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Conserved domains on  [gi|300797517|ref|NP_001178013|]
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GATOR2 complex protein WDR24 [Rattus norvegicus]

Protein Classification

WD40 and mRING-H2-C3H3C2_WDR24 domain-containing protein( domain architecture ID 11455581)

WD40 and mRING-H2-C3H3C2_WDR24 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
6-324 1.82e-31

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 127.72  E-value: 1.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517   6 RVTTALSGSALTGRTMHchlDAPANAISVCRDAAQVVVAG--RSIfKIYAIEEEQFVEKLNlrvGRKPSLNlscaDVVWH 83
Cdd:COG2319  103 RLWDLATGLLLRTLTGH---TGAVRSVAFSPDGKTLASGSadGTV-RLWDLATGKLLRTLT---GHSGAVT----SVAFS 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517  84 QmDENLLATAATNGVVVTWNLgrpSRNKQDQLFTEHKRTVNKVCFHPtEAHVLLSGSQDGFMKCFDLRRKDSVSTFSGQS 163
Cdd:COG2319  172 P-DGKLLASGSDDGTVRLWDL---ATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLATGKLLRTLTGHS 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 164 ESVRDVQFSiRDYFTFASTFENGNVQLWDIRrPDRCERMFTAHNGPVFCCDWHPeDRGWLATGGRDKMVKVWDMTTHRak 243
Cdd:COG2319  247 GSVRSVAFS-PDGRLLASGSADGTVRLWDLA-TGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGK-- 321

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 244 eihCVQTI----ASVARVKWRPEcRHHLATCSMmvDHNIYVWDVRRPfVPAAMFEEHRDVTTGIAWrHPhDPSFLLSGSK 319
Cdd:COG2319  322 ---LLRTLtghtGAVRSVAFSPD-GKTLASGSD--DGTVRLWDLATG-ELLRTLTGHTGAVTSVAF-SP-DGRTLASGSA 392


                 ....*
gi 300797517 320 DSTLC 324
Cdd:COG2319  393 DGTVR 397
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
 742-787 1.42e-26

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 (WDR24) and similar proteins; WDR24 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea3/WDR59, and Mio/Sea4. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. WDR24 contains an N-terminal WD40 domain and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type. Sea2 is the yeast counterpart of WDR24. It is not included in this subfamily.


:

Pssm-ID: 438354  Cd Length: 46  Bit Score: 102.36  E-value: 1.42e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 300797517 742 MCAVCHHVVKGLFVWCQGCSHGGHLQHIMKWLEGSSHCPAGCGHLC 787
Cdd:cd16693    1 MCSVCHLPVKGLYVWCQGCGHGGHLEHMKEWFSTNSHCPAGCGHLC 46
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
6-324 1.82e-31

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 127.72  E-value: 1.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517   6 RVTTALSGSALTGRTMHchlDAPANAISVCRDAAQVVVAG--RSIfKIYAIEEEQFVEKLNlrvGRKPSLNlscaDVVWH 83
Cdd:COG2319  103 RLWDLATGLLLRTLTGH---TGAVRSVAFSPDGKTLASGSadGTV-RLWDLATGKLLRTLT---GHSGAVT----SVAFS 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517  84 QmDENLLATAATNGVVVTWNLgrpSRNKQDQLFTEHKRTVNKVCFHPtEAHVLLSGSQDGFMKCFDLRRKDSVSTFSGQS 163
Cdd:COG2319  172 P-DGKLLASGSDDGTVRLWDL---ATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLATGKLLRTLTGHS 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 164 ESVRDVQFSiRDYFTFASTFENGNVQLWDIRrPDRCERMFTAHNGPVFCCDWHPeDRGWLATGGRDKMVKVWDMTTHRak 243
Cdd:COG2319  247 GSVRSVAFS-PDGRLLASGSADGTVRLWDLA-TGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGK-- 321

