Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988826    280 GNFTSPNYPNDYDSYTEQMFYLTVADGFQVNVTIDDFLTEN----RFDVLEVYDNYTIpGVNMIANLTGDSIAPWNWLSQ 355
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESsdncEYDYVEIYDGPSA-SSPLLGRFCGSEAPPPVISSS 79

                           90       100
                   ....*....|....*....|...
gi 71988826    356 SSHVTMRFRTDGSVQKRGFHGYW 378
Cdd:smart00042  80 SNSLTLTFVSDSSVQKRGFSARY 102

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988826    169 GNITSPGYPVQYYNNLDCLYTITSPNKTYITLTFNPYLVEGYV----DYVLIYDGPDTTYPSLG--STSSALKLEYESTN 242
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGrfCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 71988826    243 NSVTLKFHTDRSITNKGWLLKW 264
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988826    280 GNFTSPNYPNDYDSYTEQMFYLTVADGFQVNVTIDDFLTEN----RFDVLEVYDNYTIpGVNMIANLTGDSIAPWNWLSQ 355
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESsdncEYDYVEIYDGPSA-SSPLLGRFCGSEAPPPVISSS 79

                           90       100
                   ....*....|....*....|...
gi 71988826    356 SSHVTMRFRTDGSVQKRGFHGYW 378
Cdd:smart00042  80 SNSLTLTFVSDSSVQKRGFSARY 102

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988826     26 CPSGWSFSNEtsYCYIVSDRYMPFSETSSYCQSLGGTQVFISLSYEFTFMKTFTQGLFAQ--PWLSITRDPTDNKWYNPD 103
Cdd:smart00034   1 CPSGWISYGG--KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSD 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 71988826    104 GTTPFI-SWWSTGEPSL-NGDCATFkSTDPQGMKATPCWSIQPAMCK 148
Cdd:smart00034  79 GSGPVSySNWAPGEPNNsSGDCVVL-STSGGKWNDVSCTSKLPFVCE 124

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 71988826  38 YCYIVSDRYMPFSETSSYCQSLGGTQVFISLSYEFTFMKTFTQGLFAQP-WLSITRDPTDNKWYNPDGTTPFI-SWWSTG 115
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDvWIGLNDLSSEGTWKWSDGSPLVDyTNWAPG 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 71988826 116 EPSLNG--DCATFKSTDPQGMKATPCWSIQPAMCKQ 149
Cdd:cd00037  81 EPNPGGseDCVVLSSSSDGKWNDVSCSSKLPFICEK 116

C-type lectin-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988826    9 FLFFVSTFSDVTADNSLCPSGW-SFSNEtsyCYIVSDRYMPFSETSSYCQSLGGTQVFISLSYEFTFMKTFTQGlfAQPW 87
Cdd:PHA02642  71 LMAFKSDTQEPTIKYVTCPKGWiGFGYK---CFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDS--SDHW 145

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 71988826   88 LSITRDPTDNKWYNPDGTTPFISWWSTGepslNGDCA 124
Cdd:PHA02642 146 IGLNRESSNHPWKWADNSNYNASFVITG----TGECA 178

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988826    169 GNITSPGYPVQYYNNLDCLYTITSPNKTYITLTFNPYLVEGYV----DYVLIYDGPDTTYPSLG--STSSALKLEYESTN 242
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGrfCGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 71988826    243 NSVTLKFHTDRSITNKGWLLKW 264
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988826    280 GNFTSPNYPNDYDSYTEQMFYLTVADGFQVNVTIDDFLTEN----RFDVLEVYDNYTIpGVNMIANLTGDSIAPWNWLSQ 355
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESsdncEYDYVEIYDGPSA-SSPLLGRFCGSEAPPPVISSS 79

                           90       100
                   ....*....|....*....|...
gi 71988826    356 SSHVTMRFRTDGSVQKRGFHGYW 378
Cdd:smart00042  80 SNSLTLTFVSDSSVQKRGFSARY 102

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988826     26 CPSGWSFSNEtsYCYIVSDRYMPFSETSSYCQSLGGTQVFISLSYEFTFMKTFTQGLFAQ--PWLSITRDPTDNKWYNPD 103
Cdd:smart00034   1 CPSGWISYGG--KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSD 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 71988826    104 GTTPFI-SWWSTGEPSL-NGDCATFkSTDPQGMKATPCWSIQPAMCK 148
Cdd:smart00034  79 GSGPVSySNWAPGEPNNsSGDCVVL-STSGGKWNDVSCTSKLPFVCE 124

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 71988826  38 YCYIVSDRYMPFSETSSYCQSLGGTQVFISLSYEFTFMKTFTQGLFAQP-WLSITRDPTDNKWYNPDGTTPFI-SWWSTG 115
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDvWIGLNDLSSEGTWKWSDGSPLVDyTNWAPG 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 71988826 116 EPSLNG--DCATFKSTDPQGMKATPCWSIQPAMCKQ 149
Cdd:cd00037  81 EPNPGGseDCVVLSSSSDGKWNDVSCSSKLPFICEK 116

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        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988826  40 YIVSDRYMPFSETSSYCQSLGGTQVFISLSYEFTFMKTfTQGLFAQPWLSITRDPTDNKWYNPDGTTPFISWWSTGEPSL 119
Cdd:cd03603   3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLS-NFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHN 81

                ...
gi 71988826 120 NGD 122
Cdd:cd03603  82 NGG 84

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988826  26 CPSGWsFSNETSyCYIVSDRYMPFSETSSYCQSLGGTQVFISLSYEFTFMKTFTQGLFaqPWLSITRDPTDNKWYNPDGT 105
Cdd:cd03593   1 CPKDW-ICYGNK-CYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSS--YWIGLSREKSEKPWKWIDGS 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 71988826 106 TPFiSWWSTGEPSLNGDCATFKSTdpqGMKATPCWSIQPAMCKQ 149
Cdd:cd03593  77 PLN-NLFNIRGSTKSGNCAYLSST---GIYSEDCSTKKRWICEK 116

C-type lectin-like protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988826    9 FLFFVSTFSDVTADNSLCPSGW-SFSNEtsyCYIVSDRYMPFSETSSYCQSLGGTQVFISLSYEFTFMKTFTQGlfAQPW 87
Cdd:PHA02642  71 LMAFKSDTQEPTIKYVTCPKGWiGFGYK---CFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDS--SDHW 145

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 71988826   88 LSITRDPTDNKWYNPDGTTPFISWWSTGepslNGDCA 124
Cdd:PHA02642 146 IGLNRESSNHPWKWADNSNYNASFVITG----TGECA 178