:cd04384  159 APNLLRsKQIESACFSGTAAFMEVRIQSVVVEFILN 194
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1271-1420 7.64e-26

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: 106.35  E-value: 7.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1271 KPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHN-INLVSMEVTVNAVAGALKAFFADLPDPLIPYSL 1349
Cdd:cd04383   16 QAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDpLADDQNDHDINSVAGVLKLYFRGLENPLFPKER 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71834861 1350 HPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMR-PD 1420
Cdd:cd04383   96 FEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLMPvPE 167
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 1259-1427 8.34e-26

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: 106.29  E-value: 8.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVT------AEKPIPLFVEKCVEFIEDTG-LCTEGLYRVSGNKTDQDNIQKQFDQDHNINLV--SMEVTVNAV 1329
Cdd:cd04400    2 FGSPLEEAVElsshkyNGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTEYDVDLFssSLYPDVHTV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1330 AGALKAFFADLPDPLIPYSLHPELLEAAKIP-DKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNL 1408
Cdd:cd04400   82 AGLLKLYLRELPTLILGGELHNDFKRLVEENhDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRNV 161

                        170
                 ....*....|....*....
gi 71834861 1409 SICFWPTLMRPDFENREFL 1427
Cdd:cd04400  162 CIVFSPTLNIPAGIFVLFL 180
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1259-1423 1.02e-24

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: 103.29  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAEKP-----IPLFVEKCVEFIEDTGLCTEGLYRVSGnktdQDNIQKQFDQDHNIN---LVSMEVTVNAVA 1330
Cdd:cd04390    3 FGQRLEDTVAYERKfgprlVPILVEQCVDFIREHGLKEEGLFRLPG----QANLVKQLQDAFDAGerpSFDSDTDVHTVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1331 GALKAFFADLPDPLIPYSLHPELLEAAKIPDKTER--LHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNL 1408
Cdd:cd04390   79 SLLKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEkgLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNL 158

                        170
                 ....*....|....*
gi 71834861 1409 SICFWPTLMRPDFEN 1423
Cdd:cd04390  159 ATVFGPNILRPKVED 173
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1259-1420 6.05e-23

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: 97.76  E-value: 6.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQD-HNINLVSMEVTVnaVAGALKAFF 1337
Cdd:cd04406    1 FGVELSRLTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDaNSVNLDDYNIHV--IASVFKQWL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1338 ADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLM 1417
Cdd:cd04406   79 RDLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCIL 158


                 ....
gi 71834861 1418 R-PD 1420
Cdd:cd04406  159 RcPD 162
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 1273-1419 1.45e-22

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: 97.19  E-value: 1.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1273 IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSmEVTVNAVAGALKAFFADLPDPLIPYSLHPE 1352
Cdd:cd04408   16 VPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLS-GHSPHDITSVLKHFLKELPEPVLPFQLYDD 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71834861 1353 LLEAAK--------IPDKT----ERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMRP 1419
Cdd:cd04408   95 FIALAKelqrdsekAAESPsiveNIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLLRP 173
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1273-1419 3.73e-22

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: 96.42  E-value: 3.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1273 IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSmEVTVNAVAGALKAFFADLPDPLIPYSLHPE 1352
Cdd:cd04409   16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELS-ELSPHDISNVLKLYLRQLPEPLILFRLYNE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1353 LLEAAK------IPDKTERLHA----------------LKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSI 1410
Cdd:cd04409   95 FIGLAKesqhvnETQEAKKNSDkkwpnmctelnrillkSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNLGI 174


                 ....*....
gi 71834861 1411 CFWPTLMRP 1419
Cdd:cd04409  175 IFGPTLIRP 183
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1445 6.07e-22

