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Conserved domains on  [gi|348558014|ref|XP_003464813|]
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rho GTPase-activating protein 5 [Cavia porcellus]

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: 1088.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   556 TCLSGQNCTDIKVEQLLASSLLHLDHSRLRLYHDSSNIDKVNLFILGKDGLAQELANEIRTQST-DDEYALDGKIYELDL 634
Cdd:pfam19518    1 TCPSGPNCVDSKIEQLLASRFPQPYPRRLKSYHDDANIDRINLVILGKDGLARELANEIRALCTnDDKYVLDGKMYELSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   635 RPVDAKSPYILSQLWTAAFKPHGCFCVFNSIESLSFIGEFIGKVRTEASQiRKDKYMANLPFTLILANQR-DSISKNLPI 713
Cdd:pfam19518   81 RPIEGNVRLPVNSFQTPTFKPHGCLCLYNSKESLSYVVESIEKSRESTLG-RRDNHLAHLPLTLILVNKRgDIGGETLQS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   714 LRHQGQQLANKLQCPFVDVPTS--TYPRKFNESQIKQALRGVLESVKHNLDVVSPVPTNKDVLEADLRIIMCAMCGDPFR 791
Cdd:pfam19518  160 LIQQGQQVANKLQCPFLDPASPggGYGRNFNEKQINQVLRGLLESKRHNLNVVSPAPSIKDLSEADLRIVMCLMCGDPFS 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   792 VDLILSPFLDSHSCSAAQAGQNNSLMLDKIIGEKRRRIQITILSYHSSIGVRKDELVHGYILVYSAKRKASMGMLRAFLS 871
Cdd:pfam19518  240 VDLILSPFLQSQHCRPAQPGSGNSVLLELIIGGQRRRIELSILSYHSSFGVRKSRLVHGYILVYSAKRKASMAMLRAFLC 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   872 EVQDTIPVQLVAVTDSQADFFENEAIKELMTEGEHIATEITAKFTALYSLSQYHRQTEVFTLFFSDVLEKKNMIENSYLS 951
Cdd:pfam19518  320 EVQDIIPVQLVAVTDSQADFFESEVSREQLTEGEEIAHEIEAKFTALYCGSGYQHQTEVFTPFFKEVLEKKTIIEASHMY 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   952 DNTRELTHQsEDVFLPSPRDC--FPYNNYPDSDDDTEAPPPYSPIGDDVQLLPtsSDRSKTRLDLEGNEYPVHSTPNCHD 1029
Cdd:pfam19518  400 DNTAEACST-EEEFFSSPRAGspSPNSNLPDSEDDTEPPPPYSPIRDDVQLLP--SDRSKFSLDLEGNDYSVISTPSSFE 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  1030 HERNHkVPPPIKPKPVVPKTNVKKLDPNLLktIEAGIGKNPRKQTSRVPLAHPEDVDSSDnYAEPIDTIFKQKGYSDEIY 1109
Cdd:pfam19518  477 SKLNN-KVPPPVKPKPPVKFDVRKLDPNLY--IDGGNRDGPRSLPSRVTWAPGEGYDPSD-YAEPMDAVVKPRGEEENIY 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  1110 VVPDDS-QNRIIKIRNSFVNTQGDEENGFSDRSSKSHGERR--------PSKYKYKSKTLfSKAKSyYRRTHSDASDDEA 1180
Cdd:pfam19518  553 SVPHDStQGKIITIRNSNKTQSNGEGNGSDSEADSSSLERRkksalgvkPRLYRDRSKRL-GKFSS-YRTSFSVGSDDEL 630

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  1181 FTASII-RKGRHRGSEEDPLLSPVEtwkGGIDNPAITSDQEvddkktkkkphkVKEDKKQKKKTKNFNPPTRRNWESNYF 1259
Cdd:pfam19518  631 GPIRKKkREDDHGGSKGDNLLNPYE---GGIEDPKRRNILR------------SLRRTTKKPKPKPRPSISKPTWESNYF 695


                   ....
gi 348558014  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 2.02e-111

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: 349.45  E-value: 2.02e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFT 1338
Cdd:cd04373     1 FGVPLANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDFTVNAVAGALKSFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1339 DLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMR 1418
Cdd:cd04373    81 ELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR 160

                         170       180
                  ....*....|....*....|....*
gi 348558014 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 4.16e-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: 4.16e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   260 DAYKTQRQLVVTATDKFEKLV-QTVRDYHATWKTVSNKLKNHPDYEEYINLEGTRKARNTFSKHIEQLKQEHIRKRREEY 338
Cdd:pfam16512    1 EAAKVRKELLDSATDAFERLIrSQVTDYRALWKTVSKKLSQHPEYQEYVELFGTDKAKRLFRKHIKKLKDEHIRKRRQGY 80
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 31-246 2.08e-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: 54.84  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   31 GVGKSCLCNRFVRSKADEYY---PEHTSVlSTIDFggrvvnndhflywgditqngeDGVECKIHVI---EQTEFiddqtf 104
Cdd:cd00876     9 GVGKSALTIRFVSGEFVEEYdptIEDSYR-KQIVV---------------------DGETYTLDILdtaGQEEF------ 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  105 lphrSTNLQPYIKraaasklqsaeklmyictdqlgleqdfeqkqmpegklNVDGFLLCIDVsqgCNRK-FDDQLKFVNNL 183
Cdd:cd00876    61 ----SAMRDQYIR-------------------------------------NGDGFILVYSI---TSREsFEEIKNIREQI 96

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348558014  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 ...
 429-473 1.61e-07

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: 49.11  E-value: 1.61e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 348558014    429 EMKEKFKKTLEKIQFISPGQPWEEVICFVMEDEAFKYITEADSKE 473
Cdd:smart00441    2 EAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSESERE 46
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 484-533 2.19e-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: 2.19e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 348558014    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 3.21e-03

