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Conserved domains on  [gi|115534356|ref|NP_500439|]
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C-type lectin domain-containing protein [Caenorhabditis elegans]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10441677)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein similar to Caenorhabditis elegans C-type lectin domain-containing protein 87

CATH:  3.10.100.10
Gene Ontology:  GO:0030246
PubMed:  16336259|10508765
SCOP:  4002453

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
 39-147 2.66e-17

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


:

Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 77.13  E-value: 2.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534356   39 QMTYTDARNWCHYKNpvgsSYLAYVPDQKTSNYLAFYArtafGPAAQHFWIGLSKNGSSGSLTWDNGSPVGYTNLG--SQ 116
Cdd:pfam00059   1 SKTWDEAREACRKLG----GHLVSINSAEELDFLSSTL----KKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWApePN 72

                          90       100       110
                  ....*....|....*....|....*....|...
gi 115534356  117 NGNNLYFTESLANT--KWNTLGDDKINYFVCSY 147
Cdd:pfam00059  73 NNGENEDCVELSSSsgKWNDENCNSKNPFVCEK 105
 
Name Accession Description Interval E-value
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 39-147 2.66e-17

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 77.13  E-value: 2.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534356   39 QMTYTDARNWCHYKNpvgsSYLAYVPDQKTSNYLAFYArtafGPAAQHFWIGLSKNGSSGSLTWDNGSPVGYTNLG--SQ 116
Cdd:pfam00059   1 SKTWDEAREACRKLG----GHLVSINSAEELDFLSSTL----KKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWApePN 72

                          90       100       110
                  ....*....|....*....|....*....|...
gi 115534356  117 NGNNLYFTESLANT--KWNTLGDDKINYFVCSY 147
Cdd:pfam00059  73 NNGENEDCVELSSSsgKWNDENCNSKNPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 20-145 3.05e-17

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: 77.64  E-value: 3.05e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534356    20 CPdSNDHEVQGFCFKFVAQQMTYTDARNWCHYKNpvgsSYLAYVPDQKTSNYLAFYARTAFGPaaQHFWIGLSKNGSSGS 99
Cdd:smart00034   1 CP-SGWISYGGKCYKFSTEKKTWEDAQAFCQSLG----GHLASIHSEAENDFVASLLKNSGSS--DYYWIGLSDPDSNGS 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 115534356   100 LTWDNGSP-VGYTNLGS---QNGNNLYFTESLANTKWNTLGDDKINYFVC 145
Cdd:smart00034  74 WQWSDGSGpVSYSNWAPgepNNSSGDCVVLSTSGGKWNDVSCTSKLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 31-147 1.12e-13

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: 67.26  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534356  31 FCFKFVAQQMTYTDARNWCHYKNpvgsSYLAYVPDQKTSNYLAFYARTAFGpaaQHFWIGLSKNGSSGSLTWDNGSP-VG 109
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLG----GHLASIHSEEENDFLASLLKKSSS---SDVWIGLNDLSSEGTWKWSDGSPlVD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 115534356 110 YTN------LGSQNGNNLYFTeSLANTKWNTLGDDKINYFVCSY 147
Cdd:cd00037   74 YTNwapgepNPGGSEDCVVLS-SSSDGKWNDVSCSSKLPFICEK 116
 
Name Accession Description Interval E-value
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 39-147 2.66e-17

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 77.13  E-value: 2.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534356   39 QMTYTDARNWCHYKNpvgsSYLAYVPDQKTSNYLAFYArtafGPAAQHFWIGLSKNGSSGSLTWDNGSPVGYTNLG--SQ 116
Cdd:pfam00059   1 SKTWDEAREACRKLG----GHLVSINSAEELDFLSSTL----KKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWApePN 72

                          90       100       110
                  ....*....|....*....|....*....|...
gi 115534356  117 NGNNLYFTESLANT--KWNTLGDDKINYFVCSY 147
Cdd:pfam00059  73 NNGENEDCVELSSSsgKWNDENCNSKNPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 20-145 3.05e-17

