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Conserved domains on  [gi|47085783|ref|NP_998228|]
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GATOR2 complex protein WDR24 [Danio rerio]

Protein Classification

RING finger and WD40 repeat domain-containing protein( domain architecture ID 13235784)

RING finger and WD40 repeat domain-containing protein similar to Homo sapiens GATOR complex protein WDR24 and Saccharomyces cerevisiae restriction of telomere capping protein 1 (RTC1)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 82-318 1.15e-33

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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 130.92  E-value: 1.15e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  82 NLLATAATNGAVVTWNLSRpcrNKQEQLFTEHKRTVNKVCFHPTEvNMLLSGSQDGFMKCFDLRKKESVSTFSGQSESVR 161
Cdd:cd00200  22 KLLATGSGDGTIKVWDLET---GELLRTLKGHTGPVRDVAASADG-TYLASGSSDKTIRLWDLETGECVRTLTGHTSYVS 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 162 DVQFSmKDYFTFAASFENGNVQLWDIRrPDRYERMFTAHTGPVFCCDWHPeDRGWLATGGRDKMVKVWDMSTNRvkeiyC 241
Cdd:cd00200  98 SVAFS-PDGRILSSSSRDKTIKVWDVE-TGKCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKLWDLRTGK-----C 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 242 VQTF----ASVARVKWRPERRyHLATCSMmvDHNIYVWDVRRpFIPFATFEEHKDVTTGIVWrhQHDPYFLLSGSKDSTL 317
Cdd:cd00200 170 VATLtghtGEVNSVAFSPDGE-KLLSSSS--DGTIKLWDLST-GKCLGTLRGHENGVNSVAF--SPDGYLLASGSEDGTI 243


                .
gi 47085783 318 Y 318
Cdd:cd00200 244 R 244
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
 731-776 4.49e-27

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: 103.90  E-value: 4.49e-27
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 47085783 731 VCAVCHHVVKGLFVWCQGCSHGGHLEHVMEWLKQSKHCPAGCGHLC 776
Cdd:cd16693   1 MCSVCHLPVKGLYVWCQGCGHGGHLEHMKEWFSTNSHCPAGCGHLC 46
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 82-318 1.15e-33

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: 130.92  E-value: 1.15e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  82 NLLATAATNGAVVTWNLSRpcrNKQEQLFTEHKRTVNKVCFHPTEvNMLLSGSQDGFMKCFDLRKKESVSTFSGQSESVR 161
Cdd:cd00200  22 KLLATGSGDGTIKVWDLET---GELLRTLKGHTGPVRDVAASADG-TYLASGSSDKTIRLWDLETGECVRTLTGHTSYVS 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 162 DVQFSmKDYFTFAASFENGNVQLWDIRrPDRYERMFTAHTGPVFCCDWHPeDRGWLATGGRDKMVKVWDMSTNRvkeiyC 241
Cdd:cd00200  98 SVAFS-PDGRILSSSSRDKTIKVWDVE-TGKCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKLWDLRTGK-----C 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 242 VQTF----ASVARVKWRPERRyHLATCSMmvDHNIYVWDVRRpFIPFATFEEHKDVTTGIVWrhQHDPYFLLSGSKDSTL 317
Cdd:cd00200 170 VATLtghtGEVNSVAFSPDGE-KLLSSSS--DGTIKLWDLST-GKCLGTLRGHENGVNSVAF--SPDGYLLASGSEDGTI 243