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: 95.23  E-value: 6.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDL----VTAEKPIPLFVEKCVEFIEDTgLCTEGLYRVSGNKTDQDNIQKQFDQDHNinlvsmeVTVNA----VA 1330
Cdd:cd04394    2 FGVPLHSLphstVPEYGNVPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEA-------CLSSAlpcdVA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1331 GALKAFFADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSI 1410
Cdd:cd04394   74 GLLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAV 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 71834861 1411 CFWPTLMrPDFENREFLST-----TKIHQSVVETFIQQCQ 1445
Cdd:cd04394  154 IFAPNLF-QSEEGGEKMSSstekrLRLQAAVVQTLIDNAS 192
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 1259-1419 1.34e-21

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: 94.46  E-value: 1.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAE---KPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVT--VNAVAGAL 1333
Cdd:cd04379    1 FGVPLSRLVEREgesRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEELYpdINVITGVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1334 KAFFADLPDPLIPYSLHPELLEAAKI--PDK--TERLHALKeIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLS 1409
Cdd:cd04379   81 KDYLRELPEPLITPQLYEMVLEALAValPNDvqTNTHLTLS-IIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLA 159

                        170
                 ....*....|
gi 71834861 1410 ICFWPTLMRP 1419
Cdd:cd04379  160 VCFGPVLMFC 169
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1416 6.42e-19

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: 87.02  E-value: 6.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLV------TAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSME-VTVNAVAG 1331
Cdd:cd04391    2 FGVPLSTLLerdqkkVPGSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKFYEGTFLWDqVKQHDAAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1332 ALKAFFADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSIC 1411
Cdd:cd04391   82 LLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAMI 161


                 ....*
gi 71834861 1412 FWPTL 1416
Cdd:cd04391  162 MAPNL 166
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1265-1448 1.21e-18

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: 85.96  E-value: 1.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1265 DLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSmEVTVNAVAGALKAFFADLPDPL 1344
Cdd:cd04376    1 SLNPIARQVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDE-NHSVHDVAALLKEFFRDMPDPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1345 IPYSLHPELLEAAKIPDKtERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQ---------HKI--NLMTADNLSICFW 1413
Cdd:cd04376   80 LPRELYTAFIGTALLEPD-EQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEHaadsidedgQEVsgNKMTSLNLATIFG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 71834861 1414 PTLMRPD-FENREFLSTT-----KIHQ-SVVETFIQQCQFFF 1448
Cdd:cd04376  159 PNLLHKQkSGEREFVQASlrieeSTAIiNVVQTMIDNYEELF 200
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1448 4.51e-17

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: 81.19  E-value: 4.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVTAEKPiPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVnaVAGALKAFFA 1338
Cdd:cd04402    2 FGQPLSNICEDDNL-PKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVEVDLKAEPVLL--LASVLKDFLR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1339 DLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMR 1418
Cdd:cd04402   79 NIPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLW 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 71834861 1419 PDFENREFLSTTKIHQSVVETFIQQCQFFF 1448
Cdd:cd04402  159 PPASSELQNEDLKKVTSLVQFLIENCQEIF 188
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1441 5.38e-17

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: 81.35  E-value: 5.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPL-QDLVTAEKPIPLFVEKcvefiedtGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFF 1337
Cdd:cd04392    1 FGAPLtEEGIAQIYQLIEYLEK--------NLRVEGLFRKPGNSARQQELRDLLNSGTDLDLESGGFHAHDCATVLKGFL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1338 ADLPDPLIPYSLHPELLEAAK------------IPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTA 1405
Cdd:cd04392   73 GELPEPLLTHAHYPAHLQIADlcqfdekgnktsAPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSA 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 71834861 1406 DNLSICFWPTLMRPDFENREFLSTTKIHQSVVETFI 1441
Cdd:cd04392  153 DNLALLFTPHLICPRNLTPEDLHENAQKLNSIVTFM 188
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1273-1442 2.23e-14

