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Conserved domains on  [gi|1333552760|ref|XP_023479422|]
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rho GTPase-activating protein 5 isoform X3 [Equus caballus]

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, ...
 556-1222 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: 1085.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  556 TCLSGQNCTDIKVEQLLASSLLQLDHGRLRLYHDSTNIDKVNLFILGKDGLAQELANEIRTQST-DDEYALDGKIYELDL 634
Cdd:pfam19518    1 TCPSGPNCVDSKIEQLLASRFPQPYPRRLKSYHDDANIDRINLVILGKDGLARELANEIRALCTnDDKYVLDGKMYELSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  635 RPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLNFIGEFIGKIRTEASQiRKDKYMANLPFTLILANQR-DSISKNLPI 713
Cdd:pfam19518   81 RPIEGNVRLPVNSFQTPTFKPHGCLCLYNSKESLSYVVESIEKSRESTLG-RRDNHLAHLPLTLILVNKRgDIGGETLQS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  714 LRHQGQQLANKLQCPFVDVP--AGTYPRKFNETQIKQALRGVLESVKHNLDVVSPVPTNKDVSEADLRIVMCAMCGDPFS 791
Cdd:pfam19518  160 LIQQGQQVANKLQCPFLDPAspGGGYGRNFNEKQINQVLRGLLESKRHNLNVVSPAPSIKDLSEADLRIVMCLMCGDPFS 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  792 VDLILSPFLDSHSCSAAQAGQNNSLMLDKIIGEKRRRIQITILSYHSSIGVRKDELVHGYILVYSAKRKASMGMLRAFLS 871
Cdd:pfam19518  240 VDLILSPFLQSQHCRPAQPGSGNSVLLELIIGGQRRRIELSILSYHSSFGVRKSRLVHGYILVYSAKRKASMAMLRAFLC 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  872 EVQDTIPVQLVAVTDSQADFFENEAIKELMTEGEHIATEITAKFTALYSLSQYHRQTEVFTLFFSDVLEKKNMIENSYLS 951
Cdd:pfam19518  320 EVQDIIPVQLVAVTDSQADFFESEVSREQLTEGEEIAHEIEAKFTALYCGSGYQHQTEVFTPFFKEVLEKKTIIEASHMY 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  952 DNTRESTHQsEDVFLPSPRDC--FPYNNYPDSDDDTEAPPPYSPIGDDVQLLptPSDRSRYRLDLEGNEYPIHSTPNCHD 1029
Cdd:pfam19518  400 DNTAEACST-EEEFFSSPRAGspSPNSNLPDSEDDTEPPPPYSPIRDDVQLL--PSDRSKFSLDLEGNDYSVISTPSSFE 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760 1030 HERNHkVPPPIKPKPVVPKTNVKKLDPNLLktIEAGIGKNPRKQTSRVPLAHPEDMDPSDnYSEPIDTIFRQKGYPDEIY 1109
Cdd:pfam19518  477 SKLNN-KVPPPVKPKPPVKFDVRKLDPNLY--IDGGNRDGPRSLPSRVTWAPGEGYDPSD-YAEPMDAVVKPRGEEENIY 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760 1110 VVPDDS-QNRIIKIRNSFVNNTQGdEENGFSDRTSKSHGERR--------PSKYKYKSKTLfSKAKSyYRRTHSDASDDE 1180
Cdd:pfam19518  553 SVPHDStQGKIITIRNSNKTQSNG-EGNGSDSEADSSSLERRkksalgvkPRLYRDRSKRL-GKFSS-YRTSFSVGSDDE 629

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1333552760 1181 AFTTSKTKRKGRHRGSEEDPLLSPVEtwkGGIDNPAITSDQE 1222
Cdd:pfam19518  630 LGPIRKKKREDDHGGSKGDNLLNPYE---GGIEDPKRRNILR 668
RhoGAP-FF1 pfam16512
p190-A and -B Rho GAPs FF domain; RhoGAP-FF1 is the FF domain of the Rho GTPase activating ...
 260-338 1.11e-35

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: 130.02  E-value: 1.11e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  260 DAYKTQRQLVVTATDKFEKLV-QTVRDYHATWKTVSNKLKNHPDYEEYINLEGTRKARNTFSKHIEQLKQEHIRKRREEY 338
Cdd:pfam16512    1 EAAKVRKELLDSATDAFERLIrSQVTDYRALWKTVSKKLSQHPEYQEYVELFGTDKAKRLFRKHIKKLKDEHIRKRRQGY 80
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 429-481 7.89e-09

