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Conserved domains on  [gi|1907157175|ref|XP_036020294|]
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DDB1- and CUL4-associated factor 12 isoform X3 [Mus musculus]

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 ...
 85-297 1.14e-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: 55.03  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175  85 HLGTLNKVfaSQWLNHRQVVCGTKCNTLFVVDVQTGQITkipilkdREPGGVTQqgcGIHAIELNPSRTLLATGGDNpNS 164
Cdd:cd00200    50 HTGPVRDV--AASADGTYLASGSSDKTIRLWDLETGECV-------RTLTGHTS---YVSSVAFSPDGRILSSSSRD-KT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175 165 LAIYRLPTldPVCVGD-DGHKDWIFSIAWI-NDTMAVSGSRDGSMGLWEVTddvltksdarhnvSPVPVYAHITHkalkd 242
Cdd:cd00200   117 IKVWDVET--GKCLTTlRGHTDWVNSVAFSpDGTFVASSSQDGTIKLWDLR-------------TGKCVATLTGH----- 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907157175 243 ipkedtnpdNCKVRALAFNNKNKVLCFG--------FDLHTGlvsklpILTALFISHLQPITG 297
Cdd:cd00200   177 ---------TGEVNSVAFSPDGEKLLSSssdgtiklWDLSTG------KCLGTLRGHENGVNS 224
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 85-297 1.14e-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: 55.03  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175  85 HLGTLNKVfaSQWLNHRQVVCGTKCNTLFVVDVQTGQITkipilkdREPGGVTQqgcGIHAIELNPSRTLLATGGDNpNS 164
Cdd:cd00200    50 HTGPVRDV--AASADGTYLASGSSDKTIRLWDLETGECV-------RTLTGHTS---YVSSVAFSPDGRILSSSSRD-KT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175 165 LAIYRLPTldPVCVGD-DGHKDWIFSIAWI-NDTMAVSGSRDGSMGLWEVTddvltksdarhnvSPVPVYAHITHkalkd 242
Cdd:cd00200   117 IKVWDVET--GKCLTTlRGHTDWVNSVAFSpDGTFVASSSQDGTIKLWDLR-------------TGKCVATLTGH----- 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907157175 243 ipkedtnpdNCKVRALAFNNKNKVLCFG--------FDLHTGlvsklpILTALFISHLQPITG 297
Cdd:cd00200   177 ---------TGEVNSVAFSPDGEKLLSSssdgtiklWDLSTG------KCLGTLRGHENGVNS 224
WD40 COG2319
WD40 repeat [General function prediction only];
101-224 3.35e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 54.15  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175 101 RQVVCGTKCNTLFVVDVQTGQITKIpilkdrepggVTQQGCGIHAIELNPSRTLLATGGDNpNSLAIYRLPTLDPVcVGD 180
Cdd:COG2319   259 RLLASGSADGTVRLWDLATGELLRT----------LTGHSGGVNSVAFSPDGKLLASGSDD-GTVRLWDLATGKLL-RTL 326

