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Conserved domains on  [gi|398366225|ref|NP_011741|]
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Ama1p [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 ...
 266-561 1.01e-16

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: 80.84  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 266 HQYLSEKRDLVTCVSFCPYNTYFIVGTKFGRILLYD-QKEFFHSSNTNEKEPVFVFQTESFKgicclewfkpgeiCKFYV 344
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDlETGELLRTLKGHTGPVRDVAASADG-------------TYLAS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 345 GEENGNVSLFeikslhfpiknwskrqkledeNLIGLKLHSTYQAQAQQVCGISLNEHANLLAVGGNDNSCSLWDIsdlDK 424
Cdd:cd00200   69 GSSDKTIRLW---------------------DLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV---ET 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 425 PIKKFVLP-HKAAVKAIAFCPwSKSLLAtgGGSKDRCIKFWHTSTGTLLDEICT-SGQVTSLIWSLRHKQIVAtfGFGDT 502
Cdd:cd00200  125 GKCLTTLRgHTDWVNSVAFSP-DGTFVA--SSSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLS--SSSDG 199

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366225 503 KnpvlITLYSyPKLSKLLEVRSPNPLRVLSAVISPSSMAICVATNDETIRFYELWNDKE 561
Cdd:cd00200  200 T----IKLWD-LSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGEC 253
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 266-561 1.01e-16

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: 80.84  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 266 HQYLSEKRDLVTCVSFCPYNTYFIVGTKFGRILLYD-QKEFFHSSNTNEKEPVFVFQTESFKgicclewfkpgeiCKFYV 344
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDlETGELLRTLKGHTGPVRDVAASADG-------------TYLAS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 345 GEENGNVSLFeikslhfpiknwskrqkledeNLIGLKLHSTYQAQAQQVCGISLNEHANLLAVGGNDNSCSLWDIsdlDK 424
Cdd:cd00200   69 GSSDKTIRLW---------------------DLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV---ET 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 425 PIKKFVLP-HKAAVKAIAFCPwSKSLLAtgGGSKDRCIKFWHTSTGTLLDEICT-SGQVTSLIWSLRHKQIVAtfGFGDT 502
Cdd:cd00200  125 GKCLTTLRgHTDWVNSVAFSP-DGTFVA--SSSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLS--SSSDG 199

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366225 503 KnpvlITLYSyPKLSKLLEVRSPNPLRVLSAVISPSSMAICVATNDETIRFYELWNDKE 561
Cdd:cd00200  200 T----IKLWD-LSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGEC 253
WD40 COG2319
WD40 repeat [General function prediction only];
376-558 2.68e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 71.87  E-value: 2.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 376 NLIGLKLHSTYQAQAQQVCGISLNEHANLLAVGGNDNSCSLWDISDlDKPIKKFVlPHKAAVKAIAFCPWSKsLLATGGG 455
Cdd:COG2319  190 DLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT-GKLLRTLT-GHSGSVRSVAFSPDGR-LLASGSA 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 456 skDRCIKFWHTSTGTLLDEI-CTSGQVTSLIWSlRHKQIVATFGFGDTknpvlITLYSyPKLSKLLEVRSPNPLRVLSAV 534
Cdd:COG2319  267 --DGTVRLWDLATGELLRTLtGHSGGVNSVAFS-PDGKLLASGSDDGT-----VRLWD-LATGKLLRTLTGHTGAVRSVA 337

                        170       180
                 ....*....|....*....|....
gi 398366225 535 ISPSSMAICVATNDETIRfyeLWN 558
Cdd:COG2319  338 FSPDGKTLASGSDDGTVR---LWD 358
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 266-561 1.01e-16

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: 80.84  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 266 HQYLSEKRDLVTCVSFCPYNTYFIVGTKFGRILLYD-QKEFFHSSNTNEKEPVFVFQTESFKgicclewfkpgeiCKFYV 344
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDlETGELLRTLKGHTGPVRDVAASADG-------------TYLAS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 345 GEENGNVSLFeikslhfpiknwskrqkledeNLIGLKLHSTYQAQAQQVCGISLNEHANLLAVGGNDNSCSLWDIsdlDK 424
Cdd:cd00200   69 GSSDKTIRLW---------------------DLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV---ET 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 425 PIKKFVLP-HKAAVKAIAFCPwSKSLLAtgGGSKDRCIKFWHTSTGTLLDEICT-SGQVTSLIWSLRHKQIVAtfGFGDT 502
Cdd:cd00200  125 GKCLTTLRgHTDWVNSVAFSP-DGTFVA--SSSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLS--SSSDG 199

