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Conserved domains on  [gi|28572024|ref|NP_651720|]
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WD repeat domain 24, isoform B [Drosophila melanogaster]

Protein Classification

WD40 and mRING-H2-C3H3C2_WDR24 domain-containing protein( domain architecture ID 11525911)

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 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 13-311 7.41e-39

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: 145.94  E-value: 7.41e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024  13 LRICLEGHAN---ALALNKDNNQIALAGR-SLLKVYSINsngfTESCNMRGKNQNLSYsaNDVAWStLDSNLLATAATNG 88
Cdd:cd00200   1 LRRTLKGHTGgvtCVAFSPDGKLLATGSGdGTIKVWDLE----TGELLRTLKGHTGPV--RDVAAS-ADGTYLASGSSDK 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024  89 VVSVWDLSKfgrQKQLLVYNEHERTAHTVTFHSSEPnILISGSQDGTIKCFDIRSDKSINTYFCNSESVRDVKFSPHTQN 168
Cdd:cd00200  74 TIRLWDLET---GECVRTLTGHTSYVSSVAFSPDGR-ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024 169 IFSAvSENGTVQLWDMRKWdKCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWNMD-GRPGLEHTIHTIAVVGrVK 247
Cdd:cd00200 150 VASS-SQDGTIKLWDLRTG-KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLStGKCLGTLRGHENGVNS-VA 226

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28572024 248 WRPERtYHIASCAlvVDYSVHVWDIRRPYIPfASFNEHTNVTTGIAWQGsDSHCLLSISKDSTI 311
Cdd:cd00200 227 FSPDG-YLLASGS--EDGTIRVWDLRTGECV-QTLSGHTNSVTSLAWSP-DGKRLASGSADGTI 285
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
 729-773 2.04e-21

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: 87.72  E-value: 2.04e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 28572024 729 KCCVCGLIVRGVYAWCQGCSHGGHIEHLQKYFAKHSKCPK-CGHLC 773
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 ...
 13-311 7.41e-39

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: 145.94  E-value: 7.41e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024  13 LRICLEGHAN---ALALNKDNNQIALAGR-SLLKVYSINsngfTESCNMRGKNQNLSYsaNDVAWStLDSNLLATAATNG 88
Cdd:cd00200   1 LRRTLKGHTGgvtCVAFSPDGKLLATGSGdGTIKVWDLE----TGELLRTLKGHTGPV--RDVAAS-ADGTYLASGSSDK 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024  89 VVSVWDLSKfgrQKQLLVYNEHERTAHTVTFHSSEPnILISGSQDGTIKCFDIRSDKSINTYFCNSESVRDVKFSPHTQN 168
Cdd:cd00200  74 TIRLWDLET---GECVRTLTGHTSYVSSVAFSPDGR-ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024 169 IFSAvSENGTVQLWDMRKWdKCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWNMD-GRPGLEHTIHTIAVVGrVK 247
Cdd:cd00200 150 VASS-SQDGTIKLWDLRTG-KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLStGKCLGTLRGHENGVNS-VA 226

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28572024 248 WRPERtYHIASCAlvVDYSVHVWDIRRPYIPfASFNEHTNVTTGIAWQGsDSHCLLSISKDSTI 311
Cdd:cd00200 227 FSPDG-YLLASGS--EDGTIRVWDLRTGECV-QTLSGHTNSVTSLAWSP-DGKRLASGSADGTI 285
WD40 COG2319
WD40 repeat [General function prediction only];
7-273 3.61e-35

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 138.51  E-value: 3.61e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024   7 DTSTISLRICLEGHA---NALALNKDNNQIALAGR-SLLKVYSINSNGFTEScnMRGKNQnlsySANDVAWSTlDSNLLA 82
Cdd:COG2319 148 DLATGKLLRTLTGHSgavTSVAFSPDGKLLASGSDdGTVRLWDLATGKLLRT--LTGHTG----AVRSVAFSP-DGKLLA 220

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024  83 TAATNGVVSVWDLSkfgRQKQLLVYNEHERTAHTVTFhSSEPNILISGSQDGTIKCFDIRSDKSINTYFCNSESVRDVKF 162
Cdd:COG2319 221 SGSADGTVRLWDLA---TGKLLRTLTGHSGSVRSVAF-SPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAF 296