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


:

Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 52.96  E-value: 7.89e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1333552760   429 EMKEKFKKTLEKIQFISPGQPWEEVMCFVMEDEAFKYITEADSKEVYGRHQRE 481
Cdd:smart00441    2 EAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 31-246 1.66e-08

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


The actual alignment was detected with superfamily member cd00876:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 160  Bit Score: 55.22  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760   31 GVGKSCLCNRFVRSKADEYY---PEHTSVlSTIDFggrvvnndhflywgditqngeDGVECKIHVI---EQTEFiddqtf 104
Cdd:cd00876      9 GVGKSALTIRFVSGEFVEEYdptIEDSYR-KQIVV---------------------DGETYTLDILdtaGQEEF------ 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  105 lphrSTNLQPYIKraaasklqsaeklmyictdqlgleqdfeqkqmpegklNVDGFLLCIDVsqgCNRK-FDDQLKFVNNL 183
Cdd:cd00876     61 ----SAMRDQYIR-------------------------------------NGDGFILVYSI---TSREsFEEIKNIREQI 96

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333552760  184 FVQLSKSKKPVIIAATKCDEcvDHYlREV-----QAFAsNKKNLLVVETSARFNVNIETCFTALVQML 246
Cdd:cd00876     97 LRVKDKEDVPIVLVGNKCDL--ENE-RQVsteegEALA-EEWGCPFLETSAKTNINIDELFNTLVREI 160
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 484-533 3.10e-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: 42.56  E-value: 3.10e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1333552760   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 8.69e-04

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


:

Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 38.71  E-value: 8.69e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333552760   368 MEKRADFQLCFVVLEK----TPWDETDHIDKINDRRIpfDLLSTLEAEKVYQNHVQH 420
Cdd:smart00441    1 EEAKEAFKELLKEHEVitpdTTWSEARKKLKNDPRYK--ALLSESEREQLFEDHIEE 55
 
Name Accession Description Interval E-value
RhoGAP_pG1_pG2 pfam19518
p190RhoGAP, pG1 and pG2 domains; The p190RhoGAP (GTPase-activating protein) proteins, ...
 556-1222 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: 1085.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  556 TCLSGQNCTDIKVEQLLASSLLQLDHGRLRLYHDSTNIDKVNLFILGKDGLAQELANEIRTQST-DDEYALDGKIYELDL 634
Cdd:pfam19518    1 TCPSGPNCVDSKIEQLLASRFPQPYPRRLKSYHDDANIDRINLVILGKDGLARELANEIRALCTnDDKYVLDGKMYELSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  635 RPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLNFIGEFIGKIRTEASQiRKDKYMANLPFTLILANQR-DSISKNLPI 713
Cdd:pfam19518   81 RPIEGNVRLPVNSFQTPTFKPHGCLCLYNSKESLSYVVESIEKSRESTLG-RRDNHLAHLPLTLILVNKRgDIGGETLQS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  714 LRHQGQQLANKLQCPFVDVP--AGTYPRKFNETQIKQALRGVLESVKHNLDVVSPVPTNKDVSEADLRIVMCAMCGDPFS 791
Cdd:pfam19518  160 LIQQGQQVANKLQCPFLDPAspGGGYGRNFNEKQINQVLRGLLESKRHNLNVVSPAPSIKDLSEADLRIVMCLMCGDPFS 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  792 VDLILSPFLDSHSCSAAQAGQNNSLMLDKIIGEKRRRIQITILSYHSSIGVRKDELVHGYILVYSAKRKASMGMLRAFLS 871
Cdd:pfam19518  240 VDLILSPFLQSQHCRPAQPGSGNSVLLELIIGGQRRRIELSILSYHSSFGVRKSRLVHGYILVYSAKRKASMAMLRAFLC 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  872 EVQDTIPVQLVAVTDSQADFFENEAIKELMTEGEHIATEITAKFTALYSLSQYHRQTEVFTLFFSDVLEKKNMIENSYLS 951
Cdd:pfam19518  320 EVQDIIPVQLVAVTDSQADFFESEVSREQLTEGEEIAHEIEAKFTALYCGSGYQHQTEVFTPFFKEVLEKKTIIEASHMY 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  952 DNTRESTHQsEDVFLPSPRDC--FPYNNYPDSDDDTEAPPPYSPIGDDVQLLptPSDRSRYRLDLEGNEYPIHSTPNCHD 1029
Cdd:pfam19518  400 DNTAEACST-EEEFFSSPRAGspSPNSNLPDSEDDTEPPPPYSPIRDDVQLL--PSDRSKFSLDLEGNDYSVISTPSSFE 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760 1030 HERNHkVPPPIKPKPVVPKTNVKKLDPNLLktIEAGIGKNPRKQTSRVPLAHPEDMDPSDnYSEPIDTIFRQKGYPDEIY 1109
Cdd:pfam19518  477 SKLNN-KVPPPVKPKPPVKFDVRKLDPNLY--IDGGNRDGPRSLPSRVTWAPGEGYDPSD-YAEPMDAVVKPRGEEENIY 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760 1110 VVPDDS-QNRIIKIRNSFVNNTQGdEENGFSDRTSKSHGERR--------PSKYKYKSKTLfSKAKSyYRRTHSDASDDE 1180
Cdd:pfam19518  553 SVPHDStQGKIITIRNSNKTQSNG-EGNGSDSEADSSSLERRkksalgvkPRLYRDRSKRL-GKFSS-YRTSFSVGSDDE 629