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 398366225 503 KnpvlITLYSyPKLSKLLEVRSPNPLRVLSAVISPSSMAICVATNDETIRFYELWNDKE 561
Cdd:cd00200  200 T----IKLWD-LSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGEC 253
WD40 COG2319
WD40 repeat [General function prediction only];
376-558 2.68e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 71.87  E-value: 2.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 376 NLIGLKLHSTYQAQAQQVCGISLNEHANLLAVGGNDNSCSLWDISDlDKPIKKFVlPHKAAVKAIAFCPWSKsLLATGGG 455
Cdd:COG2319  190 DLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT-GKLLRTLT-GHSGSVRSVAFSPDGR-LLASGSA 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 456 skDRCIKFWHTSTGTLLDEI-CTSGQVTSLIWSlRHKQIVATFGFGDTknpvlITLYSyPKLSKLLEVRSPNPLRVLSAV 534
Cdd:COG2319  267 --DGTVRLWDLATGELLRTLtGHSGGVNSVAFS-PDGKLLASGSDDGT-----VRLWD-LATGKLLRTLTGHTGAVRSVA 337

                        170       180
                 ....*....|....*....|....
gi 398366225 535 ISPSSMAICVATNDETIRfyeLWN 558
Cdd:COG2319  338 FSPDGKTLASGSDDGTVR---LWD 358
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 382-556 7.50e-13

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: 69.29  E-value: 7.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 382 LHSTYQAQAQQVCGISLNEHANLLAVGGNDNSCSLWDISDlDKPIKKFVLpHKAAVKAIAFCPWSKSLLAtggGSKDRCI 461
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLET-GELLRTLKG-HTGPVRDVAASADGTYLAS---GSSDKTI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 462 KFWHTSTGTLLDEI-CTSGQVTSLIWSlRHKQIVATfGFGDTknpvliTLysypklsKLLEVRSPNPLRVL--------S 532
Cdd:cd00200   76 RLWDLETGECVRTLtGHTSYVSSVAFS-PDGRILSS-SSRDK------TI-------KVWDVETGKCLTTLrghtdwvnS 140

                        170       180
                 ....*....|....*....|....
gi 398366225 533 AVISPSSMAICVATNDETIRFYEL 556
Cdd:cd00200  141 VAFSPDGTFVASSSQDGTIKLWDL 164
WD40 COG2319
WD40 repeat [General function prediction only];
376-558 4.90e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 68.01  E-value: 4.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 376 NLIGLKLHSTYQAQAQQVCGISLNEHANLLAVGGNDNSCSLWDISDlDKPIKKFVlPHKAAVKAIAFCPWSKsLLATGGG 455
Cdd:COG2319  106 DLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT-GKLLRTLT-GHSGAVTSVAFSPDGK-LLASGSD 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 456 skDRCIKFWHTSTGTLLDEI-CTSGQVTSLIWSlRHKQIVATFGFGDTknpvlITLYSyPKLSKLLEVRSPNPLRVLSAV 534
Cdd:COG2319  183 --DGTVRLWDLATGKLLRTLtGHTGAVRSVAFS-PDGKLLASGSADGT-----VRLWD-LATGKLLRTLTGHSGSVRSVA 253

                        170       180
                 ....*....|....*....|....
gi 398366225 535 ISPSSMAICVATNDETIRfyeLWN 558
Cdd:COG2319  254 FSPDGRLLASGSADGTVR---LWD 274
WD40 COG2319
WD40 repeat [General function prediction only];
381-558 7.27e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.08  E-value: 7.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 381 KLHSTYQAQAQQVCGISLNEHANLLAVGGNDNSCSLWDISDldKPIKKFVLPHKAAVKAIAFCPWSKsLLATGGGSKDrc 460
Cdd:COG2319  237 KLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT--GELLRTLTGHSGGVNSVAFSPDGK-LLASGSDDGT-- 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 461 IKFWHTSTGTLLDEIC-TSGQVTSLIWSlRHKQIVATFGFGDTknpvlITLYSyPKLSKLLEVRSPNPLRVLSAVISPSS 539
Cdd:COG2319  312 VRLWDLATGKLLRTLTgHTGAVRSVAFS-PDGKTLASGSDDGT-----VRLWD-LATGELLRTLTGHTGAVTSVAFSPDG 384