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024 163 SPHTQNIFSAvSENGTVQLWDMRKWdKCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWNMDGRpGLEHTI--HTi 240
Cdd:COG2319 297 SPDGKLLASG-SDDGTVRLWDLATG-KLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG-ELLRTLtgHT- 372

                       250       260       270
                ....*....|....*....|....*....|...
gi 28572024 241 AVVGRVKWRPERTYhIASCALvvDYSVHVWDIR 273
Cdd:COG2319 373 GAVTSVAFSPDGRT-LASGSA--DGTVRLWDLA 402
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
 729-773 2.04e-21

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: 87.72  E-value: 2.04e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 28572024 729 KCCVCGLIVRGVYAWCQGCSHGGHIEHLQKYFAKHSKCPK-CGHLC 773
Cdd:cd16693   1 MCSVCHLPVKGLYVWCQGCGHGGHLEHMKEWFSTNSHCPAgCGHLC 46
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 23-227 3.45e-10

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 63.57  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024   23 ALALNKDNNQIALAG-RSLLKVYSINSngftescnMRGKNQNLSYSANDVA---------WSTLDSNLLATAATNGVVSV 92
Cdd:PLN00181 488 AIGFDRDGEFFATAGvNKKIKIFECES--------IIKDGRDIHYPVVELAsrsklsgicWNSYIKSQVASSNFEGVVQV 559

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024   93 WDLSkfgRQKQLLVYNEHERTAHTVTFHSSEPNILISGSQDGTIKCFDIRSDKSINTyFCNSESVRDVKFSPHTQNIFSA 172
Cdd:PLN00181 560 WDVA---RSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGT-IKTKANICCVQFPSESGRSLAF 635

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 28572024  173 VSENGTVQLWDMRKWDKCMVQFTAHYGPVYTCDWHPTRNwLATGSRDKQIKVWNM 227
Cdd:PLN00181 636 GSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFVDSST-LVSSSTDNTLKLWDL 689
WD40 pfam00400
WD domain, G-beta repeat;
189-226 3.27e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 3.27e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 28572024   189 KCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWN 226
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 189-226 5.69e-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: 49.23  E-value: 5.69e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 28572024    189 KCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWN 226
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
zinc_ribbon_16 pfam17034
Zinc-ribbon like family; This family is found at the C-terminus of WD40 repeat structures in ...
 719-776 4.44e-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: 38.10  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024   719 CDKCkSMQSAKCCVCGL----------------IVRGV----------YAWCQGCSHGGHIEHLQKYFAKHSKCP--KCG 770
Cdd:pfam17034  41 CPAC-SQPLPRCAVCGLslgtsnltnkdsrrksVVKDPqdfeklfekwFSFCLSCGHGSHADHATEWFSTHSICPvaDCN 119


                  ....*.
gi 28572024   771 HLCAYS 776
Cdd:pfam17034 120 CLCREK 125
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 13-311 7.41e-39

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: 145.94  E-value: 7.41e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024  13 LRICLEGHAN---ALALNKDNNQIALAGR-SLLKVYSINsngfTESCNMRGKNQNLSYsaNDVAWStLDSNLLATAATNG 88
Cdd:cd00200   1 LRRTLKGHTGgvtCVAFSPDGKLLATGSGdGTIKVWDLE----TGELLRTLKGHTGPV--RDVAAS-ADGTYLASGSSDK 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024  89 VVSVWDLSKfgrQKQLLVYNEHERTAHTVTFHSSEPnILISGSQDGTIKCFDIRSDKSINTYFCNSESVRDVKFSPHTQN 168
Cdd:cd00200  74 TIRLWDLET---GECVRTLTGHTSYVSSVAFSPDGR-ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024 169 IFSAvSENGTVQLWDMRKWdKCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWNMD-GRPGLEHTIHTIAVVGrVK 247
Cdd:cd00200 150 VASS-SQDGTIKLWDLRTG-KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLStGKCLGTLRGHENGVNS-VA 226

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28572024 248 WRPERtYHIASCAlvVDYSVHVWDIRRPYIPfASFNEHTNVTTGIAWQGsDSHCLLSISKDSTI 311
Cdd:cd00200 227 FSPDG-YLLASGS--EDGTIRVWDLRTGECV-QTLSGHTNSVTSLAWSP-DGKRLASGSADGTI 285
WD40 COG2319
WD40 repeat [General function prediction only];
7-273 3.61e-35

