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Conserved domains on  [gi|569001211|ref|XP_006524786|]
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tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit WDR4 isoform X2 [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 ...
 33-128 5.31e-12

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: 65.05  E-value: 5.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211  33 LEPDGCGRLELGHLSMLLDVAVSPDDQFVLTADRDEKIRVsWAAAPHSIESFCLGHTEFVSRILVVPShPELLLSSSGDG 112
Cdd:cd00200  122 VETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKL-WDLRTGKCVATLTGHTGEVNSVAFSPD-GEKLLSSSSDG 199

                         90
                 ....*....|....*.
gi 569001211 113 TLRLWEYRSGRQLQCC 128
Cdd:cd00200  200 TIKLWDLSTGKCLGTL 215
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 33-128 5.31e-12

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: 65.05  E-value: 5.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211  33 LEPDGCGRLELGHLSMLLDVAVSPDDQFVLTADRDEKIRVsWAAAPHSIESFCLGHTEFVSRILVVPShPELLLSSSGDG 112
Cdd:cd00200  122 VETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKL-WDLRTGKCVATLTGHTGEVNSVAFSPD-GEKLLSSSSDG 199

                         90
                 ....*....|....*.
gi 569001211 113 TLRLWEYRSGRQLQCC 128
Cdd:cd00200  200 TIKLWDLSTGKCLGTL 215
WD40 COG2319
WD40 repeat [General function prediction only];
7-160 4.87e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 59.92  E-value: 4.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211   7 TALTFTASEDRVLVADKSGDVYSFSVlEPDGCGRLELGHLSMLLDVAVSPDDQFVLTADRDEKIRVsWAAAPHSIESFCL 86
Cdd:COG2319  250 RSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRL-WDLATGKLLRTLT 327

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569001211  87 GHTEFVSRILVVPShPELLLSSSGDGTLRLWeyrsgrqlqccDLAGLQEPGEQPGHKGlAASRIAFWGQESYVV 160
Cdd:COG2319  328 GHTGAVRSVAFSPD-GKTLASGSDDGTVRLW-----------DLATGELLRTLTGHTG-AVTSVAFSPDGRTLA 388
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 87-118 6.89e-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: 33.83  E-value: 6.89e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 569001211    87 GHTEFVSRILVVPSHPeLLLSSSGDGTLRLWE 118
Cdd:smart00320  10 GHTGPVTSVAFSPDGK-YLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
87-118 9.59e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 33.47  E-value: 9.59e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 569001211   87 GHTEFVSRILVVPSHPeLLLSSSGDGTLRLWE 118
Cdd:pfam00400   9 GHTGSVTSLAFSPDGK-LLASGSDDGTVKVWD 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 ...
 33-128 5.31e-12

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: 65.05  E-value: 5.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211  33 LEPDGCGRLELGHLSMLLDVAVSPDDQFVLTADRDEKIRVsWAAAPHSIESFCLGHTEFVSRILVVPShPELLLSSSGDG 112
Cdd:cd00200  122 VETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKL-WDLRTGKCVATLTGHTGEVNSVAFSPD-GEKLLSSSSDG 199

                         90
                 ....*....|....*.
gi 569001211 113 TLRLWEYRSGRQLQCC 128
Cdd:cd00200  200 TIKLWDLSTGKCLGTL 215
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 44-126 7.68e-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: 61.58  E-value: 7.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211  44 GHLSMLLDVAVSPDDQFVLTADRDEKIRVsWAAAPHSIESFCLGHTEFVSRILVVPSHpELLLSSSGDGTLRLWEYRSGR 123
Cdd:cd00200    7 GHTGGVTCVAFSPDGKLLATGSGDGTIKV-WDLETGELLRTLKGHTGPVRDVAASADG-TYLASGSSDKTIRLWDLETGE 84


                 ...
gi 569001211 124 QLQ 126
Cdd:cd00200   85 CVR 87
WD40 COG2319
WD40 repeat [General function prediction only];
7-160 4.87e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 59.92  E-value: 4.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211   7 TALTFTASEDRVLVADKSGDVYSFSVlEPDGCGRLELGHLSMLLDVAVSPDDQFVLTADRDEKIRVsWAAAPHSIESFCL 86
Cdd:COG2319  250 RSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRL-WDLATGKLLRTLT 327