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 244 eihCVQTI----ASVARVKWRPEcRHHLATCSMmvDHNIYVWDVRRPfVPAAMFEEHRDVTTGIAWrHPhDPSFLLSGSK 319
Cdd:COG2319  322 ---LLRTLtghtGAVRSVAFSPD-GKTLASGSD--DGTVRLWDLATG-ELLRTLTGHTGAVTSVAF-SP-DGRTLASGSA 392


                 ....*
gi 300797517 320 DSTLC 324
Cdd:COG2319  393 DGTVR 397
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 86-323 3.74e-31

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 123.60  E-value: 3.74e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517  86 DENLLATAATNGVVVTWNLgrpSRNKQDQLFTEHKRTVNKVCFHPTEaHVLLSGSQDGFMKCFDLRRKDSVSTFSGQSES 165
Cdd:cd00200   62 DGTYLASGSSDKTIRLWDL---ETGECVRTLTGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVETGKCLTTLRGHTDW 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 166 VRDVQFSIRDYFTFASTfENGNVQLWDIrRPDRCERMFTAHNGPVFCCDWHPeDRGWLATGGRDKMVKVWDMTThrakeI 245
Cdd:cd00200  138 VNSVAFSPDGTFVASSS-QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLST-----G 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 246 HCVQTI----ASVARVKWRPEcRHHLATCSMmvDHNIYVWDVrRPFVPAAMFEEHRDVTTGIAWrHPhDPSFLLSGSKDS 321
Cdd:cd00200  210 KCLGTLrgheNGVNSVAFSPD-GYLLASGSE--DGTIRVWDL-RTGECVQTLSGHTNSVTSLAW-SP-DGKRLASGSADG 283


                 ..
gi 300797517 322 TL 323
Cdd:cd00200  284 TI 285
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
 742-787 1.42e-26

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 (WDR24) and similar proteins; WDR24 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea3/WDR59, and Mio/Sea4. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. WDR24 contains an N-terminal WD40 domain and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type. Sea2 is the yeast counterpart of WDR24. It is not included in this subfamily.


Pssm-ID: 438354  Cd Length: 46  Bit Score: 102.36  E-value: 1.42e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 300797517 742 MCAVCHHVVKGLFVWCQGCSHGGHLQHIMKWLEGSSHCPAGCGHLC 787
Cdd:cd16693    1 MCSVCHLPVKGLYVWCQGCGHGGHLEHMKEWFSTNSHCPAGCGHLC 46
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 180-323 1.44e-09

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 61.64  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 180 ASTFEnGNVQLWDIRRPDRCERMfTAHNGPVFCCDWHPEDRGWLATGGRDKMVKVWdmTTHRAKEIHCVQTIASVARVKW 259
Cdd:PLN00181 550 SSNFE-GVVQVWDVARSQLVTEM-KEHEKRVWSIDYSSADPTLLASGSDDGSVKLW--SINQGVSIGTIKTKANICCVQF 625

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300797517 260 RPECRHHLATCSmmVDHNIYVWDVRRPFVP-AAMFEEHRDVTtgiaWRHPHDPSFLLSGSKDSTL 323
Cdd:PLN00181 626 PSESGRSLAFGS--ADHKVYYYDLRNPKLPlCTMIGHSKTVS----YVRFVDSSTLVSSSTDNTL 684
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 198-236 4.19e-08

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 49.62  E-value: 4.19e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 300797517   198 RCERMFTAHNGPVFCCDWHPeDRGWLATGGRDKMVKVWD 236
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
198-236 9.13e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 48.88  E-value: 9.13e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 300797517  198 RCERMFTAHNGPVFCCDWHPEDRgWLATGGRDKMVKVWD 236
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGK-LLASGSDDGTVKVWD 39
zf-RING_16 pfam17120
RING/Ubox like zinc-binding domain;
742-787 7.28e-04

RING/Ubox like zinc-binding domain;