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 138.51  E-value: 3.61e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024   7 DTSTISLRICLEGHA---NALALNKDNNQIALAGR-SLLKVYSINSNGFTEScnMRGKNQnlsySANDVAWSTlDSNLLA 82
Cdd:COG2319 148 DLATGKLLRTLTGHSgavTSVAFSPDGKLLASGSDdGTVRLWDLATGKLLRT--LTGHTG----AVRSVAFSP-DGKLLA 220

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024  83 TAATNGVVSVWDLSkfgRQKQLLVYNEHERTAHTVTFhSSEPNILISGSQDGTIKCFDIRSDKSINTYFCNSESVRDVKF 162
Cdd:COG2319 221 SGSADGTVRLWDLA---TGKLLRTLTGHSGSVRSVAF-SPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAF 296

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024 163 SPHTQNIFSAvSENGTVQLWDMRKWdKCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWNMDGRpGLEHTI--HTi 240
Cdd:COG2319 297 SPDGKLLASG-SDDGTVRLWDLATG-KLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG-ELLRTLtgHT- 372

                       250       260       270
                ....*....|....*....|....*....|...
gi 28572024 241 AVVGRVKWRPERTYhIASCALvvDYSVHVWDIR 273
Cdd:COG2319 373 GAVTSVAFSPDGRT-LASGSA--DGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
7-229 4.65e-31

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 126.18  E-value: 4.65e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024   7 DTSTISLRICLEGHA---NALALNKDNNQIALAGR-SLLKVYSINSNgfTESCNMRGKnqnlSYSANDVAWSTlDSNLLA 82
Cdd:COG2319 190 DLATGKLLRTLTGHTgavRSVAFSPDGKLLASGSAdGTVRLWDLATG--KLLRTLTGH----SGSVRSVAFSP-DGRLLA 262

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024  83 TAATNGVVSVWDLSkfgRQKQLLVYNEHERTAHTVTFhSSEPNILISGSQDGTIKCFDIRSDKSINTYFCNSESVRDVKF 162
Cdd:COG2319 263 SGSADGTVRLWDLA---TGELLRTLTGHSGGVNSVAF-SPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAF 338

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28572024 163 SPHTQNIFSAvSENGTVQLWDMRKWdKCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWNMDG 229
Cdd:COG2319 339 SPDGKTLASG-SDDGTVRLWDLATG-ELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 7-226 1.03e-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: 1.03e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024   7 DTSTISLRICLEGHA---NALALNKDNnQIALAGRSL--LKVYSINSNGFTEScnMRGKNQnlsySANDVAWSTlDSNLL 81
Cdd:cd00200  79 DLETGECVRTLTGHTsyvSSVAFSPDG-RILSSSSRDktIKVWDVETGKCLTT--LRGHTD----WVNSVAFSP-DGTFV 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024  82 ATAATNGVVSVWDLSKFGRQKQLLvynEHERTAHTVTFHSSEPNiLISGSQDGTIKCFDIRSDKSINTYFCNSESVRDVK 161
Cdd:cd00200 151 ASSSQDGTIKLWDLRTGKCVATLT---GHTGEVNSVAFSPDGEK-LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVA 226

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28572024 162 FSPHtQNIFSAVSENGTVQLWDMRKWdKCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWN 226
Cdd:cd00200 227 FSPD-GYLLASGSEDGTIRVWDLRTG-ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
mRING-H2-C3H3C2_WDR24 cd16693
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 24 ...
 729-773 2.04e-21