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1333552760 1181 AFTTSKTKRKGRHRGSEEDPLLSPVEtwkGGIDNPAITSDQE 1222
Cdd:pfam19518  630 LGPIRKKKREDDHGGSKGDNLLNPYE---GGIEDPKRRNILR 668
pseudoGTPaseD_p190RhoGAP-B cd22220
pseudoGTPase domain found in p190RhoGAP-B and similar proteins; p190RhoGAP protein B ...
 592-762 1.44e-122

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: 375.73  E-value: 1.44e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  592 NIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLNFI 671
Cdd:cd22220      1 NIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDANSPYLLSQLWTSAFKPHGCFCVFNSIESLNFI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  672 GEFIGKIRTEASQIRKDKYMANLPFTLILANQRDSISKNLPILRHQGQQLANKLQCPFVDVPAGTYPRKFNETQIKQALR 751
Cdd:cd22220     81 GECIGKIRAEASQIRRDRYIANLPFTLILANQRDSVSKNLPILRHQGQQLANKLQCPFVDVPAGTYPRKFNETQIKQALR 160

                          170
                   ....*....|.
gi 1333552760  752 GVLESVKHNLD 762
Cdd:cd22220    161 GVLESVKHNLD 171
RhoGAP-FF1 pfam16512
p190-A and -B Rho GAPs FF domain; RhoGAP-FF1 is the FF domain of the Rho GTPase activating ...
 260-338 1.11e-35

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: 130.02  E-value: 1.11e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  260 DAYKTQRQLVVTATDKFEKLV-QTVRDYHATWKTVSNKLKNHPDYEEYINLEGTRKARNTFSKHIEQLKQEHIRKRREEY 338
Cdd:pfam16512    1 EAAKVRKELLDSATDAFERLIrSQVTDYRALWKTVSKKLSQHPEYQEYVELFGTDKAKRLFRKHIKKLKDEHIRKRRQGY 80
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 429-481 7.89e-09

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


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 52.96  E-value: 7.89e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1333552760   429 EMKEKFKKTLEKIQFISPGQPWEEVMCFVMEDEAFKYITEADSKEVYGRHQRE 481
Cdd:smart00441    2 EAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
 31-246 1.66e-08

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


Pssm-ID: 206642 [Multi-domain]  Cd Length: 160  Bit Score: 55.22  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760   31 GVGKSCLCNRFVRSKADEYY---PEHTSVlSTIDFggrvvnndhflywgditqngeDGVECKIHVI---EQTEFiddqtf 104
Cdd:cd00876      9 GVGKSALTIRFVSGEFVEEYdptIEDSYR-KQIVV---------------------DGETYTLDILdtaGQEEF------ 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  105 lphrSTNLQPYIKraaasklqsaeklmyictdqlgleqdfeqkqmpegklNVDGFLLCIDVsqgCNRK-FDDQLKFVNNL 183
Cdd:cd00876     61 ----SAMRDQYIR-------------------------------------NGDGFILVYSI---TSREsFEEIKNIREQI 96