                .
gi 47085783 318 Y 318
Cdd:cd00200 244 R 244
WD40 COG2319
WD40 repeat [General function prediction only];
18-317 6.85e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 122.71  E-value: 6.85e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  18 HLDAPANAISVCRDATQVVVAGRNIFKIYGLEEDGFVERLNLRVGRKPSLNFSCADvmwhqmeeNLLATAATNGAVVTWN 97
Cdd:COG2319  35 LAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDG--------RLLASASADGTVRLWD 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  98 LSRPcrnKQEQLFTEHKRTVNKVCFHPTEvNMLLSGSQDGFMKCFDLRKKESVSTFSGQSESVRDVQFSmKDYFTFAASF 177
Cdd:COG2319 107 LATG---LLLRTLTGHTGAVRSVAFSPDG-KTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFS-PDGKLLASGS 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 178 ENGNVQLWDIRRpDRYERMFTAHTGPVFCCDWHPeDRGWLATGGRDKMVKVWDMSTNRvkeiyCVQTF----ASVARVKW 253
Cdd:COG2319 182 DDGTVRLWDLAT-GKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLATGK-----LLRTLtghsGSVRSVAF 254

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47085783 254 RPERRYhLATCSMmvDHNIYVWDVRRPFIPfATFEEHKDVTTGIVWRhqHDPYFLLSGSKDSTL 317
Cdd:COG2319 255 SPDGRL-LASGSA--DGTVRLWDLATGELL-RTLTGHSGGVNSVAFS--PDGKLLASGSDDGTV 312
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
 731-776 4.49e-27

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: 103.90  E-value: 4.49e-27
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 47085783 731 VCAVCHHVVKGLFVWCQGCSHGGHLEHVMEWLKQSKHCPAGCGHLC 776
Cdd:cd16693   1 MCSVCHLPVKGLYVWCQGCGHGGHLEHMKEWFSTNSHCPAGCGHLC 46
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 174-317 1.62e-09

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 61.64  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  174 AASFENGNVQLWDIRRPDRYERMfTAHTGPVFCCDWHPEDRGWLATGGRDKMVKVWdmSTNRVKEIYCVQTFASVARVKW 253
Cdd:PLN00181 549 ASSNFEGVVQVWDVARSQLVTEM-KEHEKRVWSIDYSSADPTLLASGSDDGSVKLW--SINQGVSIGTIKTKANICCVQF 625

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47085783  254 RPERRYHLATCSmmVDHNIYVWDVRRPFIPFATFEEHKDVTTGIVWRhqhDPYFLLSGSKDSTL 317
Cdd:PLN00181 626 PSESGRSLAFGS--ADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFV---DSSTLVSSSTDNTL 684
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 195-230 4.43e-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: 4.43e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 47085783    195 RMFTAHTGPVFCCDWHPeDRGWLATGGRDKMVKVWD 230
Cdd:smart00320   6 KTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
195-230 6.21e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 49.27  E-value: 6.21e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 47085783   195 RMFTAHTGPVFCCDWHPEDRgWLATGGRDKMVKVWD 230
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGK-LLASGSDDGTVKVWD 39
zinc_ribbon_16 pfam17034
Zinc-ribbon like family; This family is found at the C-terminus of WD40 repeat structures in ...
 718-776 1.43e-03

Zinc-ribbon like family; This family is found at the C-terminus of WD40 repeat structures in eukaryotes.


Pssm-ID: 374955  Cd Length: 125  Bit Score: 39.26  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783   718 KGWICDRCHQCASVCAVC----------------HHVVKGL----------FVWCQGCSHGGHLEHVMEWLKQSKHCP-A 770
Cdd:pfam17034  37 KSTLCPACSQPLPRCAVCglslgtsnltnkdsrrKSVVKDPqdfeklfekwFSFCLSCGHGSHADHATEWFSTHSICPvA 116


                  ....*.
gi 47085783   771 GCGHLC 776
Cdd:pfam17034 117 DCNCLC 122
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 82-318 1.15e-33