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: 87.72  E-value: 2.04e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 28572024 729 KCCVCGLIVRGVYAWCQGCSHGGHIEHLQKYFAKHSKCPK-CGHLC 773
Cdd:cd16693   1 MCSVCHLPVKGLYVWCQGCGHGGHLEHMKEWFSTNSHCPAgCGHLC 46
WD40 COG2319
WD40 repeat [General function prediction only];
75-311 6.56e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.81  E-value: 6.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024  75 TLDSNLLATAATNGVVSVWDLSKFGRQKQLLvyneHERTAHTVTFHSSEPNILISGSQDGTIKCFDIRSDKSINTYFCNS 154
Cdd:COG2319   3 SADGAALAAASADLALALLAAALGALLLLLL----GLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024 155 ESVRDVKFSPHTQNIFSAvSENGTVQLWDMRKWdKCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWNM-DGRPGL 233
Cdd:COG2319  79 AAVLSVAFSPDGRLLASA-SADGTVRLWDLATG-LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLaTGKLLR 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28572024 234 EHTIHTIAVVGrVKWRPERTYhIASCALvvDYSVHVWDIRRPyIPFASFNEHTNVTTGIAWqGSDSHCLLSISKDSTI 311
Cdd:COG2319 157 TLTGHSGAVTS-VAFSPDGKL-LASGSD--DGTVRLWDLATG-KLLRTLTGHTGAVRSVAF-SPDGKLLASGSADGTV 228
mRING-H2-C3H3C2_WDR59 cd16692
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein 59 ...
 729-773 6.90e-11

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: 57.78  E-value: 6.90e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 28572024 729 KCCVCGLIVRGVYAWCQGCSHGGHIEHLQKYFAKHSKCPK-CGHLC 773
Cdd:cd16692   2 QCAICHVAVRGSSNFCLACGHGGHTSHMMEWFRTQDVCPTgCGCHC 47
mRING-H2-C3H3C2_Mio-like cd16488
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 729-771 1.24e-10

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: 56.95  E-value: 1.24e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 28572024 729 KCCVCGLIVRGVYAWCQGCSHGGHIEHLQKYFAKHSKCPK-CGH 771
Cdd:cd16488   1 SCAICHLPVKGLSSFCLNCGHGGHAECIREWFEDHTECPTgCGC 44
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 23-227 3.45e-10

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 63.57  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024   23 ALALNKDNNQIALAG-RSLLKVYSINSngftescnMRGKNQNLSYSANDVA---------WSTLDSNLLATAATNGVVSV 92
Cdd:PLN00181 488 AIGFDRDGEFFATAGvNKKIKIFECES--------IIKDGRDIHYPVVELAsrsklsgicWNSYIKSQVASSNFEGVVQV 559

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024   93 WDLSkfgRQKQLLVYNEHERTAHTVTFHSSEPNILISGSQDGTIKCFDIRSDKSINTyFCNSESVRDVKFSPHTQNIFSA 172
Cdd:PLN00181 560 WDVA---RSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGT-IKTKANICCVQFPSESGRSLAF 635

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 28572024  173 VSENGTVQLWDMRKWDKCMVQFTAHYGPVYTCDWHPTRNwLATGSRDKQIKVWNM 227
Cdd:PLN00181 636 GSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFVDSST-LVSSSTDNTLKLWDL 689
WD40 pfam00400
WD domain, G-beta repeat;
189-226 3.27e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 3.27e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 28572024   189 KCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWN 226
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
mRING-H2-C3H3C2_Mio cd16691
Modified RING finger, H2 subclass (C3H3C2-type), found in WD repeat-containing protein mio and ...
 704-767 4.19e-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: 50.91  E-value: 4.19e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28572024 704 CGECGRPMGGKVGWYCDKCKSMQSAKCCVCGLIVRGVYAWCQGCSHGGHIEHLQKYFAKHSKCP 767
Cdd:cd16691   4 CSLCLIPMGTPSSSLPGATASDVDLSSDKKLAPFSSWFTWCQTCRHGGHAGHLQEWFRDHSECP 67
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 189-226 5.69e-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: 49.23  E-value: 5.69e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 28572024    189 KCMVQFTAHYGPVYTCDWHPTRNWLATGSRDKQIKVWN 226
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG5354 COG5354
Uncharacterized protein, contains Trp-Asp (WD) repeat [General function prediction only];
139-333 3.08e-07

Uncharacterized protein, contains Trp-Asp (WD) repeat [General function prediction only];