                        170
                 ....*....|....*....
gi 398366225 540 MAICVATNDETIRfyeLWN 558
Cdd:COG2319  385 RTLASGSADGTVR---LWD 400
WD40 COG2319
WD40 repeat [General function prediction only];
376-495 8.22e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.00  E-value: 8.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 376 NLIGLKLHSTYQAQAQQVCGISLNEHANLLAVGGNDNSCSLWDISDlDKPIKKFVlPHKAAVKAIAFCPWSKsLLATGGG 455
Cdd:COG2319  274 DLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLAT-GKLLRTLT-GHTGAVRSVAFSPDGK-TLASGSD 350

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 398366225 456 skDRCIKFWHTSTGTLLDEICT-SGQVTSLIWSLRHKQIVA 495
Cdd:COG2319  351 --DGTVRLWDLATGELLRTLTGhTGAVTSVAFSPDGRTLAS 389
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 269-464 1.19e-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: 53.49  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 269 LSEKRDLVTCVSFCPYNTYFIVGTKFGRILLYDqkeffhssnTNEKEPVFVFQTESfKGICCLEWFKPGEicKFYVGEEN 348
Cdd:cd00200  131 LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD---------LRTGKCVATLTGHT-GEVNSVAFSPDGE--KLLSSSSD 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366225 349 GNVSLFEIKSlhfpiknwskrqkledenligLKLHSTYQAQAQQVCGISLNEHANLLAVGGNDNSCSLWdisDLDKPIKK 428
Cdd:cd00200  199 GTIKLWDLST---------------------GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVW---DLRTGECV 254

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 398366225 429 FVLP-HKAAVKAIAFCPwSKSLLATggGSKDRCIKFW 464
Cdd:cd00200  255 QTLSgHTNSVTSLAWSP-DGKRLAS--GSADGTIRIW 288
HCoV_HKU1-like_RdRp cd21593
human coronavirus HKU1 RNA-dependent RNA polymerase, also known as non-structural protein 12, ...
 501-571 3.58e-03

human coronavirus HKU1 RNA-dependent RNA polymerase, also known as non-structural protein 12, and similar proteins from betacoronaviruses in the A lineage: responsible for replication and transcription of the viral RNA genome; This group contains the RNA-dependent RNA polymerase (RdRp) of human coronavirus HKU1, murine hepatitis virus, and similar proteins from betacoronaviruses in the embecovirus subgenera (A lineage). CoVs utilize a multi-subunit replication/transcription machinery. A set of non-structural proteins (Nsps) generated as cleavage products of the ORF1a and ORF1ab viral polyproteins assemble to facilitate viral replication and transcription. A key component, the RNA-dependent RNA polymerase (RdRp, also known as Nsp12), catalyzes the synthesis of viral RNA and thus plays a central role in the replication and transcription cycle of CoV, possibly interacting with its co-factors, Nsp7 and Nsp8. RdRp is therefore considered a primary target for nucleotide analog antiviral inhibitors such as remdesivir. Nsp12 contains a RdRp domain as well as a large N-terminal extension that adopts a nidovirus RdRp-associated nucleotidyltransferase (NiRAN) architecture. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.


Pssm-ID: 394897  Cd Length: 925  Bit Score: 40.33  E-value: 3.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366225 501 DTKNPVLITlYSYPKLSKLLevrsPNPLRVLSAVISPSSMAICVATNDetiRFYELWNDKEEIINEIQESG 571
Cdd:cd21593  601 DVDNPVLMG-WDYPKCDRAM----PNILRIVSSLVLARKHDSCCSHGD---RFYRLANECAQVLSEIVMCG 663
 
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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