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: 37.17  E-value: 3.21e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 348558014    368 MEKRTDFQLCFVVLEK----TPWDETDHIDKIHDRRIpfDLLSTLEAEKVYQNHVQH 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: 1088.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   556 TCLSGQNCTDIKVEQLLASSLLHLDHSRLRLYHDSSNIDKVNLFILGKDGLAQELANEIRTQST-DDEYALDGKIYELDL 634
Cdd:pfam19518    1 TCPSGPNCVDSKIEQLLASRFPQPYPRRLKSYHDDANIDRINLVILGKDGLARELANEIRALCTnDDKYVLDGKMYELSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   635 RPVDAKSPYILSQLWTAAFKPHGCFCVFNSIESLSFIGEFIGKVRTEASQiRKDKYMANLPFTLILANQR-DSISKNLPI 713
Cdd:pfam19518   81 RPIEGNVRLPVNSFQTPTFKPHGCLCLYNSKESLSYVVESIEKSRESTLG-RRDNHLAHLPLTLILVNKRgDIGGETLQS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   714 LRHQGQQLANKLQCPFVDVPTS--TYPRKFNESQIKQALRGVLESVKHNLDVVSPVPTNKDVLEADLRIIMCAMCGDPFR 791
Cdd:pfam19518  160 LIQQGQQVANKLQCPFLDPASPggGYGRNFNEKQINQVLRGLLESKRHNLNVVSPAPSIKDLSEADLRIVMCLMCGDPFS 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   792 VDLILSPFLDSHSCSAAQAGQNNSLMLDKIIGEKRRRIQITILSYHSSIGVRKDELVHGYILVYSAKRKASMGMLRAFLS 871
Cdd:pfam19518  240 VDLILSPFLQSQHCRPAQPGSGNSVLLELIIGGQRRRIELSILSYHSSFGVRKSRLVHGYILVYSAKRKASMAMLRAFLC 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   872 EVQDTIPVQLVAVTDSQADFFENEAIKELMTEGEHIATEITAKFTALYSLSQYHRQTEVFTLFFSDVLEKKNMIENSYLS 951
Cdd:pfam19518  320 EVQDIIPVQLVAVTDSQADFFESEVSREQLTEGEEIAHEIEAKFTALYCGSGYQHQTEVFTPFFKEVLEKKTIIEASHMY 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   952 DNTRELTHQsEDVFLPSPRDC--FPYNNYPDSDDDTEAPPPYSPIGDDVQLLPtsSDRSKTRLDLEGNEYPVHSTPNCHD 1029
Cdd:pfam19518  400 DNTAEACST-EEEFFSSPRAGspSPNSNLPDSEDDTEPPPPYSPIRDDVQLLP--SDRSKFSLDLEGNDYSVISTPSSFE 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  1030 HERNHkVPPPIKPKPVVPKTNVKKLDPNLLktIEAGIGKNPRKQTSRVPLAHPEDVDSSDnYAEPIDTIFKQKGYSDEIY 1109
Cdd:pfam19518  477 SKLNN-KVPPPVKPKPPVKFDVRKLDPNLY--IDGGNRDGPRSLPSRVTWAPGEGYDPSD-YAEPMDAVVKPRGEEENIY 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  1110 VVPDDS-QNRIIKIRNSFVNTQGDEENGFSDRSSKSHGERR--------PSKYKYKSKTLfSKAKSyYRRTHSDASDDEA 1180
Cdd:pfam19518  553 SVPHDStQGKIITIRNSNKTQSNGEGNGSDSEADSSSLERRkksalgvkPRLYRDRSKRL-GKFSS-YRTSFSVGSDDEL 630

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  1181 FTASII-RKGRHRGSEEDPLLSPVEtwkGGIDNPAITSDQEvddkktkkkphkVKEDKKQKKKTKNFNPPTRRNWESNYF 1259
Cdd:pfam19518  631 GPIRKKkREDDHGGSKGDNLLNPYE---GGIEDPKRRNILR------------SLRRTTKKPKPKPRPSISKPTWESNYF 695


                   ....
gi 348558014  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 2.66e-118

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: 367.64  E-value: 2.66e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  592 NIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDAKSPYILSQLWTAAFKPHGCFCVFNSIESLSFI 671
Cdd:cd22220     1 NIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDANSPYLLSQLWTSAFKPHGCFCVFNSIESLNFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  672 GEFIGKVRTEASQIRKDKYMANLPFTLILANQRDSISKNLPILRHQGQQLANKLQCPFVDVPTSTYPRKFNESQIKQALR 751
Cdd:cd22220    81 GECIGKIRAEASQIRRDRYIANLPFTLILANQRDSVSKNLPILRHQGQQLANKLQCPFVDVPAGTYPRKFNETQIKQALR 160

                         170
                  ....*....|.
gi 348558014  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 2.02e-111

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: 349.45  E-value: 2.02e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFT 1338
Cdd:cd04373     1 FGVPLANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDFTVNAVAGALKSFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1339 DLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMR 1418
Cdd:cd04373    81 ELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR 160

                         170       180
                  ....*....|....*....|....*
gi 348558014 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 1.08e-65

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: 219.83  E-value: 1.08e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   1271 KPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFTDLPDPLIPYSLH 1350
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   1351 PELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMRPDFENREFLSTT 1430
Cdd:smart00324   81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160

                           170
                    ....*....|....
gi 348558014   1431 KIHQSVVETFIQQC 1444
Cdd:smart00324  161 RHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 1274-1420 1.25e-58

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 198.54  E-value: 1.25e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  1274 PLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFTDLPDPLIPYSLHPEL 1353
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 348558014  1354 LEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMRPD 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 4.16e-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: 4.16e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   260 DAYKTQRQLVVTATDKFEKLV-QTVRDYHATWKTVSNKLKNHPDYEEYINLEGTRKARNTFSKHIEQLKQEHIRKRREEY 338
Cdd:pfam16512    1 EAAKVRKELLDSATDAFERLIrSQVTDYRALWKTVSKKLSQHPEYQEYVELFGTDKAKRLFRKHIKKLKDEHIRKRRQGY 80
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
 31-246 2.08e-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: 54.84  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   31 GVGKSCLCNRFVRSKADEYY---PEHTSVlSTIDFggrvvnndhflywgditqngeDGVECKIHVI---EQTEFiddqtf 104
Cdd:cd00876     9 GVGKSALTIRFVSGEFVEEYdptIEDSYR-KQIVV---------------------DGETYTLDILdtaGQEEF------ 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  105 lphrSTNLQPYIKraaasklqsaeklmyictdqlgleqdfeqkqmpegklNVDGFLLCIDVsqgCNRK-FDDQLKFVNNL 183
Cdd:cd00876    61 ----SAMRDQYIR-------------------------------------NGDGFILVYSI---TSREsFEEIKNIREQI 96

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348558014  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 ...
 429-473 1.61e-07

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: 49.11  E-value: 1.61e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 348558014    429 EMKEKFKKTLEKIQFISPGQPWEEVICFVMEDEAFKYITEADSKE 473
Cdd:smart00441    2 EAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSESERE 46
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 28-244 4.09e-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: 51.36  E-value: 4.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014    28 GNCGVGKSCLCNRFVRSKADEYYpehtsvLSTIdfggrvvnndhflywgditqngedGVECKIHVIEqtefIDDQTflph 107
Cdd:pfam00071    6 GDGGVGKSSLLIRFTQNKFPEEY------IPTI------------------------GVDFYTKTIE----VDGKT---- 47

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   108 rstnlqpyikraaaSKLQsaeklmyIcTDQLGLEqDFE---QKQMPegklNVDGFLLCIDVSqgcNRK-FDDQLKFVNNL 183
Cdd:pfam00071   48 --------------VKLQ-------I-WDTAGQE-RFRalrPLYYR----GADGFLLVYDIT---SRDsFENVKKWVEEI 97

