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Conserved domains on  [gi|1254006590|ref|NP_001343800|]
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C-type lectin domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 38-145 2.39e-14

Lectin C-type domain; This family includes both long and short form C-type


:

Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 68.66  E-value: 2.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006590  38 KMTYNDARNWCHHQNpvgpSYLAYVPKKDTSSYLAFYARSAfgvdAQQFWIGLFRNVSSGMLSWDNGLPVGYTN---FGS 114
Cdd:pfam00059   1 SKTWDEAREACRKLG----GHLVSINSAEELDFLSSTLKKS----NKYFWIGLTDRKNEGTWKWVDGSPVNYTNwapEPN 72

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1254006590 115 HVGENYFYEKISNT--KWDTLGDNDVNYFVCSY 145
Cdd:pfam00059  73 NNGENEDCVELSSSsgKWNDENCNSKNPFVCEK 105
BTHB super family cl39748
basic tilted helix bundle (BTHB) domain; BTHB domain is found in the N-terminal region of ...
 232-281 4.91e-03

basic tilted helix bundle (BTHB) domain; BTHB domain is found in the N-terminal region of FKBPs such as FKBP25 and in the core region of E3 ubiquitin ligase HectD1. It adopts a compact 5-helix bundle, hence termed BTHB (Basic Tilted Helix Bundle) domain. In FKBP25, it may have a role in regulating the association state of nucleosomes by interacting with nucleolin. This basic domain in FKBP25 also forms alternative complexes with other chromatin-related proteins, such as the HDAC1, HDAC2, and the transcriptional regulator YY1, the DNA binding activity of which is enhanced on binding FKBP25. Structural analysis of this fold suggests that the DNA binding properties of FKBP25 and HectD1 are presented by the conserved basic region.


The actual alignment was detected with superfamily member cd21062:

Pssm-ID: 477119  Cd Length: 66  Bit Score: 35.34  E-value: 4.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254006590 232 VSYVSSHLpnstlafgdsttGSNVL---DVINYLEKN----FLRKFEFSG--KFCRRAR 281
Cdd:cd21062     4 VEYVEQSL------------GTGELpksDVITYLQKNadeaFLRRWKLTGtaKNIRKNR 50
 
Name Accession Description Interval E-value
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 38-145 2.39e-14

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 68.66  E-value: 2.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006590  38 KMTYNDARNWCHHQNpvgpSYLAYVPKKDTSSYLAFYARSAfgvdAQQFWIGLFRNVSSGMLSWDNGLPVGYTN---FGS 114
Cdd:pfam00059   1 SKTWDEAREACRKLG----GHLVSINSAEELDFLSSTLKKS----NKYFWIGLTDRKNEGTWKWVDGSPVNYTNwapEPN 72

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1254006590 115 HVGENYFYEKISNT--KWDTLGDNDVNYFVCSY 145
Cdd:pfam00059  73 NNGENEDCVELSSSsgKWNDENCNSKNPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 19-143 7.18e-14

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 68.01  E-value: 7.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006590   19 CPDSNDQEINKlCFKFVAQKMTYNDARNWCHHQNpvgpSYLAYVPKKDTSSYLAFYARSAFGVDaqQFWIGLFRNVSSGM 98
Cdd:smart00034   1 CPSGWISYGGK-CYKFSTEKKTWEDAQAFCQSLG----GHLASIHSEAENDFVASLLKNSGSSD--YYWIGLSDPDSNGS 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1254006590   99 LSWDNGLP-VGYTNFGS----HVGENYFYEKISNTKWDTLGDNDVNYFVC 143
Cdd:smart00034  74 WQWSDGSGpVSYSNWAPgepnNSSGDCVVLSTSGGKWNDVSCTSKLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 31-145 1.91e-11

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 60.71  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006590  31 CFKFVAQKMTYNDARNWCHHQNpvgpSYLAYVPKKDTSSYLAFYARSAfgvDAQQFWIGLFRNVSSGMLSWDNGLP-VGY 109
Cdd:cd00037     2 CYKFSTEKLTWEEAQEYCRSLG----GHLASIHSEEENDFLASLLKKS---SSSDVWIGLNDLSSEGTWKWSDGSPlVDY 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1254006590 110 TNFGSHVGENYFYE------KISNTKWDTLGDNDVNYFVCSY 145
Cdd:cd00037    75 TNWAPGEPNPGGSEdcvvlsSSSDGKWNDVSCSSKLPFICEK 116
BTHB_HectD1 cd21062
basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and ...
 232-281 4.91e-03

basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and similar proteins; HectD1, also called E3 ligase for inhibin receptor (EULIR), is a Hect-type E3 ubiquitin transferase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. HectD1 is required for development of head mesenchyme and neural tube closure.


