CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648 160 GGQYTG--SGTITSPGYPNQYYNNLDCVYTILSPNNTYITMQFSPYMVEEY----FDWIDLFDGPNTTYPFLGTTDDwWS 233
Cdd:cd00041    2 GGTLTAstSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSpncsYDYLEIYDGPSTSSPLLGRFCG-ST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 193207648 234 LRFNFESSSNAVSFIFHTDSIVTDKGWLLTWSA 266
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648  37 YCYIQSAQYLSYSEASNYCQSIGGTQVFIFTLRELTWLTDFTSSSFAQP-WLATTRNITTDKWYNSDGTTPAA-TYWTSG 114
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDvWIGLNDLSSEGTWKWSDGSPLVDyTNWAPG 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 193207648 115 EPGVNG--DCATFKGAGASGLKATQCYSIQPALC 146
Cdd:cd00037   81 EPNPGGseDCVVLSSSSDGKWNDVSCSSKLPFIC 114

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648 160 GGQYTG--SGTITSPGYPNQYYNNLDCVYTILSPNNTYITMQFSPYMVEEY----FDWIDLFDGPNTTYPFLGTTDDwWS 233
Cdd:cd00041    2 GGTLTAstSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSpncsYDYLEIYDGPSTSSPLLGRFCG-ST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 193207648 234 LRFNFESSSNAVSFIFHTDSIVTDKGWLLTWSA 266
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648 276 SGQNGSFTSPNYPNNYDPYTEQIYYVNAPTGFQVNLTIPDFVTEA----NYDVLEIYNTSTVISSgLVANLSGSaVAPYS 351
Cdd:cd00041    7 ASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSP-LLGRFCGS-TLPPP 84

                         90       100
                 ....*....|....*....|....*....
gi 193207648 352 WLSPSNYVTMRFRSDGVVQKQGFSIVWFI 380
Cdd:cd00041   85 IISSGNSLTVRFRSDSSVTGRGFKATYSA 113

CUB domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648  160 GGQYTG-SGTITSPGYPNQYYNNLDCVYTILSPNNTYITMQFSPYMVEE----YFDWIDLFDGPNTTYPFLGttddwwsl 234
Cdd:pfam00431   2 GGVLTDsSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDhdecGYDYVEIRDGPSASSPLLG-------- 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 193207648  235 RF-------NFESSSNAVSFIFHTDSIVTDKGWLLT 263
Cdd:pfam00431  74 RFcgsgipeDIVSSSNQMTIKFVSDASVQKRGFKAT 109

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648  37 YCYIQSAQYLSYSEASNYCQSIGGTQVFIFTLRELTWLTDFTSSSFAQP-WLATTRNITTDKWYNSDGTTPAA-TYWTSG 114
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDvWIGLNDLSSEGTWKWSDGSPLVDyTNWAPG 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 193207648 115 EPGVNG--DCATFKGAGASGLKATQCYSIQPALC 146
Cdd:cd00037   81 EPNPGGseDCVVLSSSSDGKWNDVSCSSKLPFIC 114

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648   46 LSYSEASNYCQSIGGTQVFIFTLRELTWLTDFTSSSFAQPWLATTRNITTDKWYNSDGTTPAATYW--TSGEPGVNGDCA 123
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWapEPNNNGENEDCV 81

                          90       100
                  ....*....|....*....|....*
gi 193207648  124 TFkGAGASGLKATQCYSIQPALCRQ 148
Cdd:pfam00059  82 EL-SSSSGKWNDENCNSKNPFVCEK 105

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648 160 GGQYTG--SGTITSPGYPNQYYNNLDCVYTILSPNNTYITMQFSPYMVEEY----FDWIDLFDGPNTTYPFLGTTDDwWS 233
Cdd:cd00041    2 GGTLTAstSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESSpncsYDYLEIYDGPSTSSPLLGRFCG-ST 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 193207648 234 LRFNFESSSNAVSFIFHTDSIVTDKGWLLTWSA 266
Cdd:cd00041   81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648 276 SGQNGSFTSPNYPNNYDPYTEQIYYVNAPTGFQVNLTIPDFVTEA----NYDVLEIYNTSTVISSgLVANLSGSaVAPYS 351
Cdd:cd00041    7 ASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSP-LLGRFCGS-TLPPP 84