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 348558014   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 3.08e-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: 3.08e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 348558014    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 1.02e-05

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 47.12  E-value: 1.02e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014     28 GNCGVGKSCLCNRFVRskaDEYYPEHTSvlsTIdfggrvvnndhflywgditqngedGVECKIHVIEqtefIDDQTFlph 107
Cdd:smart00175    7 GDSGVGKSSLLSRFTD---GKFSEQYKS---TI------------------------GVDFKTKTIE----VDGKRV--- 49

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014    108 rstnlqpyikraaasKLQsaeklmyICtDQLGLE------QDFEQkqmpegklNVDGFLLCIDVSqgcNRK-FDDQLKFV 180
Cdd:smart00175   50 ---------------KLQ-------IW-DTAGQErfrsitSSYYR--------GAVGALLVYDIT---NREsFENLENWL 95

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 348558014    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 2.19e-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: 2.19e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 348558014    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 4.25e-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: 42.44  E-value: 4.25e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 348558014   485 KAKEEFQEMLFEHselfydldlNATPSSdKMSEIHTVLSEEPRYKALQKLApDRESLLLKH 545
Cdd:pfam01846    1 KAREAFKELLKEH---------KITPYS-TWSEIKKKIENDPRYKALLDGS-EREELFEDY 50
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
28-246 7.96e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 41.89  E-value: 7.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   28 GNCGVGKSCLCNRFVRSK--ADEYYPEHTSVLSTIDFggRVvnndhflywgditqngeDGVECKIHVIE---QTEFIDDQ 102
Cdd:COG1100    10 GTGGVGKTSLVNRLVGDIfsLEKYLSTNGVTIDKKEL--KL-----------------DGLDVDLVIWDtpgQDEFRETR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  103 TFLphrstnlqpyikraaASKLQSAeklmyictdqlgleqdfeqkqmpegklnvDGFLLCIDVSQGCNRKfddQLKFVNN 182
Cdd:COG1100    71 QFY---------------ARQLTGA-----------------------------SLYLFVVDGTREETLQ---SLYELLE 103

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 348558014  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 3.21e-03

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: 37.17  E-value: 3.21e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 348558014    368 MEKRTDFQLCFVVLEK----TPWDETDHIDKIHDRRIpfDLLSTLEAEKVYQNHVQH 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: 1088.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   556 TCLSGQNCTDIKVEQLLASSLLHLDHSRLRLYHDSSNIDKVNLFILGKDGLAQELANEIRTQST-DDEYALDGKIYELDL 634
Cdd:pfam19518    1 TCPSGPNCVDSKIEQLLASRFPQPYPRRLKSYHDDANIDRINLVILGKDGLARELANEIRALCTnDDKYVLDGKMYELSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   635 RPVDAKSPYILSQLWTAAFKPHGCFCVFNSIESLSFIGEFIGKVRTEASQiRKDKYMANLPFTLILANQR-DSISKNLPI 713
Cdd:pfam19518   81 RPIEGNVRLPVNSFQTPTFKPHGCLCLYNSKESLSYVVESIEKSRESTLG-RRDNHLAHLPLTLILVNKRgDIGGETLQS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   714 LRHQGQQLANKLQCPFVDVPTS--TYPRKFNESQIKQALRGVLESVKHNLDVVSPVPTNKDVLEADLRIIMCAMCGDPFR 791
Cdd:pfam19518  160 LIQQGQQVANKLQCPFLDPASPggGYGRNFNEKQINQVLRGLLESKRHNLNVVSPAPSIKDLSEADLRIVMCLMCGDPFS 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   792 VDLILSPFLDSHSCSAAQAGQNNSLMLDKIIGEKRRRIQITILSYHSSIGVRKDELVHGYILVYSAKRKASMGMLRAFLS 871
Cdd:pfam19518  240 VDLILSPFLQSQHCRPAQPGSGNSVLLELIIGGQRRRIELSILSYHSSFGVRKSRLVHGYILVYSAKRKASMAMLRAFLC 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   872 EVQDTIPVQLVAVTDSQADFFENEAIKELMTEGEHIATEITAKFTALYSLSQYHRQTEVFTLFFSDVLEKKNMIENSYLS 951
Cdd:pfam19518  320 EVQDIIPVQLVAVTDSQADFFESEVSREQLTEGEEIAHEIEAKFTALYCGSGYQHQTEVFTPFFKEVLEKKTIIEASHMY 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   952 DNTRELTHQsEDVFLPSPRDC--FPYNNYPDSDDDTEAPPPYSPIGDDVQLLPtsSDRSKTRLDLEGNEYPVHSTPNCHD 1029
Cdd:pfam19518  400 DNTAEACST-EEEFFSSPRAGspSPNSNLPDSEDDTEPPPPYSPIRDDVQLLP--SDRSKFSLDLEGNDYSVISTPSSFE 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  1030 HERNHkVPPPIKPKPVVPKTNVKKLDPNLLktIEAGIGKNPRKQTSRVPLAHPEDVDSSDnYAEPIDTIFKQKGYSDEIY 1109
Cdd:pfam19518  477 SKLNN-KVPPPVKPKPPVKFDVRKLDPNLY--IDGGNRDGPRSLPSRVTWAPGEGYDPSD-YAEPMDAVVKPRGEEENIY 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  1110 VVPDDS-QNRIIKIRNSFVNTQGDEENGFSDRSSKSHGERR--------PSKYKYKSKTLfSKAKSyYRRTHSDASDDEA 1180
Cdd:pfam19518  553 SVPHDStQGKIITIRNSNKTQSNGEGNGSDSEADSSSLERRkksalgvkPRLYRDRSKRL-GKFSS-YRTSFSVGSDDEL 630

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  1181 FTASII-RKGRHRGSEEDPLLSPVEtwkGGIDNPAITSDQEvddkktkkkphkVKEDKKQKKKTKNFNPPTRRNWESNYF 1259
Cdd:pfam19518  631 GPIRKKkREDDHGGSKGDNLLNPYE---GGIEDPKRRNILR------------SLRRTTKKPKPKPRPSISKPTWESNYF 695


                   ....
gi 348558014  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 2.66e-118

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: 367.64  E-value: 2.66e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  592 NIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDAKSPYILSQLWTAAFKPHGCFCVFNSIESLSFI 671
Cdd:cd22220     1 NIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDANSPYLLSQLWTSAFKPHGCFCVFNSIESLNFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  672 GEFIGKVRTEASQIRKDKYMANLPFTLILANQRDSISKNLPILRHQGQQLANKLQCPFVDVPTSTYPRKFNESQIKQALR 751
Cdd:cd22220    81 GECIGKIRAEASQIRRDRYIANLPFTLILANQRDSVSKNLPILRHQGQQLANKLQCPFVDVPAGTYPRKFNETQIKQALR 160

                         170
                  ....*....|.
gi 348558014  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 2.02e-111