Pssm-ID: 375001  Cd Length: 57  Bit Score: 38.15  E-value: 7.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 300797517  742 MCAVCHHVVKGLFVWCQGCSHGGHLQHIMKWLE-GSSHCPAGCGHLC 787
Cdd:pfam17120   6 SCNYCCLRVRGRVFLCGVCQHVLHASCAREWWEnDDGECPSGCGCNC 52
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
6-324 1.82e-31

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 127.72  E-value: 1.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517   6 RVTTALSGSALTGRTMHchlDAPANAISVCRDAAQVVVAG--RSIfKIYAIEEEQFVEKLNlrvGRKPSLNlscaDVVWH 83
Cdd:COG2319  103 RLWDLATGLLLRTLTGH---TGAVRSVAFSPDGKTLASGSadGTV-RLWDLATGKLLRTLT---GHSGAVT----SVAFS 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517  84 QmDENLLATAATNGVVVTWNLgrpSRNKQDQLFTEHKRTVNKVCFHPtEAHVLLSGSQDGFMKCFDLRRKDSVSTFSGQS 163
Cdd:COG2319  172 P-DGKLLASGSDDGTVRLWDL---ATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLATGKLLRTLTGHS 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 164 ESVRDVQFSiRDYFTFASTFENGNVQLWDIRrPDRCERMFTAHNGPVFCCDWHPeDRGWLATGGRDKMVKVWDMTTHRak 243
Cdd:COG2319  247 GSVRSVAFS-PDGRLLASGSADGTVRLWDLA-TGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGK-- 321

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 244 eihCVQTI----ASVARVKWRPEcRHHLATCSMmvDHNIYVWDVRRPfVPAAMFEEHRDVTTGIAWrHPhDPSFLLSGSK 319
Cdd:COG2319  322 ---LLRTLtghtGAVRSVAFSPD-GKTLASGSD--DGTVRLWDLATG-ELLRTLTGHTGAVTSVAF-SP-DGRTLASGSA 392


                 ....*
gi 300797517 320 DSTLC 324
Cdd:COG2319  393 DGTVR 397
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 86-323 3.74e-31

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 123.60  E-value: 3.74e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517  86 DENLLATAATNGVVVTWNLgrpSRNKQDQLFTEHKRTVNKVCFHPTEaHVLLSGSQDGFMKCFDLRRKDSVSTFSGQSES 165
Cdd:cd00200   62 DGTYLASGSSDKTIRLWDL---ETGECVRTLTGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVETGKCLTTLRGHTDW 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 166 VRDVQFSIRDYFTFASTfENGNVQLWDIrRPDRCERMFTAHNGPVFCCDWHPeDRGWLATGGRDKMVKVWDMTThrakeI 245
Cdd:cd00200  138 VNSVAFSPDGTFVASSS-QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLST-----G 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 246 HCVQTI----ASVARVKWRPEcRHHLATCSMmvDHNIYVWDVrRPFVPAAMFEEHRDVTTGIAWrHPhDPSFLLSGSKDS 321
Cdd:cd00200  210 KCLGTLrgheNGVNSVAFSPD-GYLLASGSE--DGTIRVWDL-RTGECVQTLSGHTNSVTSLAW-SP-DGKRLASGSADG 283


                 ..
gi 300797517 322 TL 323
Cdd:cd00200  284 TI 285
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 86-324 8.16e-29

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 117.05  E-value: 8.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517  86 DENLLATAATNGVVVTWNLgrpSRNKQDQLFTEHKRTVNKVCFHPTeAHVLLSGSQDGFMKCFDLRRKDSVSTFSGQSES 165
Cdd:cd00200   20 DGKLLATGSGDGTIKVWDL---ETGELLRTLKGHTGPVRDVAASAD-GTYLASGSSDKTIRLWDLETGECVRTLTGHTSY 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 166 VRDVQFSiRDYFTFASTFENGNVQLWDIrRPDRCERMFTAHNGPVFCCDWHPeDRGWLATGGRDKMVKVWDMTTHRakei 245
Cdd:cd00200   96 VSSVAFS-PDGRILSSSSRDKTIKVWDV-ETGKCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKLWDLRTGK---- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 246 hCVQTI----ASVARVKWRPECRHHLATCSmmvDHNIYVWDVRRPFVpAAMFEEHRDVTTGIAWrHPHDpSFLLSGSKDS 321
Cdd:cd00200  169 -CVATLtghtGEVNSVAFSPDGEKLLSSSS---DGTIKLWDLSTGKC-LGTLRGHENGVNSVAF-SPDG-YLLASGSEDG 241