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: 73.98  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1273 IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQ--DHNINLVSMEVTVNAVAGALKAFFADLPDPLIPYSLH 1350
Cdd:cd04396   32 IPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTppDYGKSFDWDGYTVHDAASVLRRYLNNLPEPLVPLDLY 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1351 PE----LLEAAKIP-------------DKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFW 1413
Cdd:cd04396  112 EEfrnpLRKRPRILqymkgrineplntDIDQAIKEYRDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIFQ 191

                        170       180       190
                 ....*....|....*....|....*....|..
gi 71834861 1414 PTLM---RPDFENREflstTKIHQSVVETFIQ 1442
Cdd:cd04396  192 PGILshpDHEMDPKE----YKLSRLVVEFLIE 219
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1257-1436 1.13e-12

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: 68.98  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1257 NYFGMPLqdLVTAEK---PIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTdqdNIQK--QFDQDHNINLVSMEVTVNAVAG 1331
Cdd:cd04375    3 NVFGVPL--LVNLQRtgqPLPRSIQQAMRWLRNNALDQVGLFRKSGVKS---RIQKlrSMIESSTDNVNYDGQQAYDVAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1332 ALKAFFADLPDPLIPYSLHPELLEAAKIPDKTERLHALKEIVKKFHPVNYDVFRYVITHLNRVSQQHKINLMTADNLSIC 1411
Cdd:cd04375   78 MLKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVC 157

                        170       180
                 ....*....|....*....|....*
gi 71834861 1412 FWPTLMRPDFENREFLSTTKIHQSV 1436
Cdd:cd04375  158 LAPSLFHLNTSRRENSSPARRMQRK 182
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1291-1443 3.72e-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: 66.65  E-value: 3.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1291 TEGLYRVSGNKTDQDNIQKQFDQDHnINLVSMEvTVNAVAGALKAFFADLPDPLIPYSLHPELLEAAKIPDKTerlhalK 1370
Cdd:cd04389   40 TEGIFRVPGDIDEVNELKLRVDQWD-YPLSGLE-DPHVPASLLKLWLRELEEPLIPDALYQQCISASEDPDKA------V 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71834861 1371 EIVKKFHPVNYDVFRYVITHLNRVSQQHKI--NLMTADNLSICFWPTLMRPDFEN-REFLSTTKIHQSVVETFIQQ 1443
Cdd:cd04389  112 EIVQKLPIINRLVLCYLINFLQVFAQPENVahTKMDVSNLAMVFAPNILRCTSDDpRVIFENTRKEMSFLRTLIEH 187
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 1274-1468 4.50e-12

RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in the p85 isoforms of the regulatory subunit of the class IA PI3K (phosphatidylinositol 3'-kinase). This domain is also called Bcr (breakpoint cluster region protein) homology (BH) domain. Class IA PI3Ks are heterodimers, containing a regulatory subunit (p85) and a catalytic subunit (p110) and are activated by growth factor receptor tyrosine kinases (RTKs); this activation is mediated by the p85 subunit. p85 isoforms, alpha and beta, contain a C-terminal p110-binding domain flanked by two SH2 domains, an N-terminal SH3 domain, and a RhoGAP domain flanked by two proline-rich regions. 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: 239853  Cd Length: 200  Bit Score: 66.82  E-value: 4.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1274 PLFVeKCVEFIEDTGLCTEGLYR--VSGNKTDQdniqKQFDQDHNINLVSMEVTVNAVAGALKAFFADLPDPLIPYSLHP 1351
Cdd:cd04388   17 PLLI-KLVEAIEKKGLESSTLYRtqSSSSLTEL----RQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1352 ELLEAAKIPDKT-ERLHALKEIVKKFH-PVNYDV-FRYVITHLNRVSQQHKINLMTADNLSICFWPTLMR---PDFENRE 1425
Cdd:cd04388   92 EMISRAQEVQSSdEYAQLLRKLIRSPNlPHQYWLtLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRfqpASSDSPE 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 71834861 1426 FlsttkiHQSVVETFIQQcqfffyngeivETTNIVAPP--PPSNP 1468
Cdd:cd04388  172 F------HIRIIEVLITS-----------EWNERQAAPalPPKPP 199
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1249-1441 8.83e-10