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: 349.45  E-value: 2.02e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFT 1338
Cdd:cd04373     1 FGVPLANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNLDLVSKDFTVNAVAGALKSFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1339 DLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMR 1418
Cdd:cd04373    81 ELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR 160

                         170       180
                  ....*....|....*....|....*
gi 348558014 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 1.08e-65

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: 219.83  E-value: 1.08e-65
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   1271 KPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFTDLPDPLIPYSLH 1350
Cdd:smart00324    1 KPIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLDLSEYDVHDVAGLLKLFLRELPEPLITYELY 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   1351 PELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMRPDFENREFLSTT 1430
Cdd:smart00324   81 EEFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKDI 160

                           170
                    ....*....|....
gi 348558014   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 1.20e-62

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: 210.97  E-value: 1.20e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  596 VNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDAKSPYILSQLWTAAFKPHGCFCVFNSIESLSFIGEFI 675
Cdd:cd22207     1 LNLVLLGSDGLADELANEIRALCEDDEYELDGVVYSLDLRTIDGDVSLPQNSFQTTDFKPHGCLCVYSSRESLEYIKTSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  676 GKVRTEASQIRKDKYMANLPFTLILANQRDSISKNLPILRHQGQQLANKLQCPFVDVPTSTYP--RKFNESQIKQALRGV 753
Cdd:cd22207    81 EKTLLSDLEEEDKLPFQGLPIVLLFARDPSISEKEVSQLREEGQELADRLQCVFIDVPSSGEAmgRKFHESQIDDALRSL 160


                  ....*.
gi 348558014  754 LESVKH 759
Cdd:cd22207   161 IESIKH 166
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 1274-1420 1.25e-58

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 198.54  E-value: 1.25e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  1274 PLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFFTDLPDPLIPYSLHPEL 1353
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 348558014  1354 LEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMRPD 1420
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147
pseudoGTPaseD_p190RhoGAP-A cd22221
pseudoGTPase domain found in p190RhoGAP-A and similar proteins; p190RhoGAP protein A ...
 592-760 2.64e-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: 190.08  E-value: 2.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  592 NIDKVNLFILGKDGLAQELANEIRTQST-DDEYALDGKIYELDLRPVDAKSPYILSQLWTAAFKPHGCFCVFNSIESLSF 670
Cdd:cd22221     1 NVDRINLVILGKDGLARELANEIRALCTnDDKYVLDGKMYELSLRPIEGNVRLPVNSFQTPTFQPHGCLCLYNSKESLSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  671 IGEFIGKVRtEASQIRKDKYMANLPFTLILANQR-DSISKNLPILRHQGQQLANKLQCPFVDvPTST---YPRKFNESQI 746
Cdd:cd22221    81 VVESIEKSR-ESTLGRRDNHLAHLPLTLILVNKRgDTSGETLQSLIQQGQQVASKLQCVFLD-PASTgigYGRNINEKQI 158

                         170
                  ....*....|....
gi 348558014  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 7.52e-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: 185.58  E-value: 7.52e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1274 PLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSmEVTVNAVAGALKAFFTDLPDPLIPYSLHPEL 1353
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLE-DYDVHDVASLLKLYLRELPEPLIPFELYDEF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1354 LEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMRPDFENREFLSTTKIH 1433
Cdd:cd00159    80 IELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELLEDIKKL 159


                  ....*....
gi 348558014 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 1.57e-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: 159.99  E-value: 1.57e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAEK-PIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEV--TVNAVAGALKA 1335
Cdd:cd04372     1 YGCDLTTLVKAHNtQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADISATVypDINVITGALKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1336 FFTDLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPT 1415
Cdd:cd04372    81 YFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPT 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 348558014 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 1.14e-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: 151.78  E-value: 1.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTA--EKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQfdqdhnINLVSMEVT--------VNA 1328
Cdd:cd04395     2 FGVPLDDCPPSseNPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEE------LNRGGFDIDlqdprwrdVNV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1329 VAGALKAFFTDLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNL 1408
Cdd:cd04395    76 VSSLLKSFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 348558014 1409 SICFWPTLMRPDFENREFLSTTKIHQ-SVVETFIQQCQFFF 1448
Cdd:cd04395   156 AIVFGPTLVRTSDDNMETMVTHMPDQcKIVETLIQHYDWFF 196
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1448 1.88e-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: 148.32  E-value: 1.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAEKP-IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQD-HNINLVSMEVT---VNAVAGAL 1333
Cdd:cd04398     1 FGVPLEDLILREGDnVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDpLNVLLISPEDYesdIHSVASLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1334 KAFFTDLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFW 1413
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 348558014 1414 PTLMRPDFENREFLSttkiHQS-VVETFIQQCQFFF 1448
Cdd:cd04398   161 PTLMNAAPDNAADMS----FQSrVIETLLDNAYQIF 192
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1259-1443 3.47e-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: 147.15  E-value: 3.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAEKP-IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTdqdNIQK---QFDQDHNINL-VSMEVTVNAVAGAL 1333
Cdd:cd04403     1 FGCHLEALCQRENStVPKFVRLCIEAVEKRGLDVDGIYRVSGNLA---VIQKlrfAVDHDEKLDLdDSKWEDIHVITGAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1334 KAFFTDLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFW 1413
Cdd:cd04403    78 KLFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFG 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 348558014 1414 PTLMRPDFENREfLSTTKIHQS-VVETFIQQ 1443
Cdd:cd04403   158 PTLLRPEQETGN-IAVHMVYQNqIVELILLE 187
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 1273-1420 3.88e-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: 147.07  E-value: 3.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1273 IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQD-HNINLVSMEVTVNAVAGALKAFFTDLPDPLIPYSLHP 1351
Cdd:cd04385    15 IPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDaRSVQLREGEYTVHDVADVLKRFLRDLPDPLLTSELHA 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 348558014 1352 ELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMRPD 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 4.16e-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: 4.16e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   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 3.42e-34

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: 130.65  E-value: 3.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQD-LVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDH-NINLVSMEVTVNAVAGALKAF 1336
Cdd:cd04386     5 FGTPLEEhLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTfSLPLDEFYSDPHAVASALKSY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1337 FTDLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTL 1416
Cdd:cd04386    85 LRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAPNL 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 348558014 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 7.07e-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: 123.32  E-value: 7.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQD-HNINLvsMEVTVNAVAGALKAFF 1337
Cdd:cd04377     1 FGVSLSSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDpDSVNL--EDYPIHVITSVLKQWL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1338 TDLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLM 1417
Cdd:cd04377    79 RELPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCIL 158


                  ....
gi 348558014 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 1.69e-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: 122.89  E-value: 1.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1276 FVEKCVEFIEDTGLCTEGLYRVSGNKTdqdNIQKQ----FDQ----DHNINLVSMEVTVNAVAGALKAFFTDLPDPLIPY 1347
Cdd:cd04374    31 FVRKCIEAVETRGINEQGLYRVVGVNS---KVQKLlslgLDPktstPGDVDLDNSEWEIKTITSALKTYLRNLPEPLMTY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1348 SLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMRPDFENREFL 1427
Cdd:cd04374   108 ELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEETVAAI 187