                 ...
gi 300797517 322 TLC 324
Cdd:cd00200  242 TIR 244
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 116-323 6.25e-28

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 114.35  E-value: 6.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 116 FTEHKRTVNKVCFHPTEaHVLLSGSQDGFMKCFDLRRKDSVSTFSGQSESVRDVQFSiRDYFTFASTFENGNVQLWDIRR 195
Cdd:cd00200    5 LKGHTGGVTCVAFSPDG-KLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAAS-ADGTYLASGSSDKTIRLWDLET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 196 PdRCERMFTAHNGPVFCCDWHPeDRGWLATGGRDKMVKVWDMTTHRakeihCVQTI----ASVARVKWRPeCRHHLATCS 271
Cdd:cd00200   83 G-ECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKTIKVWDVETGK-----CLTTLrghtDWVNSVAFSP-DGTFVASSS 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 300797517 272 mmVDHNIYVWDVrRPFVPAAMFEEHRDVTTGIAWrHPhDPSFLLSGSKDSTL 323
Cdd:cd00200  155 --QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAF-SP-DGEKLLSSSSDGTI 201
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
 742-787 1.42e-26

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 (WDR24) and similar proteins; WDR24 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea3/WDR59, and Mio/Sea4. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. WDR24 contains an N-terminal WD40 domain and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type. Sea2 is the yeast counterpart of WDR24. It is not included in this subfamily.


Pssm-ID: 438354  Cd Length: 46  Bit Score: 102.36  E-value: 1.42e-26
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 300797517 742 MCAVCHHVVKGLFVWCQGCSHGGHLQHIMKWLEGSSHCPAGCGHLC 787
Cdd:cd16693    1 MCSVCHLPVKGLYVWCQGCGHGGHLEHMKEWFSTNSHCPAGCGHLC 46
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 79-236 1.74e-25

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 107.04  E-value: 1.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517  79 DVVWHQmDENLLATAATNGVVVTWNLGRPSRNKQdqlFTEHKRTVNKVCFHPTEAHvLLSGSQDGFMKCFDLRRKDSVST 158
Cdd:cd00200  140 SVAFSP-DGTFVASSSQDGTIKLWDLRTGKCVAT---LTGHTGEVNSVAFSPDGEK-LLSSSSDGTIKLWDLSTGKCLGT 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300797517 159 FSGQSESVRDVQFSIRDYFtFASTFENGNVQLWDIRrPDRCERMFTAHNGPVFCCDWHPeDRGWLATGGRDKMVKVWD 236
Cdd:cd00200  215 LRGHENGVNSVAFSPDGYL-LASGSEDGTIRVWDLR-TGECVQTLSGHTNSVTSLAWSP-DGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
65-323 4.81e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 105.38  E-value: 4.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517  65 LRVGRKPSLNLSCADVVWHQMDENLLATAATNGVVVTWNLGRPSRNKQDQLFTEHKRTVNKVCFHPtEAHVLLSGSQDGF 144
Cdd:COG2319   23 AALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSP-DGRLLASASADGT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 145 MKCFDLRRKDSVSTFSGQSESVRDVQFSiRDYFTFASTFENGNVQLWDIRRPdRCERMFTAHNGPVFCCDWHPeDRGWLA 224
Cdd:COG2319  102 VRLWDLATGLLLRTLTGHTGAVRSVAFS-PDGKTLASGSADGTVRLWDLATG-KLLRTLTGHSGAVTSVAFSP-DGKLLA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 225 TGGRDKMVKVWDMTTHRakeihCVQTI----ASVARVKWRPEcRHHLATCSMmvDHNIYVWDVRRPfVPAAMFEEHRDVT 300
Cdd:COG2319  179 SGSDDGTVRLWDLATGK-----LLRTLtghtGAVRSVAFSPD-GKLLASGSA--DGTVRLWDLATG-KLLRTLTGHSGSV 249

