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Conserved domains on  [gi|6320369|ref|NP_010449|]
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Trm82p [Saccharomyces cerevisiae S288C]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 1000017)

WD40 repeat domain-containing protein folds into a beta-propeller structure and functions as a scaffold, providing a platform for the interaction and assembly of several proteins into a signalosome; similar to 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

CATH:  2.130.10.10
Gene Ontology:  GO:0005515
PubMed:  10322433|8090199|30069656|29026209
SCOP:  4002744

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 ...
 112-278 3.52e-08

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: 54.65  E-value: 3.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  112 SDESRLIACADSDKSLLVFDVDkTSKNVLKLRkrfCFSKRPNAISIAEDDTTVIIADKFGDVYSIDINSIPEEKFtqepI 191
Cdd:cd00200 102 SPDGRILSSSSRDKTIKVWDVE-TGKCLTTLR---GHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVAT----L 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  192 LGHVSMLTDVHLikDSDGHQFIITSDrDEHIKISHyPQCFIVDKWLFGHKHFVSSIC-CGKDYLLLSAGGDDKIFAWDWK 270
Cdd:cd00200 174 TGHTGEVNSVAF--SPDGEKLLSSSS-DGTIKLWD-LSTGKCLGTLRGHENGVNSVAfSPDGYLLASGSEDGTIRVWDLR 249


                ....*...
gi 6320369  271 TGKNLSTF 278
Cdd:cd00200 250 TGECVQTL 257
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 112-278 3.52e-08

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: 54.65  E-value: 3.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  112 SDESRLIACADSDKSLLVFDVDkTSKNVLKLRkrfCFSKRPNAISIAEDDTTVIIADKFGDVYSIDINSIPEEKFtqepI 191
Cdd:cd00200 102 SPDGRILSSSSRDKTIKVWDVE-TGKCLTTLR---GHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVAT----L 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  192 LGHVSMLTDVHLikDSDGHQFIITSDrDEHIKISHyPQCFIVDKWLFGHKHFVSSIC-CGKDYLLLSAGGDDKIFAWDWK 270
Cdd:cd00200 174 TGHTGEVNSVAF--SPDGEKLLSSSS-DGTIKLWD-LSTGKCLGTLRGHENGVNSVAfSPDGYLLASGSEDGTIRVWDLR 249


                ....*...
gi 6320369  271 TGKNLSTF 278
Cdd:cd00200 250 TGECVQTL 257
WD40 COG2319
WD40 repeat [General function prediction only];
103-279 1.94e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.83  E-value: 1.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  103 SYIRNLRLTSDeSRLIACADSDKSLLVFDVDkTSKNVLKLRKRfcfSKRPNAISIAEDDTTVIIA--DKFGDVYSIDins 180
Cdd:COG2319 163 GAVTSVAFSPD-GKLLASGSDDGTVRLWDLA-TGKLLRTLTGH---TGAVRSVAFSPDGKLLASGsaDGTVRLWDLA--- 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  181 ipeekfTQEPIL---GHVSMLTDVHLikDSDGhQFIITSDRDEHIKIshypqcfivdkW----------LFGHKHFVSSI 247
Cdd:COG2319 235 ------TGKLLRtltGHSGSVRSVAF--SPDG-RLLASGSADGTVRL-----------WdlatgellrtLTGHSGGVNSV 294

                       170       180       190
                ....*....|....*....|....*....|....*
gi 6320369  248 CC---GKdyLLLSAGGDDKIFAWDWKTGKNLSTFD 279
Cdd:COG2319 295 AFspdGK--LLASGSDDGTVRLWDLATGKLLRTLT 327
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 112-278 3.52e-08

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: 54.65  E-value: 3.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  112 SDESRLIACADSDKSLLVFDVDkTSKNVLKLRkrfCFSKRPNAISIAEDDTTVIIADKFGDVYSIDINSIPEEKFtqepI 191
Cdd:cd00200 102 SPDGRILSSSSRDKTIKVWDVE-TGKCLTTLR---GHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVAT----L 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  192 LGHVSMLTDVHLikDSDGHQFIITSDrDEHIKISHyPQCFIVDKWLFGHKHFVSSIC-CGKDYLLLSAGGDDKIFAWDWK 270
Cdd:cd00200 174 TGHTGEVNSVAF--SPDGEKLLSSSS-DGTIKLWD-LSTGKCLGTLRGHENGVNSVAfSPDGYLLASGSEDGTIRVWDLR 249