                         170
                  ....*....|....*
gi 348558014 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 2.20e-30

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: 119.32  E-value: 2.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1263 LQDLVTAEKP-IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSmEVTVNAVAGALKAFFTDLP 1341
Cdd:cd04382     6 LADFDPSTSPmIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLS-KVDIHVICGCLKDFLRSLK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1342 DPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSqQNKINLMTADNLSICFWPTLM---R 1418
Cdd:cd04382    85 EPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVA-QSPECKMDINNLARVFGPTIVgysV 163

                         170       180
                  ....*....|....*....|
gi 348558014 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 9.69e-29

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: 114.74  E-value: 9.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVT---AEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLvSMEVTVNAVAGALKA 1335
Cdd:cd04404     6 FGVSLQFLKEknpEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEPVDF-DQYEDVHLPAVILKT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1336 FFTDLPDPLIPYSLHPELLEAAKiLDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPT 1415
Cdd:cd04404    85 FLRELPEPLLTFDLYDDIVGFLN-VDKEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGPN 163


                  ....
gi 348558014 1416 LMRP 1419
Cdd:cd04404   164 LLWA 167
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1273-1419 4.83e-28

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: 112.90  E-value: 4.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1273 IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDqdHNINLVSM-EVTVNAVAGALKAFFTDLPDPLIPYSLHP 1351
Cdd:cd04378    16 VPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFE--NGKDLVELsELSPHDISSVLKLFLRQLPEPLILFRLYN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1352 ELLEAAK-ILDKTER-------------LHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLM 1417
Cdd:cd04378    94 DFIALAKeIQRDTEEdkapntpievnriIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTLI 173


                  ..
gi 348558014 1418 RP 1419
Cdd:cd04378   174 RP 175
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 1273-1449 2.23e-27

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: 110.79  E-value: 2.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1273 IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSM-EVTVNAVAGALKAFFTDLPDPLIPYSLHP 1351
Cdd:cd04387    16 VPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVMLsEMDVNAIAGTLKLYFRELPEPLFTDELYP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1352 ELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMRPDfENREFLSTTK 1431
Cdd:cd04387    96 NFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPS-EKESKIPTNT 174

                         170
                  ....*....|....*...
gi 348558014 1432 IHQSVVETFIQQCQFFFY 1449
Cdd:cd04387   175 MTDSWSLEVMSQVQVLLY 192
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1259-1423 9.76e-27

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: 109.07  E-value: 9.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAEKP-----IPLFVEKCVEFIEDTGLCTEGLYRVSGnktdQDNIQKQFDQDHNIN---LVSMEVTVNAVA 1330
Cdd:cd04390     3 FGQRLEDTVAYERKfgprlVPILVEQCVDFIREHGLKEEGLFRLPG----QANLVKQLQDAFDAGerpSFDSDTDVHTVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1331 GALKAFFTDLPDPLIPYSLHPELLEAAKILDKTER--LHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNL 1408
Cdd:cd04390    79 SLLKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEkgLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNL 158

                         170
                  ....*....|....*
gi 348558014 1409 SICFWPTLMRPDFEN 1423
Cdd:cd04390   159 ATVFGPNILRPKVED 173
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1259-1416 1.37e-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: 108.29  E-value: 1.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAEK-----PIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVnaVAGAL 1333
Cdd:cd04381     1 FGASLSLAVERSRchdgiDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLEEYEPPT--VASLL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1334 KAFFTDLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFW 1413
Cdd:cd04381    79 KQYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLS 158


                  ...
gi 348558014 1414 PTL 1416
Cdd:cd04381   159 PTV 161
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1271-1420 2.83e-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: 107.51  E-value: 2.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1271 KPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHN-INLVSMEVTVNAVAGALKAFFTDLPDPLIPYSL 1349
Cdd:cd04383    16 QAIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDpLADDQNDHDINSVAGVLKLYFRGLENPLFPKER 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348558014 1350 HPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMR-PD 1420
Cdd:cd04383    96 FEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLMPvPE 167
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1438 3.02e-26

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: 107.55  E-value: 3.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAEKP---IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLvSMEVTVNAVAGALKA 1335
Cdd:cd04393     3 FGVPLQELQQAGQPengVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDL-SKEADVCSAASLLRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1336 FFTDLPDPLIPYSLHPELLEA-AKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWP 1414
Cdd:cd04393    82 FLQELPEGLIPASLQIRLMQLyQDYNGEDEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAVFGP 161

                         170       180
                  ....*....|....*....|....*..
gi 348558014 1415 TL--MRPDFEN-REFLSTTKIHQSVVE 1438
Cdd:cd04393   162 DVfhVYTDVEDmKEQEICSRIMAKLLE 188
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1447 5.65e-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: 106.82  E-value: 5.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQD-LVTAEKPIPLFVEKCVEFIEDTGLCTeGLYRVSGNktdQDNIQK---QFDQDHNINLVS--MEVTVNAVAGA 1332
Cdd:cd04384     3 FGCDLTEhLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGI---ASNIQRlrhEFDSEQIPDLTKdvYIQDIHSVSSL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1333 LKAFFTDLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICF 1412
Cdd:cd04384    79 CKLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVW 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 348558014 1413 WPTLMR-PDFENREFLSTTKIHQSVVETFIQQCQFF 1447
Cdd:cd04384   159 APNLLRsKQIESACFSGTAAFMEVRIQSVVVEFILN 194
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 1259-1427 5.95e-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: 106.67  E-value: 5.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVT------AEKPIPLFVEKCVEFIEDTG-LCTEGLYRVSGNKTDQDNIQKQFDQDHNINLV--SMEVTVNAV 1329
Cdd:cd04400     2 FGSPLEEAVElsshkyNGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTEYDVDLFssSLYPDVHTV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1330 AGALKAFFTDLPDPLIPYSLHPELLEAAKIL-DKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNL 1408
Cdd:cd04400    82 AGLLKLYLRELPTLILGGELHNDFKRLVEENhDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRNV 161

                         170
                  ....*....|....*....
gi 348558014 1409 SICFWPTLMRPDFENREFL 1427
Cdd:cd04400   162 CIVFSPTLNIPAGIFVLFL 180
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1259-1420 1.10e-25

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: 105.84  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNiNLVSMEVTVNAVAGALKAFFT 1338
Cdd:cd04407     1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPE-NVKLENYPIHAITGLLKQWLR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1339 DLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMR 1418
Cdd:cd04407    80 ELPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLR 159


                  ...
gi 348558014 1419 -PD 1420
Cdd:cd04407   160 cPD 162
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 1273-1419 1.93e-23