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907157175 181 DGHKDWIFSIAWIND-TMAVSGSRDGSMGLWEVTDDVLTKSDARH 224
Cdd:COG2319   327 TGHTGAVRSVAFSPDgKTLASGSDDGTVRLWDLATGELLRTLTGH 371
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 181-211 3.36e-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: 34.60  E-value: 3.36e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1907157175  181 DGHKDWIFSIAWIND-TMAVSGSRDGSMGLWE 211
Cdd:smart00320   9 KGHTGPVTSVAFSPDgKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
181-211 6.93e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 33.86  E-value: 6.93e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907157175 181 DGHKDWIFSIAWIND-TMAVSGSRDGSMGLWE 211
Cdd:pfam00400   8 EGHTGSVTSLAFSPDgKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 85-297 1.14e-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: 55.03  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175  85 HLGTLNKVfaSQWLNHRQVVCGTKCNTLFVVDVQTGQITkipilkdREPGGVTQqgcGIHAIELNPSRTLLATGGDNpNS 164
Cdd:cd00200    50 HTGPVRDV--AASADGTYLASGSSDKTIRLWDLETGECV-------RTLTGHTS---YVSSVAFSPDGRILSSSSRD-KT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175 165 LAIYRLPTldPVCVGD-DGHKDWIFSIAWI-NDTMAVSGSRDGSMGLWEVTddvltksdarhnvSPVPVYAHITHkalkd 242
Cdd:cd00200   117 IKVWDVET--GKCLTTlRGHTDWVNSVAFSpDGTFVASSSQDGTIKLWDLR-------------TGKCVATLTGH----- 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907157175 243 ipkedtnpdNCKVRALAFNNKNKVLCFG--------FDLHTGlvsklpILTALFISHLQPITG 297
Cdd:cd00200   177 ---------TGEVNSVAFSPDGEKLLSSssdgtiklWDLSTG------KCLGTLRGHENGVNS 224
WD40 COG2319
WD40 repeat [General function prediction only];
101-224 3.35e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 54.15  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175 101 RQVVCGTKCNTLFVVDVQTGQITKIpilkdrepggVTQQGCGIHAIELNPSRTLLATGGDNpNSLAIYRLPTLDPVcVGD 180
Cdd:COG2319   259 RLLASGSADGTVRLWDLATGELLRT----------LTGHSGGVNSVAFSPDGKLLASGSDD-GTVRLWDLATGKLL-RTL 326

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907157175 181 DGHKDWIFSIAWIND-TMAVSGSRDGSMGLWEVTDDVLTKSDARH 224
Cdd:COG2319   327 TGHTGAVRSVAFSPDgKTLASGSDDGTVRLWDLATGELLRTLTGH 371
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 85-225 4.46e-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: 4.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175  85 HLGTLNKVFASQwlNHRQVVCGTKCNTLFVVDVQTGQITKIpiLKDREpggvtqqgCGIHAIELNPSRTLLATGGDNpNS 164
Cdd:cd00200   134 HTDWVNSVAFSP--DGTFVASSSQDGTIKLWDLRTGKCVAT--LTGHT--------GEVNSVAFSPDGEKLLSSSSD-GT 200

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907157175 165 LAIYRLPTLDPVCVGDdGHKDWIFSIAWINDT-MAVSGSRDGSMGLWEVTDDVLTKSDARHN 225
Cdd:cd00200   201 IKLWDLSTGKCLGTLR-GHENGVNSVAFSPDGyLLASGSEDGTIRVWDLRTGECVQTLSGHT 261
WD40 COG2319
WD40 repeat [General function prediction only];
101-225 7.32e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 49.91  E-value: 7.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175 101 RQVVCGTKCNTLFVVDVQTGQITKIpiLKDREPGgvtqqgcgIHAIELNPSRTLLATGGDNpNSLAIYRLPTLDPVCVGD 180
Cdd:COG2319   217 KLLASGSADGTVRLWDLATGKLLRT--LTGHSGS--------VRSVAFSPDGRLLASGSAD-GTVRLWDLATGELLRTLT 285

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907157175 181 dGHKDWIFSIAWIND-TMAVSGSRDGSMGLWEVTDDVLTKSDARHN 225
Cdd:COG2319   286 -GHSGGVNSVAFSPDgKLLASGSDDGTVRLWDLATGKLLRTLTGHT 330
WD40 COG2319
WD40 repeat [General function prediction only];
101-225 1.30e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 49.14  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175 101 RQVVCGTKCNTLFVVDVQTGQitKIPILKDREPGgvtqqgcgIHAIELNPSRTLLATGGDNpNSLAIYRLPTLDPVCVGD 180
Cdd:COG2319   175 KLLASGSDDGTVRLWDLATGK--LLRTLTGHTGA--------VRSVAFSPDGKLLASGSAD-GTVRLWDLATGKLLRTLT 243

