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Conserved domains on  [gi|1831517495|ref|NP_001368633|]
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WD_REPEATS_REGION domain-containing protein [Caenorhabditis elegans]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 11455410)

WD40 repeat domain-containing protein similar to 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
PubMed:  10322433|8090199
SCOP:  4002744

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
296-490 1.52e-15

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.18  E-value: 1.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 296 PVTRWQIGEGSIHQFSFSgSDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYS 375
Cdd:COG2319   238 LLRTLTGHSGSVRSVAFS-PDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWD 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 376 VAEKRVVCRGQAHKSWVSQVKFDPylctteedleNNGIAMTSTFDDVAKDFSIRSGPVPSTSADLNSGVMNAtsTFSrcs 455
Cdd:COG2319   317 LATGKLLRTLTGHTGAVRSVAFSP----------DGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSV--AFS--- 381

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1831517495 456 lasfntingaPAGNsvryRIGSVGHDTFLCLWDIT 490
Cdd:COG2319   382 ----------PDGR----TLASGSADGTVRLWDLA 402
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
296-490 1.52e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.18  E-value: 1.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 296 PVTRWQIGEGSIHQFSFSgSDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYS 375
Cdd:COG2319   238 LLRTLTGHSGSVRSVAFS-PDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWD 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 376 VAEKRVVCRGQAHKSWVSQVKFDPylctteedleNNGIAMTSTFDDVAKDFSIRSGPVPSTSADLNSGVMNAtsTFSrcs 455
Cdd:COG2319   317 LATGKLLRTLTGHTGAVRSVAFSP----------DGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSV--AFS--- 381

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1831517495 456 lasfntingaPAGNsvryRIGSVGHDTFLCLWDIT 490
Cdd:COG2319   382 ----------PDGR----TLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 304-407 3.29e-11

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: 64.66  E-value: 3.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 304 EGSIHQFSFSGsDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYSVAEKRVVC 383
Cdd:cd00200   177 TGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQ 255

                          90       100
                  ....*....|....*....|....*..
gi 1831517495 384 RGQAHKSWVSQVKFDP---YLCTTEED 407
Cdd:cd00200   256 TLSGHTNSVTSLAWSPdgkRLASGSAD 282
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
296-490 1.52e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.18  E-value: 1.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 296 PVTRWQIGEGSIHQFSFSgSDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYS 375
Cdd:COG2319   238 LLRTLTGHSGSVRSVAFS-PDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWD 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 376 VAEKRVVCRGQAHKSWVSQVKFDPylctteedleNNGIAMTSTFDDVAKDFSIRSGPVPSTSADLNSGVMNAtsTFSrcs 455
Cdd:COG2319   317 LATGKLLRTLTGHTGAVRSVAFSP----------DGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSV--AFS--- 381

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1831517495 456 lasfntingaPAGNsvryRIGSVGHDTFLCLWDIT 490
Cdd:COG2319   382 ----------PDGR----TLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
296-489 2.11e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 75.72  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 296 PVTRWQIGEGSIHQFSFSgSDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYS 375
Cdd:COG2319   154 LLRTLTGHSGAVTSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 376 VAEKRVVCRGQAHKSWVSQVKFDPylctteedleNNGIAMTSTFDDVAKDFSIRSGPVPSTSADLNSGVMNAtsTFSrcs 455
Cdd:COG2319   233 LATGKLLRTLTGHSGSVRSVAFSP----------DGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSV--AFS--- 297

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1831517495 456 lasfntingaPAGNsvryRIGSVGHDTFLCLWDI 489
Cdd:COG2319   298 ----------PDGK----LLASGSDDGTVRLWDL 317
WD40 COG2319
WD40 repeat [General function prediction only];
296-399 6.98e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 74.18  E-value: 6.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 296 PVTRWQIGEGSIHQFSFSgSDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYS 375
Cdd:COG2319   112 LLRTLTGHTGAVRSVAFS-PDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                          90       100
                  ....*....|....*....|....
gi 1831517495 376 VAEKRVVCRGQAHKSWVSQVKFDP 399
Cdd:COG2319   191 LATGKLLRTLTGHTGAVRSVAFSP 214
WD40 COG2319
WD40 repeat [General function prediction only];
296-490 9.04e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 73.79  E-value: 9.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 296 PVTRWQIGEGSIHQFSFSgSDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYS 375
Cdd:COG2319   196 LLRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 376 VAEKRVVCRGQAHKSWVSQVKFDPylctteedleNNGIAMTSTFDDVAKDFSIRSGPVPSTSADLNSGVMNAtsTFSrcs 455
Cdd:COG2319   275 LATGELLRTLTGHSGGVNSVAFSP----------DGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV--AFS--- 339