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: 99.51  E-value: 1.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1273 IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSmEVTVNAVAGALKAFFTDLPDPLIPYSLHPE 1352
Cdd:cd04408    16 VPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLS-GHSPHDITSVLKHFLKELPEPVLPFQLYDD 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 348558014 1353 LLEAAKILDK------------TERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMRP 1419
Cdd:cd04408    95 FIALAKELQRdsekaaespsivENIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLLRP 173
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1259-1420 3.56e-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: 98.53  E-value: 3.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQD-HNINLVSMEVTVnaVAGALKAFF 1337
Cdd:cd04406     1 FGVELSRLTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDaNSVNLDDYNIHV--IASVFKQWL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1338 TDLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLM 1417
Cdd:cd04406    79 RDLPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCIL 158


                  ....
gi 348558014 1418 R-PD 1420
Cdd:cd04406   159 RcPD 162
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1273-1419 6.64e-23

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: 98.34  E-value: 6.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1273 IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSmEVTVNAVAGALKAFFTDLPDPLIPYSLHPE 1352
Cdd:cd04409    16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELS-ELSPHDISNVLKLYLRQLPEPLILFRLYNE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1353 LLEAAKIL------DKTERLHA----------------LKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSI 1410
Cdd:cd04409    95 FIGLAKESqhvnetQEAKKNSDkkwpnmctelnrillkSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNLGI 174


                  ....*....
gi 348558014 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 1.73e-21

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: 94.08  E-value: 1.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDL----VTAEKPIPLFVEKCVEFIEDTgLCTEGLYRVSGNKTDQDNIQKQFDQDHNinlvsmeVTVNA----VA 1330
Cdd:cd04394     2 FGVPLHSLphstVPEYGNVPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEA-------CLSSAlpcdVA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1331 GALKAFFTDLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSI 1410
Cdd:cd04394    74 GLLKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAV 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 348558014 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 6.26e-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: 92.53  E-value: 6.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAE---KPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVT--VNAVAGAL 1333
Cdd:cd04379     1 FGVPLSRLVEREgesRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELSEELYpdINVITGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1334 KAFFTDLPDPLIPYSLHPELLEAAKIL---DKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSI 1410
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLEALAVAlpnDVQTNTHLTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160


                  ....*....
gi 348558014 1411 CFWPTLMRP 1419
Cdd:cd04379   161 CFGPVLMFC 169
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1265-1448 6.51e-20

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: 89.81  E-value: 6.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1265 DLVTAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSmEVTVNAVAGALKAFFTDLPDPL 1344
Cdd:cd04376     1 SLNPIARQVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDE-NHSVHDVAALLKEFFRDMPDPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1345 IPYSLHPELLEAAKiLDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQ--QNKI---------NLMTADNLSICFW 1413
Cdd:cd04376    80 LPRELYTAFIGTAL-LEPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEhaADSIdedgqevsgNKMTSLNLATIFG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 348558014 1414 PTLMRPD-FENREFLSTT-----KIHQ-SVVETFIQQCQFFF 1448
Cdd:cd04376   159 PNLLHKQkSGEREFVQASlrieeSTAIiNVVQTMIDNYEELF 200
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1416 5.35e-18

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: 84.32  E-value: 5.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLV------TAEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSME-VTVNAVAG 1331
Cdd:cd04391     2 FGVPLSTLLerdqkkVPGSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKFYEGTFLWDqVKQHDAAS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1332 ALKAFFTDLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSIC 1411
Cdd:cd04391    82 LLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAMI 161


                  ....*
gi 348558014 1412 FWPTL 1416
Cdd:cd04391   162 MAPNL 166
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1448 1.94e-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: 81.96  E-value: 1.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVTAEKPiPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVnaVAGALKAFFT 1338
Cdd:cd04402     2 FGQPLSNICEDDNL-PKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVEVDLKAEPVLL--LASVLKDFLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1339 DLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMR 1418
Cdd:cd04402    79 NIPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLW 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 348558014 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 3.30e-16

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: 79.04  E-value: 3.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPL-QDLVTAEKPIPLFVEKcvefiedtGLCTEGLYRVSGNKTDQDNIQKQFDQDHNINLVSMEVTVNAVAGALKAFF 1337
Cdd:cd04392     1 FGAPLtEEGIAQIYQLIEYLEK--------NLRVEGLFRKPGNSARQQELRDLLNSGTDLDLESGGFHAHDCATVLKGFL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1338 TDLPDPLIPYSLHPELLEAAKIL------------DKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTA 1405
Cdd:cd04392    73 GELPEPLLTHAHYPAHLQIADLCqfdekgnktsapDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSA 152

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 348558014 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 8.02e-16

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


Pssm-ID: 239861  Cd Length: 225  Bit Score: 78.22  E-value: 8.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1273 IPLFVEKCVEFIEDTGLCTEGLYRVSGNKTDQDNIQKQFDQ--DHNINLVSMEVTVNAVAGALKAFFTDLPDPLIPYSLH 1350
Cdd:cd04396    32 IPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTppDYGKSFDWDGYTVHDAASVLRRYLNNLPEPLVPLDLY 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1351 PE----LLEAAKIL-------------DKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFW 1413
Cdd:cd04396   112 EEfrnpLRKRPRILqymkgrineplntDIDQAIKEYRDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIFQ 191

                         170       180       190
                  ....*....|....*....|....*....|..
gi 348558014 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 1.33e-14

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: 74.76  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1257 NYFGMPLqdLVTAEK---PIPLFVEKCVEFIEDTGLCTEGLYRVSGNKTdqdNIQK--QFDQDHNINLVSMEVTVNAVAG 1331
Cdd:cd04375     3 NVFGVPL--LVNLQRtgqPLPRSIQQAMRWLRNNALDQVGLFRKSGVKS---RIQKlrSMIESSTDNVNYDGQQAYDVAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1332 ALKAFFTDLPDPLIPYSLHPELLEAAKILDKTERLHALKEIVKKFHPVNYDVLRYVITHLNRVSQQNKINLMTADNLSIC 1411
Cdd:cd04375    78 MLKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVC 157

                         170       180
                  ....*....|....*....|....*
gi 348558014 1412 FWPTLMRPDFENREFLSTTKIHQSV 1436
Cdd:cd04375   158 LAPSLFHLNTSRRENSSPARRMQRK 182
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 1274-1468 2.08e-13

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: 70.67  E-value: 2.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1274 PLFVeKCVEFIEDTGLCTEGLYR--VSGNKTDQdniqKQFDQDHNINLVSMEVTVNAVAGALKAFFTDLPDPLIPYSLHP 1351
Cdd:cd04388    17 PLLI-KLVEAIEKKGLESSTLYRtqSSSSLTEL----RQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1352 ELLEAAKILDKT-ERLHALKEIVKKFH-PVNYDV-LRYVITHLNRVSQQNKINLMTADNLSICFWPTLMR---PDFENRE 1425
Cdd:cd04388    92 EMISRAQEVQSSdEYAQLLRKLIRSPNlPHQYWLtLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRfqpASSDSPE 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 348558014 1426 FlsttkiHQSVVETFIQQcqfffyngeivETANTVAPP--PPSNP 1468
Cdd:cd04388   172 F------HIRIIEVLITS-----------EWNERQAAPalPPKPP 199
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1291-1443 1.46e-11