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: 130.92  E-value: 1.15e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  82 NLLATAATNGAVVTWNLSRpcrNKQEQLFTEHKRTVNKVCFHPTEvNMLLSGSQDGFMKCFDLRKKESVSTFSGQSESVR 161
Cdd:cd00200  22 KLLATGSGDGTIKVWDLET---GELLRTLKGHTGPVRDVAASADG-TYLASGSSDKTIRLWDLETGECVRTLTGHTSYVS 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 162 DVQFSmKDYFTFAASFENGNVQLWDIRrPDRYERMFTAHTGPVFCCDWHPeDRGWLATGGRDKMVKVWDMSTNRvkeiyC 241
Cdd:cd00200  98 SVAFS-PDGRILSSSSRDKTIKVWDVE-TGKCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKLWDLRTGK-----C 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 242 VQTF----ASVARVKWRPERRyHLATCSMmvDHNIYVWDVRRpFIPFATFEEHKDVTTGIVWrhQHDPYFLLSGSKDSTL 317
Cdd:cd00200 170 VATLtghtGEVNSVAFSPDGE-KLLSSSS--DGTIKLWDLST-GKCLGTLRGHENGVNSVAF--SPDGYLLASGSEDGTI 243


                .
gi 47085783 318 Y 318
Cdd:cd00200 244 R 244
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 110-317 2.38e-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: 124.37  E-value: 2.38e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 110 FTEHKRTVNKVCFHPtEVNMLLSGSQDGFMKCFDLRKKESVSTFSGQSESVRDVQFSmKDYFTFAASFENGNVQLWDIRR 189
Cdd:cd00200   5 LKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAAS-ADGTYLASGSSDKTIRLWDLET 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 190 PDRYeRMFTAHTGPVFCCDWHPeDRGWLATGGRDKMVKVWDMSTNRvkeiyCVQTF----ASVARVKWRPERRYhLATCS 265
Cdd:cd00200  83 GECV-RTLTGHTSYVSSVAFSP-DGRILSSSSRDKTIKVWDVETGK-----CLTTLrghtDWVNSVAFSPDGTF-VASSS 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 47085783 266 mmVDHNIYVWDVrRPFIPFATFEEHKDVTTGIVWRhqHDPYFLLSGSKDSTL 317
Cdd:cd00200 155 --QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAFS--PDGEKLLSSSSDGTI 201
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 82-317 1.06e-30

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: 122.44  E-value: 1.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  82 NLLATAATNGAVVTWNLSRPCRNKQeqlFTEHKRTVNKVCFHPTEvNMLLSGSQDGFMKCFDLRKKESVSTFSGQSESVR 161
Cdd:cd00200  64 TYLASGSSDKTIRLWDLETGECVRT---LTGHTSYVSSVAFSPDG-RILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVN 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 162 DVQFSMKDYFTFAASfENGNVQLWDIrRPDRYERMFTAHTGPVFCCDWHPeDRGWLATGGRDKMVKVWDMSTNRvkeiyC 241
Cdd:cd00200 140 SVAFSPDGTFVASSS-QDGTIKLWDL-RTGKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLSTGK-----C 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 242 VQTF----ASVARVKWRPERRYhLATCSMmvDHNIYVWDVrRPFIPFATFEEHKDVTTGIVWrHQHDPYfLLSGSKDSTL 317
Cdd:cd00200 212 LGTLrgheNGVNSVAFSPDGYL-LASGSE--DGTIRVWDL-RTGECVQTLSGHTNSVTSLAW-SPDGKR-LASGSADGTI 285
WD40 COG2319
WD40 repeat [General function prediction only];
18-317 6.85e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 122.71  E-value: 6.85e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  18 HLDAPANAISVCRDATQVVVAGRNIFKIYGLEEDGFVERLNLRVGRKPSLNFSCADvmwhqmeeNLLATAATNGAVVTWN 97
Cdd:COG2319  35 LAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDG--------RLLASASADGTVRLWD 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  98 LSRPcrnKQEQLFTEHKRTVNKVCFHPTEvNMLLSGSQDGFMKCFDLRKKESVSTFSGQSESVRDVQFSmKDYFTFAASF 177
Cdd:COG2319 107 LATG---LLLRTLTGHTGAVRSVAFSPDG-KTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFS-PDGKLLASGS 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 178 ENGNVQLWDIRRpDRYERMFTAHTGPVFCCDWHPeDRGWLATGGRDKMVKVWDMSTNRvkeiyCVQTF----ASVARVKW 253
Cdd:COG2319 182 DDGTVRLWDLAT-GKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLATGK-----LLRTLtghsGSVRSVAF 254

