C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511837976 157 EKFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVaKSGFFRVFIGVNDLEKEGQYVFTDNTPLqNYSNWRE 236
Cdd:cd03591    1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYV-KKGNTYAFIGITDLETEGQFVYLDGGPL-TYTNWKP 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 511837976 237 GEPSDPYGHEDCVEMLSSGRWNDTECHLTMYFVCEF 272
Cdd:cd03591   79 GEPNNAGGGEDCVEMYTSGKWNDVACNLTRLFVCEF 114

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511837976 157 EKFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVaKSGFFRVFIGVNDLEKEGQYVFTDNTPLqNYSNWRE 236
Cdd:cd03591    1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYV-KKGNTYAFIGITDLETEGQFVYLDGGPL-TYTNWKP 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 511837976 237 GEPSDPYGHEDCVEMLSSGRWNDTECHLTMYFVCEF 272
Cdd:cd03591   79 GEPNNAGGGEDCVEMYTSGKWNDVACNLTRLFVCEF 114

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511837976  167 KNYRESLTHCRIRGGMLAMPKDEAANTLIADYVAKSGFFrVFIGVNDLEKEGQYVFTDNTPLqNYSNWReGEPSDPYGHE 246
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY-FWIGLTDRKNEGTWKWVDGSPV-NYTNWA-PEPNNNGENE 78

                          90       100
                  ....*....|....*....|....*..
gi 511837976  247 DCVEM-LSSGRWNDTECHLTMYFVCEF 272
Cdd:pfam00059  79 DCVELsSSSGKWNDENCNSKNPFVCEK 105

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511837976  52 DGEKGDPG---EEGKHGKVGRMGPKGIKGDLGDAGDQGNIGKTGPIGKKGDKGEKGLPGIPGGKGKAGTVCDCG 122
Cdd:NF038329 116 DGEKGEPGpagPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511837976   152 IRETEEKFYYIVQEEKNYRESLTHCRIRGGM-LAMPKDEAANTLIADYVAKSGFFRVFIGVNDLEKEGQYV--FTDNTPL 228
Cdd:TIGR00864  324 IFEENGHCFQIVPEEAAWLDAQEQCLARAGAaLAIVDNDALQNFLARKVTHSLDRGVWIGFSDVNGAEKGPahQGEAFEA 403

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 511837976   229 QNYSNWREGEPSdPYGHEDCVEMLSSGRWNDTECHLTMYFVCEF 272
Cdd:TIGR00864  404 EECEEGLAGEPH-PARAEHCVRLDPRGQCNSDLCNAPHAYVCEL 446

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511837976 157 EKFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVaKSGFFRVFIGVNDLEKEGQYVFTDNTPLqNYSNWRE 236
Cdd:cd03591    1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYV-KKGNTYAFIGITDLETEGQFVYLDGGPL-TYTNWKP 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 511837976 237 GEPSDPYGHEDCVEMLSSGRWNDTECHLTMYFVCEF 272
Cdd:cd03591   79 GEPNNAGGGEDCVEMYTSGKWNDVACNLTRLFVCEF 114

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 511837976   157 EKFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYV-AKSGFFRVFIGVNDLEKEGQYVFTDNTPLQNYSNWR 235
Cdd:smart00034  10 GKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLkNSGSSDYYWIGLSDPDSNGSWQWSDGSGPVSYSNWA 89

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 511837976   236 EGEPSDpyGHEDCVEM-LSSGRWNDTECHLTMYFVCE 271
Cdd:smart00034  90 PGEPNN--SSGDCVVLsTSGGKWNDVSCTSKLPFVCE 124

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511837976 158 KFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVAKS--GFFRVFIGVNDLEKEGQYVFTDNTPLQnYSNWR 235
Cdd:cd03596   10 KCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASvpGNWEVWLGINDMVAEGKWVDVNGSPIS-YFNWE 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 511837976 236 EGEPSDPYG--HEDCVEMLSS--GRWNDTECHLTMYFVCEF 272
Cdd:cd03596   89 REITAQPDGgkRENCVALSSSaqGKWFDEDCRREKPYVCEF 129