                         90       100
                 ....*....|....*....|....*....
gi 193207648 352 WLSPSNYVTMRFRSDGVVQKQGFSIVWFI 380
Cdd:cd00041   85 IISSGNSLTVRFRSDSSVTGRGFKATYSA 113

CUB domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648  160 GGQYTG-SGTITSPGYPNQYYNNLDCVYTILSPNNTYITMQFSPYMVEE----YFDWIDLFDGPNTTYPFLGttddwwsl 234
Cdd:pfam00431   2 GGVLTDsSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDhdecGYDYVEIRDGPSASSPLLG-------- 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 193207648  235 RF-------NFESSSNAVSFIFHTDSIVTDKGWLLT 263
Cdd:pfam00431  74 RFcgsgipeDIVSSSNQMTIKFVSDASVQKRGFKAT 109

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648  37 YCYIQSAQYLSYSEASNYCQSIGGTQVFIFTLRELTWLTDFTSSSFAQP-WLATTRNITTDKWYNSDGTTPAA-TYWTSG 114
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDvWIGLNDLSSEGTWKWSDGSPLVDyTNWAPG 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 193207648 115 EPGVNG--DCATFKGAGASGLKATQCYSIQPALC 146
Cdd:cd00037   81 EPNPGGseDCVVLSSSSDGKWNDVSCSSKLPFIC 114

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648  25 CPSGWTFSTntSYCYIQSAQYLSYSEASNYCQSIGGTQVFIFTLRELTWLTDFTSSSFAQpWLATTRNITTDKWYNSDGT 104
Cdd:cd03590    1 CPTNWKSFQ--SSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSY-WIGLSDEETEGEWKWVDGT 77

                         90       100
                 ....*....|....*....|....*..
gi 193207648 105 TPAA--TYWTSGEP----GVNGDCATF 125
Cdd:cd03590   78 PLNSskTFWHPGEPnnwgGGGEDCAEL 104

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648  25 CPSGWTFSTNtsYCYIQSAQYLSYSEASNYCQ--SIGGTQ---VFIFTLRELTWLTDFTSSSFAQP-----WLATTRNIT 94
Cdd:cd03589    1 CPTFWTAFGG--YCYRFFGDRLTWEEAELRCRsfSIPGLIahlVSIHSQEENDFVYDLFESSRGPDtpyglWIGLHDRTS 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 193207648  95 TDKWYNSDGTTPAATYWTSGEP---GVNGDCATFKGAGASGLK 134
Cdd:cd03589   79 EGPFEWTDGSPVDFTKWAGGQPdnyGGNEDCVQMWRRGDAGQS 121

C-type lectin-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193207648   5 VLTALLFAANIQVVTADVNHCPSGWT-FSTNtsyCYIQSAQYLSYSEASNYCQSIGGTQVFIFTLRELTWLTDFTSSSfa 83
Cdd:PHA02642  68 IIILMAFKSDTQEPTIKYVTCPKGWIgFGYK---CFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSS-- 142

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193207648  84 QPWLATTRNITTDKWYNSDGTTPAATYWTSGepgvNGDCATFKGAGASglkATQCYSIQPALCRQMPA--LCPSQTSY 159
Cdd:PHA02642 143 DHWIGLNRESSNHPWKWADNSNYNASFVITG----TGECAYLNDIRIS---SSRVYANRKWICSKTYTniYIPSNNSY 213

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.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193207648  47 SYSEASNYCQSIGGTQVFIFTLRELTWLTDfTSSSFAQPWLATTRNITTDKWYNSDGTTPAATYWTSGEPGVNGD 121
Cdd:cd03603   11 TWEAAQTLAESLGGHLVTINSAEENDWLLS-NFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNNGG 84