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333552760  184 FVQLSKSKKPVIIAATKCDEcvDHYlREV-----QAFAsNKKNLLVVETSARFNVNIETCFTALVQML 246
Cdd:cd00876     97 LRVKDKEDVPIVLVGNKCDL--ENE-RQVsteegEALA-EEWGCPFLETSAKTNINIDELFNTLVREI 160
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 28-244 3.59e-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: 3.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760   28 GNCGVGKSCLCNRFVRSKADEYYpehtsvLSTIdfggrvvnndhflywgditqngedGVECKIHVIEqtefIDDQTflph 107
Cdd:pfam00071    6 GDGGVGKSSLLIRFTQNKFPEEY------IPTI------------------------GVDFYTKTIE----VDGKT---- 47

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  108 rstnlqpyikraaaSKLQsaeklmyIcTDQLGLEqDFE---QKQMPegklNVDGFLLCIDVSqgcNRK-FDDQLKFVNNL 183
Cdd:pfam00071   48 --------------VKLQ-------I-WDTAGQE-RFRalrPLYYR----GADGFLLVYDIT---SRDsFENVKKWVEEI 97

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333552760  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 4.70e-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: 44.87  E-value: 4.70e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333552760   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 9.79e-06

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: 9.79e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760    28 GNCGVGKSCLCNRFVRskaDEYYPEHTSvlsTIdfggrvvnndhflywgditqngedGVECKIHVIEqtefIDDQTFlph 107
Cdd:smart00175    7 GDSGVGKSSLLSRFTD---GKFSEQYKS---TI------------------------GVDFKTKTIE----VDGKRV--- 49

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760   108 rstnlqpyikraaasKLQsaeklmyICtDQLGLE------QDFEQkqmpegklNVDGFLLCIDVSqgcNRK-FDDQLKFV 180
Cdd:smart00175   50 ---------------KLQ-------IW-DTAGQErfrsitSSYYR--------GAVGALLVYDIT---NREsFENLENWL 95

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333552760   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 3.10e-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: 42.56  E-value: 3.10e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1333552760   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 6.25e-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: 41.67  E-value: 6.25e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333552760  485 KAKEEFQEMLFEHselfydldlNATPSSdKMSEIHTVLSEEPRYKALQKLApDRESLLLKH 545
Cdd:pfam01846    1 KAREAFKELLKEH---------KITPYS-TWSEIKKKIENDPRYKALLDGS-EREELFEDY 50
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
28-246 5.69e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 42.28  E-value: 5.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760   28 GNCGVGKSCLCNRFVRSK--ADEYYPEHTSVLSTIDFggRVvnndhflywgditqngeDGVECKIHVIE---QTEFIDDQ 102
Cdd:COG1100     10 GTGGVGKTSLVNRLVGDIfsLEKYLSTNGVTIDKKEL--KL-----------------DGLDVDLVIWDtpgQDEFRETR 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  103 TFLphrstnlqpyikraaASKLQSAeklmyictdqlgleqdfeqkqmpegklnvDGFLLCIDVSQgcnRKFDDQLKFVNN 182
Cdd:COG1100     71 QFY---------------ARQLTGA-----------------------------SLYLFVVDGTR---EETLQSLYELLE 103

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333552760  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 8.69e-04

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


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 38.71  E-value: 8.69e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333552760   368 MEKRADFQLCFVVLEK----TPWDETDHIDKINDRRIpfDLLSTLEAEKVYQNHVQH 420
Cdd:smart00441    1 EEAKEAFKELLKEHEVitpdTTWSEARKKLKNDPRYK--ALLSESEREQLFEDHIEE 55
 