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569001211  87 GHTEFVSRILVVPShPELLLSSSGDGTLRLWeyrsgrqlqccDLAGLQEPGEQPGHKGlAASRIAFWGQESYVV 160
Cdd:COG2319  328 GHTGAVRSVAFSPD-GKTLASGSDDGTVRLW-----------DLATGELLRTLTGHTG-AVTSVAFSPDGRTLA 388
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 44-123 5.93e-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: 58.89  E-value: 5.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211  44 GHLSMLLDVAVSPDDQFVLTADRDEKIRVsWAAAPHSIESFCLGHTEFVSRILVVPSHPeLLLSSSGDGTLRLWEYRSGR 123
Cdd:cd00200   91 GHTSYVSSVAFSPDGRILSSSSRDKTIKV-WDVETGKCLTTLRGHTDWVNSVAFSPDGT-FVASSSQDGTIKLWDLRTGK 168
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-128 6.05e-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: 58.89  E-value: 6.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211   5 RCTALTFTASEDRVLVADKSGDVYSFSvLEPDGCGRLELGHLSMLLDVAVSPDDQFVLTADRDEKIRVSWAAAPHSIESF 84
Cdd:cd00200   11 GVTCVAFSPDGKLLATGSGDGTIKVWD-LETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTL 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 569001211  85 cLGHTEFVSRILVVPSHPeLLLSSSGDGTLRLWEYRSGRQLQCC 128
Cdd:cd00200   90 -TGHTSYVSSVAFSPDGR-ILSSSSRDKTIKVWDVETGKCLTTL 131
WD40 COG2319
WD40 repeat [General function prediction only];
44-126 7.61e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 59.15  E-value: 7.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211  44 GHLSMLLDVAVSPDDQFVLTADRDEKIRVsWAAAPHSIESFCLGHTEFVSRILVVPShPELLLSSSGDGTLRLWEYRSGR 123
Cdd:COG2319  244 GHSGSVRSVAFSPDGRLLASGSADGTVRL-WDLATGELLRTLTGHSGGVNSVAFSPD-GKLLASGSDDGTVRLWDLATGK 321


                 ...
gi 569001211 124 QLQ 126
Cdd:COG2319  322 LLR 324
WD40 COG2319
WD40 repeat [General function prediction only];
7-117 1.40e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.38  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211   7 TALTFTASEDRVLVADKSGDVYSFSVLEPDGCGRLElGHLSMLLDVAVSPDDQFVLTADRDEKIRVsWAAAPHSIESFCL 86
Cdd:COG2319  292 NSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSPDGKTLASGSDDGTVRL-WDLATGELLRTLT 369

                         90       100       110
                 ....*....|....*....|....*....|.
gi 569001211  87 GHTEFVSRILVVPSHpELLLSSSGDGTLRLW 117
Cdd:COG2319  370 GHTGAVTSVAFSPDG-RTLASGSADGTVRLW 399
WD40 COG2319
WD40 repeat [General function prediction only];
7-126 1.63e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.38  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211   7 TALTFTASEDRVLVADKSGDVYSFSVlEPDGCGRLELGHLSMLLDVAVSPDDQFVLTADRDEKIRVsW-AAAPHSIESFc 85
Cdd:COG2319   82 LSVAFSPDGRLLASASADGTVRLWDL-ATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRL-WdLATGKLLRTL- 158

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 569001211  86 LGHTEFVSRILVVPSHpELLLSSSGDGTLRLWEYRSGRQLQ 126
Cdd:COG2319  159 TGHSGAVTSVAFSPDG-KLLASGSDDGTVRLWDLATGKLLR 198
WD40 COG2319
WD40 repeat [General function prediction only];
13-126 1.85e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.00  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211  13 ASEDRVLVADKSGDVYSFSVLEPDGCGRLELGHLSMLLDVAVSPDDQFVLTADRDEKIRVsWAAAPHSIESFCLGHTEFV 92
Cdd:COG2319   45 SPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRL-WDLATGLLLRTLTGHTGAV 123

                         90       100       110
                 ....*....|....*....|....*....|....
gi 569001211  93 SRILVVPSHpELLLSSSGDGTLRLWEYRSGRQLQ 126
Cdd:COG2319  124 RSVAFSPDG-KTLASGSADGTVRLWDLATGKLLR 156
WD40 COG2319
WD40 repeat [General function prediction only];
7-126 5.46e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.84  E-value: 5.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211   7 TALTFTASEDRVLVADKSGDVYSFSVLEPDGCGRLElGHLSMLLDVAVSPDDQFVLTADRDEKIRVsWAAAPHSIESFCL 86
Cdd:COG2319  166 TSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSPDGKLLASGSADGTVRL-WDLATGKLLRTLT 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 569001211  87 GHTEFVSRILVVPSHpELLLSSSGDGTLRLWEYRSGRQLQ 126
Cdd:COG2319  244 GHSGSVRSVAFSPDG-RLLASGSADGTVRLWDLATGELLR 282
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 7-118 5.49e-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: 5.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001211   7 TALTFTASEDRVLVADKSGDVYSFSVLEPDGCGRLElGHLSMLLDVAVSPDDQFVLTADRDEKIRVsWAAAPHSIESFCL 86
Cdd:cd00200  181 NSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRV-WDLRTGECVQTLS 258

                         90       100       110
                 ....*....|....*....|....*....|..
gi 569001211  87 GHTEFVSRILVVPSHPeLLLSSSGDGTLRLWE 118
Cdd:cd00200  259 GHTNSVTSLAWSPDGK-RLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 87-118 6.89e-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: 33.83  E-value: 6.89e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 569001211    87 GHTEFVSRILVVPSHPeLLLSSSGDGTLRLWE 118
Cdd:smart00320  10 GHTGPVTSVAFSPDGK-YLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
87-118 9.59e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 33.47  E-value: 9.59e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 569001211   87 GHTEFVSRILVVPSHPeLLLSSSGDGTLRLWE 118
Cdd:pfam00400   9 GHTGSVTSLAFSPDGK-LLASGSDDGTVKVWD 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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