Pssm-ID: 227657 [Multi-domain]  Cd Length: 561  Bit Score: 53.73  E-value: 3.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024 139 FDIRSDKSINTyFCNSES-------------VRDVKFSPHTQNIFSAVSENgtVQLWDMRKWDKCmVQFTAHYgpVYTCD 205
Cdd:COG5354   5 FPLDYSAVISV-FWNSQSevihtrfesenwpVAYVSESPLGTYLFSEHAAG--VECWGGPSKAKL-VRFRHPD--VKYLD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024 206 WHPTRNWLATGSR---------------DKQIKVWN------MDGRPGLEHTIHTIAVVgrvKWRPERTYhiasCALVVD 264
Cdd:COG5354  79 FSPNEKYLVTWSRepiiepeieispftsKNNVFVWDiasgmiVFSFNGISQPYLGWPVL---KFSIDDKY----VARVVG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024 265 YSVHVWDI--RRPYIPFA----------SFNEHTNVTTGIAW----QGSD-SHCLLSISKDSTIYKHAFKDATRPALKAN 327
Cdd:COG5354 152 SSLYIHEItdNIEEHPFKnlrpvgildfSISPEGNHDELAYWtpekLNKPaMVRILSIPKNSVLVTKNLFKVSGVQLKWQ 231


                ....*.
gi 28572024 328 AQGASL 333
Cdd:COG5354 232 VLGKYL 237
PTZ00421 PTZ00421
coronin; Provisional
 70-226 2.23e-05

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 47.58  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024   70 DVAWSTLDSNLLATAATNGVVSVWDLSKFGRQKQ----LLVYNEHERTAHTVTFHSSEPNILISGSQDGTIKCFDIRSDK 145
Cdd:PTZ00421  80 DVAFNPFDPQKLFTASEDGTIMGWGIPEEGLTQNisdpIVHLQGHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERGK 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024  146 SINTYFCNSESVRDVKFSPHTqNIFSAVSENGTVQLWDMRKWDKCMVQFTAHYGPVYTCDWHPTRNWLAT----GSRDKQ 221
Cdd:PTZ00421 160 AVEVIKCHSDQITSLEWNLDG-SLLCTTSKDKKLNIIDPRDGTIVSSVEAHASAKSQRCLWAKRKDLIITlgcsKSQQRQ 238


                 ....*
gi 28572024  222 IKVWN 226
Cdd:PTZ00421 239 IMLWD 243
Utp8 pfam10395
Utp8 family; Utp8 is an essential component of the nuclear tRNA export machinery in ...
 108-183 3.72e-03

Utp8 family; Utp8 is an essential component of the nuclear tRNA export machinery in Saccharomyces cerevisiae. It is a tRNA binding protein that acts at a step between tRNA maturation /aminoacylation, and translocation of the tRNA across the nuclear pore complex.


Pssm-ID: 402149  Cd Length: 690  Bit Score: 40.78  E-value: 3.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28572024   108 NEHERTAHTVTFHSSEPNILISGSQDGTIKcFDIRSDKSINTY-FCNSESVRDVKFSPHTQNIFsAVSENGTVQLWD 183
Cdd:pfam10395  85 NSHELWCYGLTERKKVHKLLLLEKPVDSTE-DDDTDEETSVTYeVKLDKKVVGIKFISKGKQIV-VVLENGSIQFYD 159
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 143-183 4.27e-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: 35.75  E-value: 4.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 28572024    143 SDKSINTYFCNSESVRDVKFSPHTQNIFSAvSENGTVQLWD 183
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASG-SDDGTIKLWD 40
zinc_ribbon_16 pfam17034
Zinc-ribbon like family; This family is found at the C-terminus of WD40 repeat structures in ...
 719-776 4.44e-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: 38.10  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572024   719 CDKCkSMQSAKCCVCGL----------------IVRGV----------YAWCQGCSHGGHIEHLQKYFAKHSKCP--KCG 770
Cdd:pfam17034  41 CPAC-SQPLPRCAVCGLslgtsnltnkdsrrksVVKDPqdfeklfekwFSFCLSCGHGSHADHATEWFSTHSICPvaDCN 119


                  ....*.
gi 28572024   771 HLCAYS 776
Cdd:pfam17034 120 CLCREK 125
zf-RING_16 pfam17120
RING/Ubox like zinc-binding domain;
729-773 8.32e-03

RING/Ubox like zinc-binding domain;


Pssm-ID: 375001  Cd Length: 57  Bit Score: 35.45  E-value: 8.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 28572024   729 KCCVCGLIVRGVYAWCQGCSHGGHIEHLQKYFAK-HSKCPK-CGHLC 773
Cdd:pfam17120   6 SCNYCCLRVRGRVFLCGVCQHVLHASCAREWWENdDGECPSgCGCNC 52
 
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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