Name Accession Description Interval E-value
RhoGAP_pG1_pG2 pfam19518
p190RhoGAP, pG1 and pG2 domains; The p190RhoGAP (GTPase-activating protein) proteins, ...
 556-1222 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: 1085.51  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  556 TCLSGQNCTDIKVEQLLASSLLQLDHGRLRLYHDSTNIDKVNLFILGKDGLAQELANEIRTQST-DDEYALDGKIYELDL 634
Cdd:pfam19518    1 TCPSGPNCVDSKIEQLLASRFPQPYPRRLKSYHDDANIDRINLVILGKDGLARELANEIRALCTnDDKYVLDGKMYELSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  635 RPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLNFIGEFIGKIRTEASQiRKDKYMANLPFTLILANQR-DSISKNLPI 713
Cdd:pfam19518   81 RPIEGNVRLPVNSFQTPTFKPHGCLCLYNSKESLSYVVESIEKSRESTLG-RRDNHLAHLPLTLILVNKRgDIGGETLQS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  714 LRHQGQQLANKLQCPFVDVP--AGTYPRKFNETQIKQALRGVLESVKHNLDVVSPVPTNKDVSEADLRIVMCAMCGDPFS 791
Cdd:pfam19518  160 LIQQGQQVANKLQCPFLDPAspGGGYGRNFNEKQINQVLRGLLESKRHNLNVVSPAPSIKDLSEADLRIVMCLMCGDPFS 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  792 VDLILSPFLDSHSCSAAQAGQNNSLMLDKIIGEKRRRIQITILSYHSSIGVRKDELVHGYILVYSAKRKASMGMLRAFLS 871
Cdd:pfam19518  240 VDLILSPFLQSQHCRPAQPGSGNSVLLELIIGGQRRRIELSILSYHSSFGVRKSRLVHGYILVYSAKRKASMAMLRAFLC 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  872 EVQDTIPVQLVAVTDSQADFFENEAIKELMTEGEHIATEITAKFTALYSLSQYHRQTEVFTLFFSDVLEKKNMIENSYLS 951
Cdd:pfam19518  320 EVQDIIPVQLVAVTDSQADFFESEVSREQLTEGEEIAHEIEAKFTALYCGSGYQHQTEVFTPFFKEVLEKKTIIEASHMY 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  952 DNTRESTHQsEDVFLPSPRDC--FPYNNYPDSDDDTEAPPPYSPIGDDVQLLptPSDRSRYRLDLEGNEYPIHSTPNCHD 1029
Cdd:pfam19518  400 DNTAEACST-EEEFFSSPRAGspSPNSNLPDSEDDTEPPPPYSPIRDDVQLL--PSDRSKFSLDLEGNDYSVISTPSSFE 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760 1030 HERNHkVPPPIKPKPVVPKTNVKKLDPNLLktIEAGIGKNPRKQTSRVPLAHPEDMDPSDnYSEPIDTIFRQKGYPDEIY 1109
Cdd:pfam19518  477 SKLNN-KVPPPVKPKPPVKFDVRKLDPNLY--IDGGNRDGPRSLPSRVTWAPGEGYDPSD-YAEPMDAVVKPRGEEENIY 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760 1110 VVPDDS-QNRIIKIRNSFVNNTQGdEENGFSDRTSKSHGERR--------PSKYKYKSKTLfSKAKSyYRRTHSDASDDE 1180
Cdd:pfam19518  553 SVPHDStQGKIITIRNSNKTQSNG-EGNGSDSEADSSSLERRkksalgvkPRLYRDRSKRL-GKFSS-YRTSFSVGSDDE 629

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|..
gi 1333552760 1181 AFTTSKTKRKGRHRGSEEDPLLSPVEtwkGGIDNPAITSDQE 1222
Cdd:pfam19518  630 LGPIRKKKREDDHGGSKGDNLLNPYE---GGIEDPKRRNILR 668
pseudoGTPaseD_p190RhoGAP-B cd22220
pseudoGTPase domain found in p190RhoGAP-B and similar proteins; p190RhoGAP protein B ...
 592-762 1.44e-122

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: 375.73  E-value: 1.44e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  592 NIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLNFI 671
Cdd:cd22220      1 NIDKVNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDANSPYLLSQLWTSAFKPHGCFCVFNSIESLNFI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  672 GEFIGKIRTEASQIRKDKYMANLPFTLILANQRDSISKNLPILRHQGQQLANKLQCPFVDVPAGTYPRKFNETQIKQALR 751
Cdd:cd22220     81 GECIGKIRAEASQIRRDRYIANLPFTLILANQRDSVSKNLPILRHQGQQLANKLQCPFVDVPAGTYPRKFNETQIKQALR 160

                          170
                   ....*....|.
gi 1333552760  752 GVLESVKHNLD 762
Cdd:cd22220    161 GVLESVKHNLD 171
pseudoGTPaseD_p190RhoGAP cd22207
pseudoGTPase domain found in the family of p190RhoGAP; This family includes two p190RhoGAP ...
 596-759 7.25e-65