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47085783 254 RPERRYhLATCSMmvDHNIYVWDVRRPFIPfATFEEHKDVTTGIVWRhqHDPYFLLSGSKDSTL 317
Cdd:COG2319 255 SPDGRL-LASGSA--DGTVRLWDLATGELL-RTLTGHSGGVNSVAFS--PDGKLLASGSDDGTV 312
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
 731-776 4.49e-27

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: 103.90  E-value: 4.49e-27
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 47085783 731 VCAVCHHVVKGLFVWCQGCSHGGHLEHVMEWLKQSKHCPAGCGHLC 776
Cdd:cd16693   1 MCSVCHLPVKGLYVWCQGCGHGGHLEHMKEWFSTNSHCPAGCGHLC 46
WD40 COG2319
WD40 repeat [General function prediction only];
20-278 6.76e-27

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 113.85  E-value: 6.76e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  20 DAPANAISVCRDATQVVVAGR-NIFKIYGLEEDGFVERLNLRVGRKPSLNFScADvmwhqmeENLLATAATNGAVVTWNL 98
Cdd:COG2319 162 SGAVTSVAFSPDGKLLASGSDdGTVRLWDLATGKLLRTLTGHTGAVRSVAFS-PD-------GKLLASGSADGTVRLWDL 233

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  99 SRPcrnKQEQLFTEHKRTVNKVCFHPTEvNMLLSGSQDGFMKCFDLRKKESVSTFSGQSESVRDVQFSmKDYFTFAASFE 178
Cdd:COG2319 234 ATG---KLLRTLTGHSGSVRSVAFSPDG-RLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFS-PDGKLLASGSD 308

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 179 NGNVQLWDIRRPDRYeRMFTAHTGPVFCCDWHPeDRGWLATGGRDKMVKVWDMSTNRvkeiyCVQTF----ASVARVKWR 254
Cdd:COG2319 309 DGTVRLWDLATGKLL-RTLTGHTGAVRSVAFSP-DGKTLASGSDDGTVRLWDLATGE-----LLRTLtghtGAVTSVAFS 381

                       250       260
                ....*....|....*....|....
gi 47085783 255 PERRYhLATCSMmvDHNIYVWDVR 278
Cdd:COG2319 382 PDGRT-LASGSA--DGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 83-230 1.51e-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: 107.42  E-value: 1.51e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  83 LLATAATNGAVVTWNLS--RPCRNkqeqlFTEHKRTVNKVCFHPTEvNMLLSGSQDGFMKCFDLRKKESVSTFSGQSESV 160
Cdd:cd00200 149 FVASSSQDGTIKLWDLRtgKCVAT-----LTGHTGEVNSVAFSPDG-EKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGV 222

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 161 RDVQFSMKDYFtFAASFENGNVQLWDIRRPDRYeRMFTAHTGPVFCCDWHPeDRGWLATGGRDKMVKVWD 230
Cdd:cd00200 223 NSVAFSPDGYL-LASGSEDGTIRVWDLRTGECV-QTLSGHTNSVTSLAWSP-DGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
20-233 4.06e-22

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 99.60  E-value: 4.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  20 DAPANAISVCRDATQVVVAGR-NIFKIYGLEEDGFVERLNLRVGRKPSLNFScADvmwhqmeENLLATAATNGAVVTWNL 98
Cdd:COG2319 204 TGAVRSVAFSPDGKLLASGSAdGTVRLWDLATGKLLRTLTGHSGSVRSVAFS-PD-------GRLLASGSADGTVRLWDL 275