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511837976 160 YYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVAKSGFFRVFIGVNDLEKEGQYVFTDNTPLQnYSNWREGEP 239
Cdd:cd03592    3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYYWIDGNDINNEGTWVDTDKKELE-YKNWAPGEP 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 511837976 240 SDpYGHEDCVEM--LSSGRWNDTECHLTMYFVCE 271
Cdd:cd03592   82 NN-GRNENCLEIyiKDNGKWNDEPCSKKKSAICY 114

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511837976 161 YIVQEEKNYRESLTHCRIRGGMLA--------MPKDEAANTLIADYvaksGFFrvfIGVNDLEK-EGQYVFTDNTPL-QN 230
Cdd:cd03601    4 LCSDETMNYAKAGAFCRSRGMRLAslamrdseMRDAILAFTLVKGH----GYW---VGADNLQDgEYDFLWNDGVSLpTD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 511837976 231 YSNWREGEPSDPYGHEDCVEMLSS-GRWNDTECHLTMYFVCE 271
Cdd:cd03601   77 SDLWAPNEPSNPQSRQLCVQLWSKyNLLDDEYCGRAKRVICE 118

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511837976 158 KFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVAKSGFFrVFIGvndLEKEGQYV-FTDNTPLQnYSNWRE 236
Cdd:cd03602    1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSA-AWIG---LYRDVDSWrWSDGSESS-FRNWNT 75

                         90       100       110
                 ....*....|....*....|....*....|....
gi 511837976 237 GEPSdpyGHEDCVEMLSSGRWNDTECHLTMYFVC 270
Cdd:cd03602   76 FQPF---GQGDCATMYSSGRWYAALCSALKPFIC 106

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511837976 160 YYIVQEEKNYRESLTHCR-IRGGMLAMPKDEAANTLIADYVAKSGFFRVFIG--VNDLEKEGQYVFTDNTPLqNYSNWRE 236
Cdd:cd03598    4 YRFVKSPRTFRDAQVICRrCYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGgiITGKGRCRRFSWVDGSVW-NYAYWAP 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 511837976 237 GEPSDPYGHedCVEMLSS-GRWNDTECHLTMYFVCEF 272
Cdd:cd03598   83 GQPGNRRGH--CVELCTRgGHWRRAHCKLRRPFICSY 117

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 511837976 156 EEKFYYIVQEEKNYRESLTHCRIRGGMLAMPKDEAANTLIADYVAKSGFfrvFIGVNDLEKEGQYVFTDNTPlqnYSNWR 235
Cdd:cd03593    9 GNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY---WIGLSREKSEKPWKWIDGSP---LNNLF 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 511837976 236 EGEPSDPYGHedCVeMLSSGRWNDTECHLTMYFVCE 271
Cdd:cd03593   83 NIRGSTKSGN--CA-YLSSTGIYSEDCSTKKRWICE 115

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511837976  52 DGEKGDPG---EEGKHGKVGRMGPKGIKGDLGDAGDQGNIGKTGPIGKKGDKGEKGLPGIPGGKGKAGTVCDCG 122
Cdd:NF038329 116 DGEKGEPGpagPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 511837976   45 APGPKGDDGEKGDPGEEGKHGKVGRMGPKGIKGDLGDAG 83
Cdd:pfam01391  17 PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511837976   53 GEKGDPGEEGKHGKVGRMGPKGIKGDLGDAGDQGNIGKTGPigkkgdkgekglPGIPGGKGKAG 116
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGP------------PGPPGPPGAPG 52

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 511837976   45 APGPKGDDGEKGDPGEEGKHGKVGRMGPKGIKGDLGDAGDQG 86
Cdd:pfam01391  14 PPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55