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: 77.64  E-value: 3.05e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534356    20 CPdSNDHEVQGFCFKFVAQQMTYTDARNWCHYKNpvgsSYLAYVPDQKTSNYLAFYARTAFGPaaQHFWIGLSKNGSSGS 99
Cdd:smart00034   1 CP-SGWISYGGKCYKFSTEKKTWEDAQAFCQSLG----GHLASIHSEAENDFVASLLKNSGSS--DYYWIGLSDPDSNGS 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 115534356   100 LTWDNGSP-VGYTNLGS---QNGNNLYFTESLANTKWNTLGDDKINYFVC 145
Cdd:smart00034  74 WQWSDGSGpVSYSNWAPgepNNSSGDCVVLSTSGGKWNDVSCTSKLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 31-147 1.12e-13

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: 67.26  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534356  31 FCFKFVAQQMTYTDARNWCHYKNpvgsSYLAYVPDQKTSNYLAFYARTAFGpaaQHFWIGLSKNGSSGSLTWDNGSP-VG 109
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLG----GHLASIHSEEENDFLASLLKKSSS---SDVWIGLNDLSSEGTWKWSDGSPlVD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 115534356 110 YTN------LGSQNGNNLYFTeSLANTKWNTLGDDKINYFVCSY 147
Cdd:cd00037   74 YTNwapgepNPGGSEDCVVLS-SSSDGKWNDVSCSSKLPFICEK 116
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 29-145 8.73e-11

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: 59.68  E-value: 8.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534356  29 QGFCFKFVAQQMTYTDARNWCH-YKNPVGSSYLAYVPDQKTSNYLAFYARTAFGP--AAQHfWIGLSKNGSSGSLTWDNG 105
Cdd:cd03589    9 GGYCYRFFGDRLTWEEAELRCRsFSIPGLIAHLVSIHSQEENDFVYDLFESSRGPdtPYGL-WIGLHDRTSEGPFEWTDG 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 115534356 106 SPVGYTNLGSQNGNNLYFTE--------SLANTKWNTLGDDKINYFVC 145
Cdd:cd03589   88 SPVDFTKWAGGQPDNYGGNEdcvqmwrrGDAGQSWNDMPCDAVFPYIC 135
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 82-144 3.81e-05

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: 42.80  E-value: 3.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115534356  82 PAAQHFWIGLSKNGSSGSLTWDNGSPVGYTN--------LGSQNGNNLYFTESLANT-KWNTLGDDKINYFV 144
Cdd:cd03603   43 GGYGASWIGASDAATEGTWKWSDGEESTYTNwgsgephnNGGGNEDYAAINHFPGISgKWNDLANSYNTLGY 114
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 30-147 4.04e-05

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 43.13  E-value: 4.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534356  30 GFCFKFVAQQMTYTDARNWCH-YKNpvgSSYLAYVPDQKTSNYLAFYArTAFGPAAQHFWIGLSKNGSSGSLTWDNGSpv 108
Cdd:cd03594   10 GNCYGYFRQPLSWSDAELFCQkYGP---GAHLASIHSPAEAAAIASLI-SSYQKAYQPVWIGLHDPQQSRGWEWSDGS-- 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 115534356 109 gYTNLGSQNGNNLY--------FTESLANTKWNTLGDDKINYFVCSY 147
Cdd:cd03594   84 -KLDYRSWDRNPPYarggycaeLSRSTGFLKWNDANCEERNPFICKY 129
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 32-120 6.98e-05

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: 42.32  E-value: 6.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534356  32 CFKFVAQQMTYTDARNWCHYKNpvgsSYLAYVPDQKTSNYLAFYARTAFgpaaqhFWIGLSKNGSSGSLTWDNGSPvgYT 111
Cdd:cd03593   12 CYYFSMEKKTWNESKEACSSKN----SSLLKIDDEEELEFLQSQIGSSS------YWIGLSREKSEKPWKWIDGSP--LN 79


                 ....*....
gi 115534356 112 NLGSQNGNN 120
Cdd:cd03593   80 NLFNIRGST 88
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 33-112 3.88e-03

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of 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. 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: 153072  Cd Length: 108  Bit Score: 36.97  E-value: 3.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534356  33 FKFVAQQMTYTDARNWC--HYKNpvgssyLAYVPDQKTSNYLAFYARTAFGPAaqhfWIGLSKngSSGSLTWDNGSPVGY 110
Cdd:cd03602    3 FYLVNESKTWSEAQQYCreNYTD------LATVQNQEDNALLSNLSRVSNSAA----WIGLYR--DVDSWRWSDGSESSF 70


                 ..
gi 115534356 111 TN 112
Cdd:cd03602   71 RN 72
 
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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