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  99 SRpcrNKQEQLFTEHKRTVNKVCFHPTEvNMLLSGSQDGFMKCFDLRKKESVSTFSGQSESVRDVQFSMKDYFTFAASfE 178
Cdd:COG2319 276 AT---GELLRTLTGHSGGVNSVAFSPDG-KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGS-D 350

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 47085783 179 NGNVQLWDIRRPDRYERmFTAHTGPVFCCDWHPEDRgWLATGGRDKMVKVWDMST 233
Cdd:COG2319 351 DGTVRLWDLATGELLRT-LTGHTGAVTSVAFSPDGR-TLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 195-317 7.05e-18

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: 84.69  E-value: 7.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783 195 RMFTAHTGPVFCCDWHPeDRGWLATGGRDKMVKVWDMSTNRVKEIYCVQTFaSVARVKWRPERRYhLATCSMmvDHNIYV 274
Cdd:cd00200   3 RTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTG-PVRDVAASADGTY-LASGSS--DKTIRL 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 47085783 275 WDVRRPfIPFATFEEHKDVTTGIVWrhQHDPYFLLSGSKDSTL 317
Cdd:cd00200  78 WDLETG-ECVRTLTGHTSYVSSVAF--SPDGRILSSSSRDKTI 117
mRING-H2-C3H3C2_Mio-like cd16488
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 732-774 1.99e-16

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: 73.52  E-value: 1.99e-16
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 47085783 732 CAVCHHVVKGLFVWCQGCSHGGHLEHVMEWLKQSKHCPAGCGH 774
Cdd:cd16488   2 CAICHLPVKGLSSFCLNCGHGGHAECIREWFEDHTECPTGCGC 44
mRING-H2-C3H3C2_WDR59 cd16692
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 ...
 732-776 2.09e-13

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: 65.10  E-value: 2.09e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 47085783 732 CAVCHHVVKGLFVWCQGCSHGGHLEHVMEWLKQSKHCPAGCGHLC 776
Cdd:cd16692   3 CAICHVAVRGSSNFCLACGHGGHTSHMMEWFRTQDVCPTGCGCHC 47
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 174-317 1.62e-09

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 61.64  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  174 AASFENGNVQLWDIRRPDRYERMfTAHTGPVFCCDWHPEDRGWLATGGRDKMVKVWdmSTNRVKEIYCVQTFASVARVKW 253
Cdd:PLN00181 549 ASSNFEGVVQVWDVARSQLVTEM-KEHEKRVWSIDYSSADPTLLASGSDDGSVKLW--SINQGVSIGTIKTKANICCVQF 625

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47085783  254 RPERRYHLATCSmmVDHNIYVWDVRRPFIPFATFEEHKDVTTGIVWRhqhDPYFLLSGSKDSTL 317
Cdd:PLN00181 626 PSESGRSLAFGS--ADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFV---DSSTLVSSSTDNTL 684
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 195-230 4.43e-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: 4.43e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 47085783    195 RMFTAHTGPVFCCDWHPeDRGWLATGGRDKMVKVWD 230
Cdd:smart00320   6 KTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
mRING-H2-C3H3C2_Mio cd16691
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 743-772 5.70e-08

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: 50.52  E-value: 5.70e-08
                        10        20        30
                ....*....|....*....|....*....|.
gi 47085783 743 FVWCQGCSHGGHLEHVMEWLKQSKHCP-AGC 772
Cdd:cd16691  41 FTWCQTCRHGGHAGHLQEWFRDHSECPvSGC 71
WD40 pfam00400
WD domain, G-beta repeat;
195-230 6.21e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 49.27  E-value: 6.21e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 47085783   195 RMFTAHTGPVFCCDWHPEDRgWLATGGRDKMVKVWD 230
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGK-LLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 25-232 1.61e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 48.54  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783   25 AISVCRDATQVVVAGRN----IFKIYGLEEDGF-VERLNLRVGRKPSLNFSCadvmWHQMEENLLATAATNGAVVTWNLS 99
Cdd:PLN00181 488 AIGFDRDGEFFATAGVNkkikIFECESIIKDGRdIHYPVVELASRSKLSGIC----WNSYIKSQVASSNFEGVVQVWDVA 563