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: 60.43  E-value: 8.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1249 PTRRNWESNYFGMPLQDLVTAEKPI-------------------PLFVEK----CVEFIEDTGLCTEGLYRvsgNKTDQD 1305
Cdd:cd04380    3 TVTGVYLPSCFGSSLETLIRLPDPGirnlidqlelgdnpdysevPLSIPKeiwrLVDYLYTRGLAQEGLFE---EPGLPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1306 NIQKQF---------DQDHNINLvsmevTVNAVAGALKAFFADLPDPLIPYSLHPELLEAAKiPDKTERLHALKEIVKkf 1376
Cdd:cd04380   80 EPGELLaeirdaldtGSPFNSPG-----SAESVAEALLLFLESLPDPIIPYSLYERLLEAVA-NNEEDKRQVIRISLP-- 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71834861 1377 hPVNYDVFRYVITHLNRVSQQHKINLMTADNLSICFWPTLMRPDFENREFLSTTKIHQ--SVVETFI 1441
Cdd:cd04380  152 -PVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRAGGKERRAERDRkrAFIEQFL 217
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1441 3.06e-09

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: 58.53  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1259 FGMPLQDLVT------------AEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGN----KTDQDNIQKQFDQDHNINlvsm 1322
Cdd:cd04397    1 FGVPLEILVEkfgadstlgvgpGKLRIPALIDDIISAMRQMDMSVEGVFRKNGNirrlKELTEEIDKNPTEVPDLS---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1323 EVTVNAVAGALKAFFADLPDPLIPYSLHPELLEAAKIPDKTER---LHALKEIVKKFHpvnYDVFRYVITHLNRVSQQHK 1399
Cdd:cd04397   77 KENPVQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERkrvLHLVYCLLPKYH---RDTMEVLFSFLKWVSSFSH 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 71834861 1400 I-----NLMTADNLSICFWPTLMRPDFENREFLSTTKIHQSVVETFI 1441
Cdd:cd04397  154 IdeetgSKMDIHNLATVITPNILYSKTDNPNTGDEYFLAIEAVNYLI 200
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 429-481 4.42e-09

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 53.73  E-value: 4.42e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 71834861     429 EMKEKFKKTLEKIQFISPGQPWEEVMCFVMEDEAYKYITEADSKEVYGRHQRE 481
Cdd:smart00441    2 EAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
 31-246 1.56e-08

Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206642 [Multi-domain]  Cd Length: 160  Bit Score: 55.22  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   31 GVGKSCLCNRFVRSKADEYY---PEHTSVlSTIDFggrvvnndhflywgdiiqnseDGVECKIHVI---EQTEFiddqtf 104
Cdd:cd00876    9 GVGKSALTIRFVSGEFVEEYdptIEDSYR-KQIVV---------------------DGETYTLDILdtaGQEEF------ 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  105 lphrSTNLQPYIKraaasklqsaeklmyictdqlgleqdfeqkqmpegklNVDGFLLCIDVsqgCNRK-FDDQLKFVNNL 183
Cdd:cd00876   61 ----SAMRDQYIR-------------------------------------NGDGFILVYSI---TSREsFEEIKNIREQI 96

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71834861  184 FVQLSKSKKPVIIAATKCDEcvDHYlREV-----QAFAsNKKNLLVVETSARFNVNIETCFTALVQML 246
Cdd:cd00876   97 LRVKDKEDVPIVLVGNKCDL--ENE-RQVsteegEALA-EEWGCPFLETSAKTNINIDELFNTLVREI 160
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
 28-244 4.05e-08