                        250       260
                 ....*....|....*....|...
gi 300797517 301 TGIAWrHPhDPSFLLSGSKDSTL 323
Cdd:COG2319  250 RSVAF-SP-DGRLLASGSADGTV 270
WD40 COG2319
WD40 repeat [General function prediction only];
79-239 4.56e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 96.52  E-value: 4.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517  79 DVVWHQmDENLLATAATNGVVVTWNLgrpSRNKQDQLFTEHKRTVNKVCFHPtEAHVLLSGSQDGFMKCFDLRRKDSVST 158
Cdd:COG2319  251 SVAFSP-DGRLLASGSADGTVRLWDL---ATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLRT 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 159 FSGQSESVRDVQFSiRDYFTFASTFENGNVQLWDIRRPdRCERMFTAHNGPVFCCDWHPEDRgWLATGGRDKMVKVWDMT 238
Cdd:COG2319  326 LTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATG-ELLRTLTGHTGAVTSVAFSPDGR-TLASGSADGTVRLWDLA 402


                 .
gi 300797517 239 T 239
Cdd:COG2319  403 T 403
mRING-H2-C3H3C2_Mio-like cd16488
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 742-785 7.19e-17

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and its homologs; This subfamily contains Mio, WDR24, WDR59, and their counterparts Sea4, Sea2, and Sea3 from yeast, respectively. Mio/Sea4, Sea2/WDR24, and Sea3/WDR59 are components of the GATOR2 complex, which also includes another two subunits, Seh1and Sec13. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. All subfamily members contain an N-terminal WD40 domain and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type.


Pssm-ID: 438151 [Multi-domain]  Cd Length: 44  Bit Score: 74.67  E-value: 7.19e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 300797517 742 MCAVCHHVVKGLFVWCQGCSHGGHLQHIMKWLEGSSHCPAGCGH 785
Cdd:cd16488    1 SCAICHLPVKGLSSFCLNCGHGGHAECIREWFEDHTECPTGCGC 44
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 199-335 1.47e-14

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 75.06  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 199 CERMFTAHNGPVFCCDWHPeDRGWLATGGRDKMVKVWDMTTHRAKE-----IHCVQTIASVARVKWrpecrhhLATCSMm 273
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRtlkghTGPVRDVAASADGTY-------LASGSS- 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300797517 274 vDHNIYVWDVRRPfVPAAMFEEHRDVTTGIAWrHPHDPsFLLSGSKDSTL---------CQHLFRDASQPV 335
Cdd:cd00200   72 -DKTIRLWDLETG-ECVRTLTGHTSYVSSVAF-SPDGR-ILSSSSRDKTIkvwdvetgkCLTTLRGHTDWV 138
mRING-H2-C3H3C2_WDR59 cd16692
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 ...
 743-787 5.93e-12

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 (WDR59) and similar proteins; WDR59 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea2/WDR24, and Mio/Sea4. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. WDR59 contains an N-terminal WD40 domain followed by a RWD domain, and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type. Sea3 is the yeast counterpart of WDR59. It is not included in this subfamily.