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: 64.72  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1291 TEGLYRVSGNKTDQDNIQKQFDQDHnINLVSMEvTVNAVAGALKAFFTDLPDPLIPYSLHPELLEAAKILDKTerlhalK 1370
Cdd:cd04389    40 TEGIFRVPGDIDEVNELKLRVDQWD-YPLSGLE-DPHVPASLLKLWLRELEEPLIPDALYQQCISASEDPDKA------V 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 348558014 1371 EIVKKFHPVNYDVLRYVITHLNRVSQQNKI--NLMTADNLSICFWPTLMRPDFEN-REFLSTTKIHQSVVETFIQQ 1443
Cdd:cd04389   112 EIVQKLPIINRLVLCYLINFLQVFAQPENVahTKMDVSNLAMVFAPNILRCTSDDpRVIFENTRKEMSFLRTLIEH 187
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
 31-246 2.08e-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: 54.84  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   31 GVGKSCLCNRFVRSKADEYY---PEHTSVlSTIDFggrvvnndhflywgditqngeDGVECKIHVI---EQTEFiddqtf 104
Cdd:cd00876     9 GVGKSALTIRFVSGEFVEEYdptIEDSYR-KQIVV---------------------DGETYTLDILdtaGQEEF------ 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  105 lphrSTNLQPYIKraaasklqsaeklmyictdqlgleqdfeqkqmpegklNVDGFLLCIDVsqgCNRK-FDDQLKFVNNL 183
Cdd:cd00876    61 ----SAMRDQYIR-------------------------------------NGDGFILVYSI---TSREsFEEIKNIREQI 96

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 348558014  184 FVQLSKSKKPVIIAATKCDEcvDHYlREV-----QAFAsNKKNLLVVETSARFNVNIETCFTALVQML 246
Cdd:cd00876    97 LRVKDKEDVPIVLVGNKCDL--ENE-RQVsteegEALA-EEWGCPFLETSAKTNINIDELFNTLVREI 160
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1259-1441 3.84e-08

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: 55.45  E-value: 3.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1259 FGMPLQDLVT------------AEKPIPLFVEKCVEFIEDTGLCTEGLYRVSGN----KTDQDNIQKQFDQDHNINlvsm 1322
Cdd:cd04397     1 FGVPLEILVEkfgadstlgvgpGKLRIPALIDDIISAMRQMDMSVEGVFRKNGNirrlKELTEEIDKNPTEVPDLS---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1323 EVTVNAVAGALKAFFTDLPDPLIPYSLHPELLEAAKILDKTER---LHALKEIVKKFHpvnYDVLRYVITHLNRVSQQNK 1399
Cdd:cd04397    77 KENPVQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERkrvLHLVYCLLPKYH---RDTMEVLFSFLKWVSSFSH 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 348558014 1400 I-----NLMTADNLSICFWPTLMRPDFENREFLSTTKIHQSVVETFI 1441
Cdd:cd04397   154 IdeetgSKMDIHNLATVITPNILYSKTDNPNTGDEYFLAIEAVNYLI 200
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1249-1441 4.57e-08

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: 55.42  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1249 PTRRNWESNYFGMPLQDLVTAEKPI-------------------PLFVEK----CVEFIEDTGLCTEGLYRvsgNKTDQD 1305
Cdd:cd04380     3 TVTGVYLPSCFGSSLETLIRLPDPGirnlidqlelgdnpdysevPLSIPKeiwrLVDYLYTRGLAQEGLFE---EPGLPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1306 NIQKQF---------DQDHNINLvsmevTVNAVAGALKAFFTDLPDPLIPYSLHPELLEAAKiLDKTERLHALKEIVKkf 1376
Cdd:cd04380    80 EPGELLaeirdaldtGSPFNSPG-----SAESVAEALLLFLESLPDPIIPYSLYERLLEAVA-NNEEDKRQVIRISLP-- 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 348558014 1377 hPVNYDVLRYVITHLNRVSQQNKINLMTADNLSICFWPTLMRPDFENREFLSTTKIHQ--SVVETFI 1441
Cdd:cd04380   152 -PVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRAGGKERRAERDRkrAFIEQFL 217
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
 28-244 5.45e-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: 53.61  E-value: 5.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   28 GNCGVGKSCLCNRFVRSKADEYYPehtsvlSTIdfggrvvnndhflywgditqngedGVECKIHVIEqtefIDDQTFlph 107
Cdd:cd00154     7 GDSGVGKTSLLLRFVDNKFSENYK------STI------------------------GVDFKSKTIE----VDGKKV--- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  108 rstnlqpyikraaasKLQ---SA--EKL-----MYictdqlgleqdFEqkqmpegklNVDGFLLCIDVSqgcNRK-FDDQ 176
Cdd:cd00154    50 ---------------KLQiwdTAgqERFrsitsSY-----------YR---------GAHGAILVYDVT---NREsFENL 91

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 348558014  177 LKFVNNLFvQLSKSKKPVIIAATKCD----ECVDHylREVQAFAsNKKNLLVVETSARFNVNIETCFTALVQ 244
Cdd:cd00154    92 DKWLNELK-EYAPPNIPIILVGNKSDledeRQVST--EEAQQFA-KENGLLFFETSAKTGENVDEAFESLAR 159
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 429-473 1.61e-07

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: 49.11  E-value: 1.61e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 348558014    429 EMKEKFKKTLEKIQFISPGQPWEEVICFVMEDEAFKYITEADSKE 473
Cdd:smart00441    2 EAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSESERE 46
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 28-244 3.32e-07

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: 51.69  E-value: 3.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   28 GNCGVGKSCLCNRFVRSKADEYYPEHTSvlsTIDFggrvvnndhflywgDITQNGEDGVECKIHVIEqTEFIDDqTFLPH 107
Cdd:cd00882     4 GRGGVGKSSLLNALLGGEVGEVSDVPGT---TRDP--------------DVYVKELDKGKVKLVLVD-TPGLDE-FGGLG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  108 RSTNLQPYIKRAaasklqsaeklmyictdqlgleqdfeqkqmpegklnvDGFLLCIDVSQGcnRKFDDQLkfvNNLFVQL 187
Cdd:cd00882    65 REELARLLLRGA-------------------------------------DLILLVVDSTDR--ESEEDAK---LLILRRL 102