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 54.00  E-value: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   28 GNCGVGKSCLCNRFVRSKADEYYPehtsvlSTIdfggrvvnndhflywgdiiqnsedGVECKIHVIEqtefIDDQTFlph 107
Cdd:cd00154    7 GDSGVGKTSLLLRFVDNKFSENYK------STI------------------------GVDFKSKTIE----VDGKKV--- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  108 rstnlqpyikraaasKLQ---SA--EKL-----MYictdqlgleqdFEqkqmpegklNVDGFLLCIDVSqgcNRK-FDDQ 176
Cdd:cd00154   50 ---------------KLQiwdTAgqERFrsitsSY-----------YR---------GAHGAILVYDVT---NREsFENL 91

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71834861  177 LKFVNNLFvQLSKSKKPVIIAATKCD----ECVDHylREVQAFAsNKKNLLVVETSARFNVNIETCFTALVQ 244
Cdd:cd00154   92 DKWLNELK-EYAPPNIPIILVGNKSDledeRQVST--EEAQQFA-KENGLLFFETSAKTGENVDEAFESLAR 159
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 28-244 8.90e-08

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 53.23  E-value: 8.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   28 GNCGVGKSCLCNRFVRSKADEYYPEHTSvlsTIDFggrvvnndhflywgDIIQNSEDGVECKIHVIEqTEFIDDqTFLPH 107
Cdd:cd00882    4 GRGGVGKSSLLNALLGGEVGEVSDVPGT---TRDP--------------DVYVKELDKGKVKLVLVD-TPGLDE-FGGLG 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  108 RSTNLQPYIKRAaasklqsaeklmyictdqlgleqdfeqkqmpegklnvDGFLLCIDVSQGcnRKFDDQLkfvNNLFVQL 187
Cdd:cd00882   65 REELARLLLRGA-------------------------------------DLILLVVDSTDR--ESEEDAK---LLILRRL 102

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  188 SKSKKPVIIAATKCD---ECVDHYLREVQaFASNKKNLLVVETSARFNVNIETCFTALVQ 244
Cdd:cd00882  103 RKEGIPIILVGNKIDlleEREVEELLRLE-ELAKILGVPVFEVSAKTGEGVDELFEKLIE 161
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 28-244 3.04e-07

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 51.75  E-value: 3.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861     28 GNCGVGKSCLCNRFVRSKADEYYpehtsvLSTIdfggrvvnndhflywgdiiqnsedGVECKIHVIEqtefIDDQTflph 107
Cdd:pfam00071    6 GDGGVGKSSLLIRFTQNKFPEEY------IPTI------------------------GVDFYTKTIE----VDGKT---- 47

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    108 rstnlqpyikraaaSKLQsaeklmyIcTDQLGLEqDFE---QKQMPegklNVDGFLLCIDVSqgcNRK-FDDQLKFVNNL 183
Cdd:pfam00071   48 --------------VKLQ-------I-WDTAGQE-RFRalrPLYYR----GADGFLLVYDIT---SRDsFENVKKWVEEI 97

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71834861    184 FVQLSKSKkPVIIAATKCD----ECVDhyLREVQAFAsNKKNLLVVETSARFNVNIETCFTALVQ 244
Cdd:pfam00071   98 LRHADENV-PIVLVGNKCDledqRVVS--TEEGEALA-KELGLPFMETSAKTNENVEEAFEELAR 158
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 271-325 3.33e-06

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 45.64  E-value: 3.33e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 71834861     271 TATDKFEKLVQTVRD--YHATWKTVSNKLKNHPdyeEYINLEGTRKARNTFSKHIEQ 325
Cdd:smart00441    2 EAKEAFKELLKEHEVitPDTTWSEARKKLKNDP---RYKALLSESEREQLFEDHIEE 55
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
 28-244 8.30e-06

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 47.50  E-value: 8.30e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861      28 GNCGVGKSCLCNRFVRskaDEYYPEHTSvlsTIdfggrvvnndhflywgdiiqnsedGVECKIHVIEqtefIDDQTFlph 107
Cdd:smart00175    7 GDSGVGKSSLLSRFTD---GKFSEQYKS---TI------------------------GVDFKTKTIE----VDGKRV--- 49