Pssm-ID: 439138  Cd Length: 66  Bit Score: 35.34  E-value: 4.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254006590 232 VSYVSSHLpnstlafgdsttGSNVL---DVINYLEKN----FLRKFEFSG--KFCRRAR 281
Cdd:cd21062     4 VEYVEQSL------------GTGELpksDVITYLQKNadeaFLRRWKLTGtaKNIRKNR 50
 
Name Accession Description Interval E-value
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 38-145 2.39e-14

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 68.66  E-value: 2.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006590  38 KMTYNDARNWCHHQNpvgpSYLAYVPKKDTSSYLAFYARSAfgvdAQQFWIGLFRNVSSGMLSWDNGLPVGYTN---FGS 114
Cdd:pfam00059   1 SKTWDEAREACRKLG----GHLVSINSAEELDFLSSTLKKS----NKYFWIGLTDRKNEGTWKWVDGSPVNYTNwapEPN 72

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1254006590 115 HVGENYFYEKISNT--KWDTLGDNDVNYFVCSY 145
Cdd:pfam00059  73 NNGENEDCVELSSSsgKWNDENCNSKNPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 19-143 7.18e-14

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 68.01  E-value: 7.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006590   19 CPDSNDQEINKlCFKFVAQKMTYNDARNWCHHQNpvgpSYLAYVPKKDTSSYLAFYARSAFGVDaqQFWIGLFRNVSSGM 98
Cdd:smart00034   1 CPSGWISYGGK-CYKFSTEKKTWEDAQAFCQSLG----GHLASIHSEAENDFVASLLKNSGSSD--YYWIGLSDPDSNGS 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1254006590   99 LSWDNGLP-VGYTNFGS----HVGENYFYEKISNTKWDTLGDNDVNYFVC 143
Cdd:smart00034  74 WQWSDGSGpVSYSNWAPgepnNSSGDCVVLSTSGGKWNDVSCTSKLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 31-145 1.91e-11

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 60.71  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006590  31 CFKFVAQKMTYNDARNWCHHQNpvgpSYLAYVPKKDTSSYLAFYARSAfgvDAQQFWIGLFRNVSSGMLSWDNGLP-VGY 109
Cdd:cd00037     2 CYKFSTEKLTWEEAQEYCRSLG----GHLASIHSEEENDFLASLLKKS---SSSDVWIGLNDLSSEGTWKWSDGSPlVDY 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1254006590 110 TNFGSHVGENYFYE------KISNTKWDTLGDNDVNYFVCSY 145
Cdd:cd00037    75 TNWAPGEPNPGGSEdcvvlsSSSDGKWNDVSCSSKLPFICEK 116
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 31-143 6.59e-05

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.


Pssm-ID: 153059  Cd Length: 137  Bit Score: 42.35  E-value: 6.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006590  31 CFKFVAQKMTYNDARNWCH-HQNPVGPSYLAYVPKKDTSSYLAFYARSAFGVD-AQQFWIGLFRNVSSGMLSWDNGLPVG 108
Cdd:cd03589    12 CYRFFGDRLTWEEAELRCRsFSIPGLIAHLVSIHSQEENDFVYDLFESSRGPDtPYGLWIGLHDRTSEGPFEWTDGSPVD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1254006590 109 YTNFGSHVGENY---------FYEKISNTKWDTLGDNDVNYFVC 143
Cdd:cd03589    92 FTKWAGGQPDNYggnedcvqmWRRGDAGQSWNDMPCDAVFPYIC 135
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 32-142 7.31e-04

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 38.94  E-value: 7.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1254006590  32 FKFVAQKMTYNDARNWCH-HQnpvgpSYLAYVpkkdTSSYLAFYARSAFGvDAQQFWIGLFRNVSSGMLSWDNGLPVGYT 110
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAEsLG-----GHLVTI----NSAEENDWLLSNFG-GYGASWIGASDAATEGTWKWSDGEESTYT 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1254006590 111 NFGSHV-------GENYFYE---KISNTKWDTLGDNDVNYFV 142
Cdd:cd03603    73 NWGSGEphnngggNEDYAAInhfPGISGKWNDLANSYNTLGY 114
BTHB_HectD1 cd21062
basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and ...
 232-281 4.91e-03

basic tilted helix bundle (BTHB) domain found in HECT domain-containing protein 1 (HectD1) and similar proteins; HectD1, also called E3 ligase for inhibin receptor (EULIR), is a Hect-type E3 ubiquitin transferase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. HectD1 is required for development of head mesenchyme and neural tube closure.


Pssm-ID: 439138  Cd Length: 66  Bit Score: 35.34  E-value: 4.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1254006590 232 VSYVSSHLpnstlafgdsttGSNVL---DVINYLEKN----FLRKFEFSG--KFCRRAR 281
Cdd:cd21062     4 VEYVEQSL------------GTGELpksDVITYLQKNadeaFLRRWKLTGtaKNIRKNR 50
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 31-106 9.72e-03

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 35.77  E-value: 9.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1254006590  31 CFKFVAQKMTYNDARNWCHHQNpvgpSYLAYVPKKDTSSYLAFYARSAFgvdaqqFWIGLFRNVSSGMLSWDNGLP 106
Cdd:cd03593    12 CYYFSMEKKTWNESKEACSSKN----SSLLKIDDEEELEFLQSQIGSSS------YWIGLSREKSEKPWKWIDGSP 77
 
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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