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1831517495 456 lasfntingaPAGNsvryRIGSVGHDTFLCLWDIT 490
Cdd:COG2319   340 ----------PDGK----TLASGSDDGTVRLWDLA 360
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 304-407 3.29e-11

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: 64.66  E-value: 3.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 304 EGSIHQFSFSGsDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYSVAEKRVVC 383
Cdd:cd00200   177 TGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQ 255

                          90       100
                  ....*....|....*....|....*..
gi 1831517495 384 RGQAHKSWVSQVKFDP---YLCTTEED 407
Cdd:cd00200   256 TLSGHTNSVTSLAWSPdgkRLASGSAD 282
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 296-431 7.94e-11

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: 63.51  E-value: 7.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 296 PVTRWQIGEGSIHQFSFSgSDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYS 375
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831517495 376 VAEKRVVCRGQAHKSWVSQVKFDPylctteedleNNGIAMTSTFDDVAKDFSIRSG 431
Cdd:cd00200    80 LETGECVRTLTGHTSYVSSVAFSP----------DGRILSSSSRDKTIKVWDVETG 125
WD40 COG2319
WD40 repeat [General function prediction only];
296-490 3.44e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 62.62  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 296 PVTRWQIGEGSIHQFSFSgSDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYS 375
Cdd:COG2319    70 LLATLLGHTAAVLSVAFS-PDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWD 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 376 VAEKRVVCRGQAHKSWVSQVKFDPylctteedlenNG--IAmTSTFDDVAKDFSIRSGPVPSTSADLNSGVMNAtsTFSr 453
Cdd:COG2319   149 LATGKLLRTLTGHSGAVTSVAFSP-----------DGklLA-SGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV--AFS- 213

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1831517495 454 cslasfntingaPAGNsvryRIGSVGHDTFLCLWDIT 490
Cdd:COG2319   214 ------------PDGK----LLASGSADGTVRLWDLA 234
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 304-431 6.50e-10

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: 60.81  E-value: 6.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 304 EGSIHQFSFSGsDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYSVAEKRVVC 383
Cdd:cd00200   135 TDWVNSVAFSP-DGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLG 213

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1831517495 384 RGQAHKSWVSQVKFDPylctteedleNNGIAMTSTFDDVAKDFSIRSG 431
Cdd:cd00200   214 TLRGHENGVNSVAFSP----------DGYLLASGSEDGTIRVWDLRTG 251
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 228-399 2.64e-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: 52.72  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 228 SVTCIRWLPgDSNIFLASYVSGNLYVYDQRISAASSNNNGSSQPPPWTI-HKEGDKFAI----HT---WKgkVQRNPVTR 299
Cdd:cd00200    11 GVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAaSADGTYLASgssdKTirlWD--LETGECVR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 300 WQIG-EGSIHQFSFSgSDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYSVAE 378
Cdd:cd00200    88 TLTGhTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRT 166

                         170       180
                  ....*....|....*....|.
gi 1831517495 379 KRVVCRGQAHKSWVSQVKFDP 399
Cdd:cd00200   167 GKCVATLTGHTGEVNSVAFSP 187
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 228-375 1.50e-04

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: 44.25  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 228 SVTCIRWLPGDSNIFLASYvSGNLYVYDQRisaassnnngssqpppwtihkegDKFAIHTWKGKvqrnpvtrwqigEGSI 307
Cdd:cd00200   179 EVNSVAFSPDGEKLLSSSS-DGTIKLWDLS-----------------------TGKCLGTLRGH------------ENGV 222

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831517495 308 HQFSFSgSDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLLTVYS 375
Cdd:cd00200   223 NSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
292-399 5.44e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.98  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831517495 292 VQRNPVTRWQIGEGSIHQFSFSGSDGKMMATVSHDGFLRIFNYHAQELLAVMKSYFGGLLTLSWSPDAKLIATGGEDDLL 371
Cdd:COG2319    23 AALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTV 102

                          90       100
                  ....*....|....*....|....*...
gi 1831517495 372 TVYSVAEKRVVCRGQAHKSWVSQVKFDP 399
Cdd:COG2319   103 RLWDLATGLLLRTLTGHTGAVRSVAFSP 130
 
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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