Pssm-ID: 438353  Cd Length: 47  Bit Score: 60.86  E-value: 5.93e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 300797517 743 CAVCHHVVKGLFVWCQGCSHGGHLQHIMKWLEGSSHCPAGCGHLC 787
Cdd:cd16692    3 CAICHVAVRGSSNFCLACGHGGHTSHMMEWFRTQDVCPTGCGCHC 47
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 180-323 1.44e-09

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 61.64  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 180 ASTFEnGNVQLWDIRRPDRCERMfTAHNGPVFCCDWHPEDRGWLATGGRDKMVKVWdmTTHRAKEIHCVQTIASVARVKW 259
Cdd:PLN00181 550 SSNFE-GVVQVWDVARSQLVTEM-KEHEKRVWSIDYSSADPTLLASGSDDGSVKLW--SINQGVSIGTIKTKANICCVQF 625

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300797517 260 RPECRHHLATCSmmVDHNIYVWDVRRPFVP-AAMFEEHRDVTtgiaWRHPHDPSFLLSGSKDSTL 323
Cdd:PLN00181 626 PSESGRSLAFGS--ADHKVYYYDLRNPKLPlCTMIGHSKTVS----YVRFVDSSTLVSSSTDNTL 684
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 198-236 4.19e-08

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 49.62  E-value: 4.19e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 300797517   198 RCERMFTAHNGPVFCCDWHPeDRGWLATGGRDKMVKVWD 236
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
198-236 9.13e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 48.88  E-value: 9.13e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 300797517  198 RCERMFTAHNGPVFCCDWHPEDRgWLATGGRDKMVKVWD 236
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGK-LLASGSDDGTVKVWD 39
mRING-H2-C3H3C2_Mio cd16691
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 754-783 1.57e-07

Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and simialr proteins; This family contains Mio,its counterpart Sea4 from yeast, and other homologs. Mio/Sea4 is a component of the GATOR2 complex, which also includes another four subunits, Seh1, Sec13, Sea2/WDR24, and Sea3/WDR59. GATOR2 and GATOR1, which is composed of three subunits, DEPDC5, Nprl2, and Nprl3, form the Rag-interacting complex GATOR (GAP Activity Towards Rags). Inhibition of GATOR1 subunits makes mTORC1 signaling resistant to amino acid deprivation. In contrast, inhibition of GATOR2 subunits suppresses mTORC1 signaling and GATOR2 negatively regulates DEPDC5. Mio interacts with endogenous RagA and RagC, and plays an essential role in the activation of mTOR Complex 1 (mTORC1) by amino acids. In GATOR2, Mio and Seh1 localize to lysosomes and autolysosomes, and form a heterodimer that is required to oppose the TORC1 inhibitory activity of the Iml1/GATOR1 complex to prevent the constitutive down-regulation of TORC1 activity in later stages of oogenesis. A tissue-specific requirement is necessary for Mio to be involved in cell growth in the female germ line. Mio contains an N-terminal WD40 domain and a C-terminal RING-H2 finger with an unusual arrangement of zinc-coordinating residues. The cysteines and histidines in the RING-H2 finger are arranged as a modified C3H3C2-type, rather than the canonical C3H2C3-type.


Pssm-ID: 438352  Cd Length: 75  Bit Score: 49.37  E-value: 1.57e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 300797517 754 FVWCQGCSHGGHLQHIMKWLEGSSHCP-AGC 783
Cdd:cd16691   41 FTWCQTCRHGGHAGHLQEWFRDHSECPvSGC 71
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 78-238 4.06e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 47.39  E-value: 4.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517  78 ADVVWHQMDENLLATAATNGVVVTWNLGRpsrnkqDQLFTE---HKRTVNKVCFHPTEAHVLLSGSQDGFMKCFDLRRKD 154
Cdd:PLN00181 536 SGICWNSYIKSQVASSNFEGVVQVWDVAR------SQLVTEmkeHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGV 609

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 155 SVSTFSGQSeSVRDVQFSIRDYFTFASTFENGNVQLWDIRRPDRCERMFTAHNGPVFCCDWhpEDRGWLATGGRDKMVKV 234
Cdd:PLN00181 610 SIGTIKTKA-NICCVQFPSESGRSLAFGSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRF--VDSSTLVSSSTDNTLKL 686


                 ....
gi 300797517 235 WDMT 238
Cdd:PLN00181 687 WDLS 690
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
 743-780 4.12e-04