                ....*...
gi 6320369  271 TGKNLSTF 278
Cdd:cd00200 250 TGECVQTL 257
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 191-278 7.87e-07

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: 50.41  E-value: 7.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  191 ILGHVSMLTDVHLikdSDGHQFIITSDRDEHIKI--SHYPQCFIVDKwlfGHKHFVSSI-CCGKDYLLLSAGGDDKIFAW 267
Cdd:cd00200   5 LKGHTGGVTCVAF---SPDGKLLATGSGDGTIKVwdLETGELLRTLK---GHTGPVRDVaASADGTYLASGSSDKTIRLW 78

                        90
                ....*....|.
gi 6320369  268 DWKTGKNLSTF 278
Cdd:cd00200  79 DLETGECVRTL 89
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 110-278 1.01e-05

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: 46.94  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  110 LTSDESRLIACADSDKSLLVFDVDKTSknvlKLRKRFCFSKRPNAISIAEDDTTVI--IADKfgdvySIDINSIPEEKFT 187
Cdd:cd00200  58 AASADGTYLASGSSDKTIRLWDLETGE----CVRTLTGHTSYVSSVAFSPDGRILSssSRDK-----TIKVWDVETGKCL 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  188 QEpILGHVSMLTDVHLIKDSdghQFIITSDRDEHIKI--SHYPQCFIVdkwLFGHKHFVSSICCGKD-YLLLSAGGDDKI 264
Cdd:cd00200 129 TT-LRGHTDWVNSVAFSPDG---TFVASSSQDGTIKLwdLRTGKCVAT---LTGHTGEVNSVAFSPDgEKLLSSSSDGTI 201

                       170
                ....*....|....
gi 6320369  265 FAWDWKTGKNLSTF 278
Cdd:cd00200 202 KLWDLSTGKCLGTL 215
WD40 COG2319
WD40 repeat [General function prediction only];
103-279 1.94e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.83  E-value: 1.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  103 SYIRNLRLTSDeSRLIACADSDKSLLVFDVDkTSKNVLKLRKRfcfSKRPNAISIAEDDTTVIIA--DKFGDVYSIDins 180
Cdd:COG2319 163 GAVTSVAFSPD-GKLLASGSDDGTVRLWDLA-TGKLLRTLTGH---TGAVRSVAFSPDGKLLASGsaDGTVRLWDLA--- 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  181 ipeekfTQEPIL---GHVSMLTDVHLikDSDGhQFIITSDRDEHIKIshypqcfivdkW----------LFGHKHFVSSI 247
Cdd:COG2319 235 ------TGKLLRtltGHSGSVRSVAF--SPDG-RLLASGSADGTVRL-----------WdlatgellrtLTGHSGGVNSV 294

                       170       180       190
                ....*....|....*....|....*....|....*
gi 6320369  248 CC---GKdyLLLSAGGDDKIFAWDWKTGKNLSTFD 279
Cdd:COG2319 295 AFspdGK--LLASGSDDGTVRLWDLATGKLLRTLT 327
WD40 COG2319
WD40 repeat [General function prediction only];
105-278 2.29e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.44  E-value: 2.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  105 IRNLRLTSDeSRLIACADSDKSLLVFDVDkTSKNVLKLRKRfcfSKRPNAISIAEDDTTVIIADKFGDVYSIDINSiPEE 184
Cdd:COG2319 207 VRSVAFSPD-GKLLASGSADGTVRLWDLA-TGKLLRTLTGH---SGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-GEL 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  185 KFTQEpilGHVSMLTDVHLIKDSdghQFIITSDRDEHIKI--SHYPQCFivdKWLFGHKHFVSSICC---GKdyLLLSAG 259
Cdd:COG2319 281 LRTLT---GHSGGVNSVAFSPDG---KLLASGSDDGTVRLwdLATGKLL---RTLTGHTGAVRSVAFspdGK--TLASGS 349