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861     108 rstnlqpyikraaasKLQsaeklmyICtDQLGLE------QDFEQkqmpegklNVDGFLLCIDVSqgcNRK-FDDQLKFV 180
Cdd:smart00175   50 ---------------KLQ-------IW-DTAGQErfrsitSSYYR--------GAVGALLVYDIT---NREsFENLENWL 95

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71834861     181 NNLfVQLSKSKKPVIIAATKCDEcvDHyLREV-----QAFASnKKNLLVVETSARFNVNIETCFTALVQ 244
Cdd:smart00175   96 KEL-REYASPNVVIMLVGNKSDL--EE-QRQVsreeaEAFAE-EHGLPFFETSAKTNTNVEEAFEELAR 159
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 484-533 2.26e-05

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 43.33  E-value: 2.26e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 71834861     484 EKAKEEFQEMLFEHSELFYDLDLNATPSSDKMSEIH-TVLSEEPRYKALQK 533
Cdd:smart00441    1 EEAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYkALLSESEREQLFED 51
FF pfam01846
FF domain; This domain has been predicted to be involved in protein-protein interaction. This ...
 485-545 4.46e-05

FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions.


Pssm-ID: 426471 [Multi-domain]  Cd Length: 50  Bit Score: 42.06  E-value: 4.46e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71834861    485 KAKEEFQEMLFEHselfydldlNATPSSdKMSEIHTVLSEEPRYKALQKLApDRESLLLKH 545
Cdd:pfam01846    1 KAREAFKELLKEH---------KITPYS-TWSEIKKKIENDPRYKALLDGS-EREELFEDY 50
small_GTPase smart00010
Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small ...
 157-248 1.88e-04

Small GTPase of the Ras superfamily; ill-defined subfamily; SMART predicts Ras-like small GTPases of the ARF, RAB, RAN, RAS, and SAR subfamilies. Others that could not be classified in this way are predicted to be members of the small GTPase superfamily without predictions of the subfamily.


Pssm-ID: 197466 [Multi-domain]  Cd Length: 166  Bit Score: 43.70  E-value: 1.88e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861     157 DGFLLCIDVSqgcNRK-FDDQLKFVNNLFVQLSKSKKPVIIAATKCDEcvdHYLREV-----QAFAsNKKNLLVVETSAR 230
Cdd:smart00010   75 EGFLLVYSIT---DRQsFEEIAKFREQILRVKDRDDVPIVLVGNKCDL---ENERVVsteegKELA-RQWGCPFLETSAK 147

                            90
                    ....*....|....*...
gi 71834861     231 FNVNIETCFTALVQMLDK 248
Cdd:smart00010  148 ERINVDEAFYDLVREIRK 165
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
28-246 2.17e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 43.82  E-value: 2.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861   28 GNCGVGKSCLCNRFVRSK--ADEYYPEHTSVLSTIDFggrvvnndhflywgdiiqnSEDGVECKIHVIE---QTEFIDDQ 102
Cdd:COG1100   10 GTGGVGKTSLVNRLVGDIfsLEKYLSTNGVTIDKKEL-------------------KLDGLDVDLVIWDtpgQDEFRETR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  103 TFLphrstnlqpyikraaASKLQSAeklmyictdqlgleqdfeqkqmpegklnvDGFLLCIDVSQgcnRKFDDQLKFVNN 182
Cdd:COG1100   71 QFY---------------ARQLTGA-----------------------------SLYLFVVDGTR---EETLQSLYELLE 103

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71834861  183 LFVQLSKsKKPVIIAATKCDECVDHYLRE---VQAFASNKKNLLVVETSARFNVNIETCFTALVQML 246
Cdd:COG1100  104 SLRRLGK-KSPIILVLNKIDLYDEEEIEDeerLKEALSEDNIVEVVATSAKTGEGVEELFAALAEIL 169
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
 157-248 5.12e-04

Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. p21Ras couples receptor Tyr kinases and G protein receptors to protein kinase cascades


Pssm-ID: 214541 [Multi-domain]  Cd Length: 164  Bit Score: 42.16  E-value: 5.12e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861     157 DGFLLCIDVSqgcNRK-FDDQLKFVNNLFVQLSKSKKPVIIAATKCDEcvdHYLREV-----QAFAsNKKNLLVVETSAR 230
Cdd:smart00173   73 EGFLLVYSIT---DRQsFEEIKKFREQILRVKDRDDVPIVLVGNKCDL---ESERVVsteegKELA-RQWGCPFLETSAK 145

                            90
                    ....*....|....*...
gi 71834861     231 FNVNIETCFTALVQMLDK 248
Cdd:smart00173  146 ERVNVDEAFYDLVREIRK 163
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 368-420 6.39e-04

Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues.


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 39.09  E-value: 6.39e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 71834861     368 MEKRADFQLCFVVLEK----TPWDETDHIDKINDRRIpfDLLSTLEAEKVYQNHVQH 420
Cdd:smart00441    1 EEAKEAFKELLKEHEVitpdTTWSEARKKLKNDPRYK--ALLSESEREQLFEDHIEE 55
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 156-244 2.42e-03

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 40.59  E-value: 2.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861    156 VDGFLLCIDVSQGcnrkFDDQLKFVnnlFVQLSKSKKPVIIAATKCDECVDHYLREV---------QAFASNKKNLLVVE 226
Cdd:pfam00009   93 ADGAILVVDAVEG----VMPQTREH---LRLARQLGVPIIVFINKMDRVDGAELEEVveevsrellEKYGEDGEFVPVVP 165

                           90
                   ....*....|....*...
gi 71834861    227 TSARFNVNIETCFTALVQ 244
Cdd:pfam00009  166 GSALKGEGVQTLLDALDE 183
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 156-246 4.26e-03

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 39.54  E-value: 4.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  156 VDGFLLCIDVSQGCNRKFddqlkfvnNLFVQLSKSKKPVIIAATKCDECVDHylREVQAFASNKKNLL----VVETSARF 231
Cdd:cd00880   77 ADLVLLVVDSDLTPVEEE--------AKLGLLRERGKPVLLVLNKIDLVPES--EEEELLRERKLELLpdlpVIAVSALP 146

                         90
                 ....*....|....*
gi 71834861  232 NVNIETCFTALVQML 246
Cdd:cd00880  147 GEGIDELRKKIAELL 161
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1309-1423 7.37e-03

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


Pssm-ID: 239864  Cd Length: 212  Bit Score: 39.62  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861 1309 KQFDQDHNINLVSMEVTVnaVAGALKAFFADLPDPLIP----------YSLHPelleAAKIPDKTERLHALKEIVKKFHP 1378
Cdd:cd04399   63 PKKPDKEVIILKKFEPST--VASVLKLYLLELPDSLIPhdiydlirslYSAYP----PSQEDSDTARIQGLQSTLSQLPK 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 71834861 1379 VNYDVFRYVITHLNRVSQQHKIN---LMTADNLSICFWPTLMRPDFEN 1423
Cdd:cd04399  137 SHIATLDAIITHFYRLIEITKMGeseEEYADKLATSLSREILRPIIES 184
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
156-246 8.20e-03

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 39.97  E-value: 8.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834861  156 VDGFLLCIDVSqgcnRKFDDQLKFVNNlfvQLSKSKKPVIIAATKCD----ECVDHYLREVQAFASNKKnllVVETSARF 231
Cdd:COG1159   83 VDVILFVVDAT----EKIGEGDEFILE---LLKKLKTPVILVINKIDlvkkEELLPLLAEYSELLDFAE---IVPISALK 152

                         90
                 ....*....|....*
gi 71834861  232 NVNIETCFTALVQML 246
Cdd:COG1159  153 GDNVDELLDEIAKLL 167
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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