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


Pssm-ID: 412064  Cd Length: 166  Bit Score: 216.75  E-value: 7.25e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  596 VNLFILGKDGLAQELANEIRTQSTDDEYALDGKIYELDLRPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLNFIGEFI 675
Cdd:cd22207      1 LNLVLLGSDGLADELANEIRALCEDDEYELDGVVYSLDLRTIDGDVSLPQNSFQTTDFKPHGCLCVYSSRESLEYIKTSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  676 GKIRTEASQIRKDKYMANLPFTLILANQRDSISKNLPILRHQGQQLANKLQCPFVDVPAGTYP--RKFNETQIKQALRGV 753
Cdd:cd22207     81 EKTLLSDLEEEDKLPFQGLPIVLLFARDPSISEKEVSQLREEGQELADRLQCVFIDVPSSGEAmgRKFHESQIDDALRSL 160


                   ....*.
gi 1333552760  754 LESVKH 759
Cdd:cd22207    161 IESIKH 166
pseudoGTPaseD_p190RhoGAP-A cd22221
pseudoGTPase domain found in p190RhoGAP-A and similar proteins; p190RhoGAP protein A ...
 592-760 3.58e-54

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: 186.61  E-value: 3.58e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  592 NIDKVNLFILGKDGLAQELANEIRTQST-DDEYALDGKIYELDLRPVDAKSPYFLSQLWTAAFKPHGCFCVFNSIESLNF 670
Cdd:cd22221      1 NVDRINLVILGKDGLARELANEIRALCTnDDKYVLDGKMYELSLRPIEGNVRLPVNSFQTPTFQPHGCLCLYNSKESLSY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  671 IGEFIGKIRtEASQIRKDKYMANLPFTLILANQR-DSISKNLPILRHQGQQLANKLQCPFVDvPAGT---YPRKFNETQI 746
Cdd:cd22221     81 VVESIEKSR-ESTLGRRDNHLAHLPLTLILVNKRgDTSGETLQSLIQQGQQVASKLQCVFLD-PASTgigYGRNINEKQI 158

                          170
                   ....*....|....
gi 1333552760  747 KQALRGVLESVKHN 760
Cdd:cd22221    159 SQILKGLLDSKRNL 172
RhoGAP-FF1 pfam16512
p190-A and -B Rho GAPs FF domain; RhoGAP-FF1 is the FF domain of the Rho GTPase activating ...
 260-338 1.11e-35

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: 130.02  E-value: 1.11e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  260 DAYKTQRQLVVTATDKFEKLV-QTVRDYHATWKTVSNKLKNHPDYEEYINLEGTRKARNTFSKHIEQLKQEHIRKRREEY 338
Cdd:pfam16512    1 EAAKVRKELLDSATDAFERLIrSQVTDYRALWKTVSKKLSQHPEYQEYVELFGTDKAKRLFRKHIKKLKDEHIRKRRQGY 80
FF smart00441
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ...
 429-481 7.89e-09

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


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 52.96  E-value: 7.89e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1333552760   429 EMKEKFKKTLEKIQFISPGQPWEEVMCFVMEDEAFKYITEADSKEVYGRHQRE 481
Cdd:smart00441    2 EAKEAFKELLKEHEVITPDTTWSEARKKLKNDPRYKALLSESEREQLFEDHIE 54
Ras cd00876
Rat sarcoma (Ras) family of small guanosine triphosphatases (GTPases); The Ras family of the ...
 31-246 1.66e-08

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


Pssm-ID: 206642 [Multi-domain]  Cd Length: 160  Bit Score: 55.22  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760   31 GVGKSCLCNRFVRSKADEYY---PEHTSVlSTIDFggrvvnndhflywgditqngeDGVECKIHVI---EQTEFiddqtf 104
Cdd:cd00876      9 GVGKSALTIRFVSGEFVEEYdptIEDSYR-KQIVV---------------------DGETYTLDILdtaGQEEF------ 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  105 lphrSTNLQPYIKraaasklqsaeklmyictdqlgleqdfeqkqmpegklNVDGFLLCIDVsqgCNRK-FDDQLKFVNNL 183
Cdd:cd00876     61 ----SAMRDQYIR-------------------------------------NGDGFILVYSI---TSREsFEEIKNIREQI 96