                       170
                ....*....|....*....
gi 6320369  260 GDDKIFAWDWKTGKNLSTF 278
Cdd:COG2319 350 DDGTVRLWDLATGELLRTL 368
WD40 COG2319
WD40 repeat [General function prediction only];
103-271 4.02e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 45.67  E-value: 4.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  103 SYIRNLRLTSDeSRLIACADSDKSLLVFDVDkTSKNVLKLRKRfcfSKRPNAISIAEDDTTVIIADKFGDVYSIDINSiP 182
Cdd:COG2319 247 GSVRSVAFSPD-GRLLASGSADGTVRLWDLA-TGELLRTLTGH---SGGVNSVAFSPDGKLLASGSDDGTVRLWDLAT-G 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  183 EEKFTQEpilGHVSMLTDVHLikDSDGhQFIITSDRDEHIKISHyPQCFIVDKWLFGHKHFVSSICCGKDY-LLLSAGGD 261
Cdd:COG2319 321 KLLRTLT---GHTGAVRSVAF--SPDG-KTLASGSDDGTVRLWD-LATGELLRTLTGHTGAVTSVAFSPDGrTLASGSAD 393

                       170
                ....*....|
gi 6320369  262 DKIFAWDWKT 271
Cdd:COG2319 394 GTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
103-279 4.67e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 45.29  E-value: 4.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  103 SYIRNLRLTSDeSRLIACADSDKSLLVFDVDkTSKNVLKLRKRfcfSKRPNAISIAEDDTTVIIADKFGDVYSIDINSIP 182
Cdd:COG2319 121 GAVRSVAFSPD-GKTLASGSADGTVRLWDLA-TGKLLRTLTGH---SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGK 195

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  183 EEKftqePILGHVSMLTDVHLikDSDGhQFIITSDRDEHIKIshypqcfivdkW----------LFGHKHFVSSICCGKD 252
Cdd:COG2319 196 LLR----TLTGHTGAVRSVAF--SPDG-KLLASGSADGTVRL-----------WdlatgkllrtLTGHSGSVRSVAFSPD 257

                       170       180
                ....*....|....*....|....*...
gi 6320369  253 -YLLLSAGGDDKIFAWDWKTGKNLSTFD 279
Cdd:COG2319 258 gRLLASGSADGTVRLWDLATGELLRTLT 285
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 147-278 2.44e-03

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: 39.63  E-value: 2.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  147 CFSKRPNAISIAEDDTTVIIADKFGDvysidinsipEEKFTQEpilGHVSMLTDVHLIkdSDGHQFIITSDrDEHIKI-- 224
Cdd:cd00200  16 AFSPDGKLLATGSGDGTIKVWDLETG----------ELLRTLK---GHTGPVRDVAAS--ADGTYLASGSS-DKTIRLwd 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6320369  225 SHYPQCFIVdkwLFGHKHFVSSICCGKDYLLLSAGGDDK-IFAWDWKTGKNLSTF 278
Cdd:cd00200  80 LETGECVRT---LTGHTSYVSSVAFSPDGRILSSSSRDKtIKVWDVETGKCLTTL 131
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 103-264 5.94e-03

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: 38.47  E-value: 5.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  103 SYIRNLRLTSDeSRLIACADSDKSLLVFDVDKtsknvLKLRKRFCFSKRP-NAISIAEDDTTVIIAdkfGDVYSIDINSI 181
Cdd:cd00200 136 DWVNSVAFSPD-GTFVASSSQDGTIKLWDLRT-----GKCVATLTGHTGEvNSVAFSPDGEKLLSS---SSDGTIKLWDL 206

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320369  182 PEEKFTQEpILGHVSMLTDVHLIKDSDghqFIITSDRDEHIKI--SHYPQCfivDKWLFGHKHFVSSICCGKDYLLLSAG 259
Cdd:cd00200 207 STGKCLGT-LRGHENGVNSVAFSPDGY---LLASGSEDGTIRVwdLRTGEC---VQTLSGHTNSVTSLAWSPDGKRLASG 279


                ....*
gi 6320369  260 GDDKI 264
Cdd:cd00200 280 SADGT 284
 
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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