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907157175 181 dGHKDWIFSIAWIND-TMAVSGSRDGSMGLWEVTDDVLTKSDARHN 225
Cdd:COG2319   244 -GHSGSVRSVAFSPDgRLLASGSADGTVRLWDLATGELLRTLTGHS 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 87-220 4.84e-06

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: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175  87 GTLNKVFASQWLNHRQVVC-GTKCNTLFVVDVQTGQITKipilkdrepggvTQQGcgiHAIELN-----PSRTLLATGGD 160
Cdd:cd00200     7 GHTGGVTCVAFSPDGKLLAtGSGDGTIKVWDLETGELLR------------TLKG---HTGPVRdvaasADGTYLASGSS 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907157175 161 NpNSLAIYRLPTldPVCVGD-DGHKDWIFSIAWIND-TMAVSGSRDGSMGLWEVTDDVLTKS 220
Cdd:cd00200    72 D-KTIRLWDLET--GECVRTlTGHTSYVSSVAFSPDgRILSSSSRDKTIKVWDVETGKCLTT 130
WD40 COG2319
WD40 repeat [General function prediction only];
12-225 1.57e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.06  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175  12 ASASPGAGSDAQGPQFGWDHSLHKRKRLPPVKRSLVYYLKNREVRLQNETSYSRLLHGYAAQQLPSLLKEREFHLGTLNK 91
Cdd:COG2319     4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175  92 VFASqwLNHRQVVCGTKCNTLFVVDVQTGQITkipilkdREPGGVTQqgcGIHAIELNPSRTLLATGGDNpNSLAIYRLP 171
Cdd:COG2319    84 VAFS--PDGRLLASASADGTVRLWDLATGLLL-------RTLTGHTG---AVRSVAFSPDGKTLASGSAD-GTVRLWDLA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907157175 172 TLDPVCVGDdGHKDWIFSIAWIND-TMAVSGSRDGSMGLWEVTDDVLTKSDARHN 225
Cdd:COG2319   151 TGKLLRTLT-GHSGAVTSVAFSPDgKLLASGSDDGTVRLWDLATGKLLRTLTGHT 204
WD40 COG2319
WD40 repeat [General function prediction only];
110-214 1.93e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 45.67  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175 110 NTLFVVDVQTGQITKipilkdrepgGVTQQGCGIHAIELNPSRTLLATGGDNpNSLAIYRLPTLDPVCVgDDGHKDWIFS 189
Cdd:COG2319   310 GTVRLWDLATGKLLR----------TLTGHTGAVRSVAFSPDGKTLASGSDD-GTVRLWDLATGELLRT-LTGHTGAVTS 377

                          90       100
                  ....*....|....*....|....*.
gi 1907157175 190 IAWIND-TMAVSGSRDGSMGLWEVTD 214
Cdd:COG2319   378 VAFSPDgRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 110-211 5.96e-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: 40.78  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907157175 110 NTLFVVDVQTGQITKIPILKDRepggvtqqgcGIHAIELNPSRTLLATGGDNpNSLAIYRLPTLDPVCVGDdGHKDWIFS 189
Cdd:cd00200   199 GTIKLWDLSTGKCLGTLRGHEN----------GVNSVAFSPDGYLLASGSED-GTIRVWDLRTGECVQTLS-GHTNSVTS 266

                          90       100
                  ....*....|....*....|...
gi 1907157175 190 IAWINDTMA-VSGSRDGSMGLWE 211
Cdd:cd00200   267 LAWSPDGKRlASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 181-211 3.36e-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: 34.60  E-value: 3.36e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1907157175  181 DGHKDWIFSIAWIND-TMAVSGSRDGSMGLWE 211
Cdd:smart00320   9 KGHTGPVTSVAFSPDgKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
181-211 6.93e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 33.86  E-value: 6.93e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907157175 181 DGHKDWIFSIAWIND-TMAVSGSRDGSMGLWE 211
Cdd:pfam00400   8 EGHTGSVTSLAFSPDgKLLASGSDDGTVKVWD 39
 
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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