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333552760  184 FVQLSKSKKPVIIAATKCDEcvDHYlREV-----QAFAsNKKNLLVVETSARFNVNIETCFTALVQML 246
Cdd:cd00876     97 LRVKDKEDVPIVLVGNKCDL--ENE-RQVsteegEALA-EEWGCPFLETSAKTNINIDELFNTLVREI 160
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
 28-244 4.11e-08

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


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 54.00  E-value: 4.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760   28 GNCGVGKSCLCNRFVRSKADEYYPehtsvlSTIdfggrvvnndhflywgditqngedGVECKIHVIEqtefIDDQTFlph 107
Cdd:cd00154      7 GDSGVGKTSLLLRFVDNKFSENYK------STI------------------------GVDFKSKTIE----VDGKKV--- 49

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  108 rstnlqpyikraaasKLQ---SA--EKL-----MYictdqlgleqdFEqkqmpegklNVDGFLLCIDVSqgcNRK-FDDQ 176
Cdd:cd00154     50 ---------------KLQiwdTAgqERFrsitsSY-----------YR---------GAHGAILVYDVT---NREsFENL 91

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333552760  177 LKFVNNLFvQLSKSKKPVIIAATKCD----ECVDHylREVQAFAsNKKNLLVVETSARFNVNIETCFTALVQ 244
Cdd:cd00154     92 DKWLNELK-EYAPPNIPIILVGNKSDledeRQVST--EEAQQFA-KENGLLFFETSAKTGENVDEAFESLAR 159
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 28-244 1.76e-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: 52.07  E-value: 1.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760   28 GNCGVGKSCLCNRFVRSKADEYYPEHTSvlsTIDFggrvvnndhflywgDITQNGEDGVECKIHVIEqTEFIDDqTFLPH 107
Cdd:cd00882      4 GRGGVGKSSLLNALLGGEVGEVSDVPGT---TRDP--------------DVYVKELDKGKVKLVLVD-TPGLDE-FGGLG 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  108 RSTNLQPYIKRAaasklqsaeklmyictdqlgleqdfeqkqmpegklnvDGFLLCIDVSQGcnRKFDDQLkfvNNLFVQL 187
Cdd:cd00882     65 REELARLLLRGA-------------------------------------DLILLVVDSTDR--ESEEDAK---LLILRRL 102

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  188 SKSKKPVIIAATKCD---ECVDHYLREVQaFASNKKNLLVVETSARFNVNIETCFTALVQ 244
Cdd:cd00882    103 RKEGIPIILVGNKIDlleEREVEELLRLE-ELAKILGVPVFEVSAKTGEGVDELFEKLIE 161
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 28-244 3.59e-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: 3.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760   28 GNCGVGKSCLCNRFVRSKADEYYpehtsvLSTIdfggrvvnndhflywgditqngedGVECKIHVIEqtefIDDQTflph 107
Cdd:pfam00071    6 GDGGVGKSSLLIRFTQNKFPEEY------IPTI------------------------GVDFYTKTIE----VDGKT---- 47

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  108 rstnlqpyikraaaSKLQsaeklmyIcTDQLGLEqDFE---QKQMPegklNVDGFLLCIDVSqgcNRK-FDDQLKFVNNL 183
Cdd:pfam00071   48 --------------VKLQ-------I-WDTAGQE-RFRalrPLYYR----GADGFLLVYDIT---SRDsFENVKKWVEEI 97

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333552760  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 4.70e-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: 44.87  E-value: 4.70e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333552760   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 9.79e-06

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: 9.79e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760    28 GNCGVGKSCLCNRFVRskaDEYYPEHTSvlsTIdfggrvvnndhflywgditqngedGVECKIHVIEqtefIDDQTFlph 107
Cdd:smart00175    7 GDSGVGKSSLLSRFTD---GKFSEQYKS---TI------------------------GVDFKTKTIE----VDGKRV--- 49

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760   108 rstnlqpyikraaasKLQsaeklmyICtDQLGLE------QDFEQkqmpegklNVDGFLLCIDVSqgcNRK-FDDQLKFV 180
Cdd:smart00175   50 ---------------KLQ-------IW-DTAGQErfrsitSSYYR--------GAVGALLVYDIT---NREsFENLENWL 95