H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438112 [Multi-domain]  Cd Length: 43  Bit Score: 38.54  E-value: 4.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 300797517 743 CAVCHHVVK-GLFVWCQGCSHGGHLQHIMKWLEGSSH-CP 780
Cdd:cd16448    1 CVICLEEFEeGDVVRLLPCGHVFHLACILRWLESGNNtCP 40
zf-RING_16 pfam17120
RING/Ubox like zinc-binding domain;
742-787 7.28e-04

RING/Ubox like zinc-binding domain;


Pssm-ID: 375001  Cd Length: 57  Bit Score: 38.15  E-value: 7.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 300797517  742 MCAVCHHVVKGLFVWCQGCSHGGHLQHIMKWLE-GSSHCPAGCGHLC 787
Cdd:pfam17120   6 SCNYCCLRVRGRVFLCGVCQHVLHASCAREWWEnDDGECPSGCGCNC 52
PTZ00420 PTZ00420
coronin; Provisional
 152-285 7.97e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 43.01  E-value: 7.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 152 RKDSVSTFSGQSESVRDVQFSIRDYFTFASTFENGNVQLWDIRRPDRCER-------MFTAHNGPVFCCDWHPEDRGWLA 224
Cdd:PTZ00420  63 RKPPVIKLKGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHNDESVKeikdpqcILKGHKKKISIIDWNPMNYYIMC 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300797517 225 TGGRDKMVKVWDMTTH-RAKEIHCVQTIASvarVKWRPECRHHLATCsmmVDHNIYVWDVRR 285
Cdd:PTZ00420 143 SSGFDSFVNIWDIENEkRAFQINMPKKLSS---LKWNIKGNLLSGTC---VGKHMHIIDPRK 198
PTZ00421 PTZ00421
coronin; Provisional
 79-197 1.80e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 41.80  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517  79 DVVWHQMDENLLATAATNGVVVTWNLGRP--SRNKQDQL--FTEHKRTVNKVCFHPTEAHVLLSGSQDGFMKCFDLRRKD 154
Cdd:PTZ00421  80 DVAFNPFDPQKLFTASEDGTIMGWGIPEEglTQNISDPIvhLQGHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERGK 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 300797517 155 SVSTFSGQSESVRDVQFSIRDYFtFASTFENGNVQLWDIRRPD 197
Cdd:PTZ00421 160 AVEVIKCHSDQITSLEWNLDGSL-LCTTSKDKKLNIIDPRDGT 201
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
102-199 4.15e-03

Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];


Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 40.40  E-value: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 102 WNLGRPsrnkqDQLFT----------EHKRTVNKVCFHPTEAHVLLSGSQDGFMKCFDLRRK----------------DS 155
Cdd:COG5170  198 WNLEII-----DGSFNivdikphnmeELTEVITSAEFHPEMCNVFMYSSSKGEIKLNDLRQSalcdnskklfeltidgVD 272

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 300797517 156 VSTFSGQSESVRDVQFS-------IRDYFTfastfengnVQLWDIRRPDRC 199
Cdd:COG5170  273 VDFFEEIVSSISDFKFSdngryilSRDYLT---------VKIWDVNMAKNP 314
PTZ00421 PTZ00421
coronin; Provisional
 161-245 6.09e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 39.88  E-value: 6.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300797517 161 GQSESVRDVQFSIRDYFTFASTFENGNVQLWDIRRPDRCERM------FTAHNGPVFCCDWHPEDRGWLATGGRDKMVKV 234
Cdd:PTZ00421  73 GQEGPIIDVAFNPFDPQKLFTASEDGTIMGWGIPEEGLTQNIsdpivhLQGHTKKVGIVSFHPSAMNVLASAGADMVVNV 152

                         90
                 ....*....|.
gi 300797517 235 WDMTTHRAKEI 245
Cdd:PTZ00421 153 WDVERGKAVEV 163
 
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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