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  100 RpcrnkqEQLFTE---HKRTVNKVCFHPTEVNMLLSGSQDGFMKCFDLRKKESVSTFSGQSeSVRDVQFSMKDYFTFAAS 176
Cdd:PLN00181 564 R------SQLVTEmkeHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKA-NICCVQFPSESGRSLAFG 636

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 47085783  177 FENGNVQLWDIRRPDRYERMFTAHTGPVFCCDWhpEDRGWLATGGRDKMVKVWDMS 232
Cdd:PLN00181 637 SADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRF--VDSSTLVSSSTDNTLKLWDLS 690
zinc_ribbon_16 pfam17034
Zinc-ribbon like family; This family is found at the C-terminus of WD40 repeat structures in ...
 718-776 1.43e-03

Zinc-ribbon like family; This family is found at the C-terminus of WD40 repeat structures in eukaryotes.


Pssm-ID: 374955  Cd Length: 125  Bit Score: 39.26  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783   718 KGWICDRCHQCASVCAVC----------------HHVVKGL----------FVWCQGCSHGGHLEHVMEWLKQSKHCP-A 770
Cdd:pfam17034  37 KSTLCPACSQPLPRCAVCglslgtsnltnkdsrrKSVVKDPqdfeklfekwFSFCLSCGHGSHADHATEWFSTHSICPvA 116


                  ....*.
gi 47085783   771 GCGHLC 776
Cdd:pfam17034 117 DCNCLC 122
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 105-143 1.68e-03

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: 36.91  E-value: 1.68e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 47085783    105 KQEQLFTEHKRTVNKVCFHPTEvNMLLSGSQDGFMKCFD 143
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDG-KYLASGSDDGTIKLWD 40
zf-RING_16 pfam17120
RING/Ubox like zinc-binding domain;
732-776 2.36e-03

RING/Ubox like zinc-binding domain;


Pssm-ID: 375001  Cd Length: 57  Bit Score: 37.00  E-value: 2.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 47085783   732 CAVCHHVVKGLFVWCQGCSHGGHLEHVMEWLKQS-KHCPAGCGHLC 776
Cdd:pfam17120   7 CNYCCLRVRGRVFLCGVCQHVLHASCAREWWENDdGECPSGCGCNC 52
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
 732-769 2.49e-03

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: 36.23  E-value: 2.49e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 47085783 732 CAVCHHVVK-GLFVWCQGCSHGGHLEHVMEWLK-QSKHCP 769
Cdd:cd16448   1 CVICLEEFEeGDVVRLLPCGHVFHLACILRWLEsGNNTCP 40
WD40 pfam00400
WD domain, G-beta repeat;
104-143 4.35e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.40  E-value: 4.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 47085783   104 NKQEQLFTEHKRTVNKVCFHPTEvNMLLSGSQDGFMKCFD 143
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDG-KLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 155-239 9.13e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 39.49  E-value: 9.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085783  155 GQSESVRDVQFS-MKDYFTFAASfENGNVQLWDIRRPDRYERM------FTAHTGPVFCCDWHPEDRGWLATGGRDKMVK 227
Cdd:PTZ00421  73 GQEGPIIDVAFNpFDPQKLFTAS-EDGTIMGWGIPEEGLTQNIsdpivhLQGHTKKVGIVSFHPSAMNVLASAGADMVVN 151

                         90
                 ....*....|..
gi 47085783  228 VWDMSTNRVKEI 239
Cdd:PTZ00421 152 VWDVERGKAVEV 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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