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333552760   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 3.10e-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: 42.56  E-value: 3.10e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1333552760   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 6.25e-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: 41.67  E-value: 6.25e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333552760  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 2.00e-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: 2.00e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760   157 DGFLLCIDVSqgcNRK-FDDQLKFVNNLFVQLSKSKKPVIIAATKCDEcvdHYLREV-----QAFAsNKKNLLVVETSAR 230
Cdd:smart00010   75 EGFLLVYSIT---DRQsFEEIAKFREQILRVKDRDDVPIVLVGNKCDL---ENERVVsteegKELA-RQWGCPFLETSAK 147

                            90
                    ....*....|....*...
gi 1333552760   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 5.04e-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: 5.04e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760   157 DGFLLCIDVSqgcNRK-FDDQLKFVNNLFVQLSKSKKPVIIAATKCDEcvdHYLREV-----QAFAsNKKNLLVVETSAR 230
Cdd:smart00173   73 EGFLLVYSIT---DRQsFEEIKKFREQILRVKDRDDVPIVLVGNKCDL---ESERVVsteegKELA-RQWGCPFLETSAK 145

                            90
                    ....*....|....*...
gi 1333552760   231 FNVNIETCFTALVQMLDK 248
Cdd:smart00173  146 ERVNVDEAFYDLVREIRK 163
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
28-246 5.69e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 42.28  E-value: 5.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760   28 GNCGVGKSCLCNRFVRSK--ADEYYPEHTSVLSTIDFggRVvnndhflywgditqngeDGVECKIHVIE---QTEFIDDQ 102
Cdd:COG1100     10 GTGGVGKTSLVNRLVGDIfsLEKYLSTNGVTIDKKEL--KL-----------------DGLDVDLVIWDtpgQDEFRETR 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  103 TFLphrstnlqpyikraaASKLQSAeklmyictdqlgleqdfeqkqmpegklnvDGFLLCIDVSQgcnRKFDDQLKFVNN 182
Cdd:COG1100     71 QFY---------------ARQLTGA-----------------------------SLYLFVVDGTR---EETLQSLYELLE 103

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333552760  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 8.69e-04

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


Pssm-ID: 128718 [Multi-domain]  Cd Length: 55  Bit Score: 38.71  E-value: 8.69e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333552760   368 MEKRADFQLCFVVLEK----TPWDETDHIDKINDRRIpfDLLSTLEAEKVYQNHVQH 420
Cdd:smart00441    1 EEAKEAFKELLKEHEVitpdTTWSEARKKLKNDPRYK--ALLSESEREQLFEDHIEE 55
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 156-244 1.95e-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: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  156 VDGFLLCIDVSQGcnrkFDDQLKFVnnlFVQLSKSKKPVIIAATKCDECVDHYLREV---------QAFASNKKNLLVVE 226
Cdd:pfam00009   93 ADGAILVVDAVEG----VMPQTREH---LRLARQLGVPIIVFINKMDRVDGAELEEVveevsrellEKYGEDGEFVPVVP 165

                           90
                   ....*....|....*...
gi 1333552760  227 TSARFNVNIETCFTALVQ 244
Cdd:pfam00009  166 GSALKGEGVQTLLDALDE 183
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 156-246 3.58e-03

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


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 39.54  E-value: 3.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  156 VDGFLLCIDVSQGCNRKFddqlkfvnNLFVQLSKSKKPVIIAATKCDECVDHylREVQAFASNKKNLL----VVETSARF 231
Cdd:cd00880     77 ADLVLLVVDSDLTPVEEE--------AKLGLLRERGKPVLLVLNKIDLVPES--EEEELLRERKLELLpdlpVIAVSALP 146

                           90
                   ....*....|....*
gi 1333552760  232 NVNIETCFTALVQML 246
Cdd:cd00880    147 GEGIDELRKKIAELL 161
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
156-246 7.07e-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: 7.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333552760  156 VDGFLLCIDVSqgcnRKFDDQLKFVNNlfvQLSKSKKPVIIAATKCD----ECVDHYLREVQAFASNKKnllVVETSARF 231
Cdd:COG1159     83 VDVILFVVDAT----EKIGEGDEFILE---LLKKLKTPVILVINKIDlvkkEELLPLLAEYSELLDFAE---IVPISALK 152

                           90
                   ....*....|....*
gi 1333552760  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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