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  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 4.09e-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: 51.36  E-value: 4.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014    28 GNCGVGKSCLCNRFVRSKADEYYpehtsvLSTIdfggrvvnndhflywgditqngedGVECKIHVIEqtefIDDQTflph 107
Cdd:pfam00071    6 GDGGVGKSSLLIRFTQNKFPEEY------IPTI------------------------GVDFYTKTIE----VDGKT---- 47

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   108 rstnlqpyikraaaSKLQsaeklmyIcTDQLGLEqDFE---QKQMPegklNVDGFLLCIDVSqgcNRK-FDDQLKFVNNL 183
Cdd:pfam00071   48 --------------VKLQ-------I-WDTAGQE-RFRalrPLYYR----GADGFLLVYDIT---SRDsFENVKKWVEEI 97

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 348558014   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 3.08e-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: 3.08e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 348558014    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 1.02e-05

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


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 47.12  E-value: 1.02e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014     28 GNCGVGKSCLCNRFVRskaDEYYPEHTSvlsTIdfggrvvnndhflywgditqngedGVECKIHVIEqtefIDDQTFlph 107
Cdd:smart00175    7 GDSGVGKSSLLSRFTD---GKFSEQYKS---TI------------------------GVDFKTKTIE----VDGKRV--- 49

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014    108 rstnlqpyikraaasKLQsaeklmyICtDQLGLE------QDFEQkqmpegklNVDGFLLCIDVSqgcNRK-FDDQLKFV 180
Cdd:smart00175   50 ---------------KLQ-------IW-DTAGQErfrsitSSYYR--------GAVGALLVYDIT---NREsFENLENWL 95

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 348558014    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 2.19e-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: 2.19e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 348558014    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 4.25e-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: 42.44  E-value: 4.25e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 348558014   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 2.15e-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: 43.32  E-value: 2.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014    157 DGFLLCIDVSqgcNRK-FDDQLKFVNNLFVQLSKSKKPVIIAATKCDEcvdHYLREV-----QAFAsNKKNLLVVETSAR 230
Cdd:smart00010   75 EGFLLVYSIT---DRQsFEEIAKFREQILRVKDRDDVPIVLVGNKCDL---ENERVVsteegKELA-RQWGCPFLETSAK 147

                            90
                    ....*....|....*...
gi 348558014    231 FNVNIETCFTALVQMLDK 248
Cdd:smart00010  148 ERINVDEAFYDLVREIRK 165
RAS smart00173
Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. ...
 157-248 5.32e-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: 5.32e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014    157 DGFLLCIDVSqgcNRK-FDDQLKFVNNLFVQLSKSKKPVIIAATKCDEcvdHYLREV-----QAFAsNKKNLLVVETSAR 230
Cdd:smart00173   73 EGFLLVYSIT---DRQsFEEIKKFREQILRVKDRDDVPIVLVGNKCDL---ESERVVsteegKELA-RQWGCPFLETSAK 145

                            90
                    ....*....|....*...
gi 348558014    231 FNVNIETCFTALVQMLDK 248
Cdd:smart00173  146 ERVNVDEAFYDLVREIRK 163
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1309-1423 7.50e-04

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: 42.70  E-value: 7.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014 1309 KQFDQDHNINLVSMEVTVnaVAGALKAFFTDLPDPLIP----------YSLHPelleAAKILDKTERLHALKEIVKKFHP 1378
Cdd:cd04399    63 PKKPDKEVIILKKFEPST--VASVLKLYLLELPDSLIPhdiydlirslYSAYP----PSQEDSDTARIQGLQSTLSQLPK 136

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 348558014 1379 VNYDVLRYVITHLNR---VSQQNKINLMTADNLSICFWPTLMRPDFEN 1423
Cdd:cd04399   137 SHIATLDAIITHFYRlieITKMGESEEEYADKLATSLSREILRPIIES 184
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
28-246 7.96e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 41.89  E-value: 7.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   28 GNCGVGKSCLCNRFVRSK--ADEYYPEHTSVLSTIDFggRVvnndhflywgditqngeDGVECKIHVIE---QTEFIDDQ 102
Cdd:COG1100    10 GTGGVGKTSLVNRLVGDIfsLEKYLSTNGVTIDKKEL--KL-----------------DGLDVDLVIWDtpgQDEFRETR 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  103 TFLphrstnlqpyikraaASKLQSAeklmyictdqlgleqdfeqkqmpegklnvDGFLLCIDVSQGCNRKfddQLKFVNN 182
Cdd:COG1100    71 QFY---------------ARQLTGA-----------------------------SLYLFVVDGTREETLQ---SLYELLE 103

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 348558014  183 LFVQLSKsKKPVIIAATKCDECVDHYLRE---VQAFASNKKNLLVVETSARFNVNIETCFTALVQML 246
Cdd:COG1100   104 SLRRLGK-KSPIILVLNKIDLYDEEEIEDeerLKEALSEDNIVEVVATSAKTGEGVEELFAALAEIL 169
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 156-244 2.75e-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: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014   156 VDGFLLCIDVSQGcnrkFDDQLKFVnnlFVQLSKSKKPVIIAATKCDECVDHYLREV---------QAFASNKKNLLVVE 226
Cdd:pfam00009   93 ADGAILVVDAVEG----VMPQTREH---LRLARQLGVPIIVFINKMDRVDGAELEEVveevsrellEKYGEDGEFVPVVP 165

                           90
                   ....*....|....*...
gi 348558014   227 TSARFNVNIETCFTALVQ 244
Cdd:pfam00009  166 GSALKGEGVQTLLDALDE 183
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 368-420 3.21e-03

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: 37.17  E-value: 3.21e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 348558014    368 MEKRTDFQLCFVVLEK----TPWDETDHIDKIHDRRIpfDLLSTLEAEKVYQNHVQH 420
Cdd:smart00441    1 EEAKEAFKELLKEHEVitpdTTWSEARKKLKNDPRYK--ALLSESEREQLFEDHIEE 55
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 156-246 5.34e-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: 39.15  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  156 VDGFLLCIDVSQGCNRKFddqlkfvnNLFVQLSKSKKPVIIAATKCDECVDHylREVQAFASNKKNLL----VVETSARF 231
Cdd:cd00880    77 ADLVLLVVDSDLTPVEEE--------AKLGLLRERGKPVLLVLNKIDLVPES--EEEELLRERKLELLpdlpVIAVSALP 146

                          90
                  ....*....|....*
gi 348558014  232 NVNIETCFTALVQML 246
Cdd:cd00880   147 GEGIDELRKKIAELL 161
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
156-246 8.95e-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: 8.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 348558014  156 VDGFLLCIDVSqgcnRKFDDQLKFVNNlfvQLSKSKKPVIIAATKCD----ECVDHYLREVQAFASNKKnllVVETSARF 231
Cdd:COG1159    83 VDVILFVVDAT----EKIGEGDEFILE---LLKKLKTPVILVINKIDlvkkEELLPLLAEYSELLDFAE---IVPISALK 152

                          90
                  ....*....|....*
gi 348558014  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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