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 530365278  42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLN-KVLPYYSSYYWIGIRKNNKTWTWVGTKKALtNEAENWADN 120
Cdd:cd03592    1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNgFALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 530365278 121 EPNNKRnNEDCVEIYIKspsAPGKWNDEHCLKKKHALCYT 160
Cdd:cd03592   80 EPNNGR-NENCLEIYIK---DNGKWNDEPCSKKKSAICYT 115

secreted complement-binding protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365278 342 TAFAYGSSCKFECQPGYRVRGLDML--RCIDSGhWSApLPTCEAISCEPLESPVHGSMDcspsLRAFQYDTNCSFRCAEG 419
Cdd:PHA02927  42 ANYNIGDTIEYLCLPGYRKQKMGPIyaKCTGTG-WTL-FNQCIKRRCPSPRDIDNGQLD----IGGVDFGSSITYSCNSG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365278 420 FMLRGADIVRCDnLGQ-----WTAPAPVCQALQCQDLPVPNEARVNCSHPFgaFRYQSVCSFTCNEGLLLVGASVLQClA 494
Cdd:PHA02927 116 YQLIGESKSYCE-LGStgsmvWNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSCNSGYSLIGNSGVLC-S 191

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530365278 495 TGNWnSVPPECQAIPCtPLLSPQNGTMTCVQPLgSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMC 567
Cdd:PHA02927 192 GGEW-SDPPTCQIVKC-PHPTISNGYLSSGFKR-SYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.

                         10        20
                 ....*....|....*....|....*...
gi 530365278 168 CSKQGECLETIGNYTCSCYPGFYGPECE 195
Cdd:cd00054   11 CQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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 530365278  42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLN-KVLPYYSSYYWIGIRKNNKTWTWVGTKKALtNEAENWADN 120
Cdd:cd03592    1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNgFALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 530365278 121 EPNNKRnNEDCVEIYIKspsAPGKWNDEHCLKKKHALCYT 160
Cdd:cd03592   80 EPNNGR-NENCLEIYIK---DNGKWNDEPCSKKKSAICYT 115

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 530365278    42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYY--SSYYWIGIR--KNNKTWTWVGTKKALTNeaENW 117
Cdd:smart00034  11 KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSgsSDYYWIGLSdpDSNGSWQWSDGSGPVSY--SNW 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 530365278   118 ADNEPNNkrNNEDCVEIYIKSpsapGKWNDEHCLKKKHALC 158
Cdd:smart00034  89 APGEPNN--SSGDCVVLSTSG----GKWNDVSCTSKLPFVC 123

secreted complement-binding protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365278 342 TAFAYGSSCKFECQPGYRVRGLDML--RCIDSGhWSApLPTCEAISCEPLESPVHGSMDcspsLRAFQYDTNCSFRCAEG 419
Cdd:PHA02927  42 ANYNIGDTIEYLCLPGYRKQKMGPIyaKCTGTG-WTL-FNQCIKRRCPSPRDIDNGQLD----IGGVDFGSSITYSCNSG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365278 420 FMLRGADIVRCDnLGQ-----WTAPAPVCQALQCQDLPVPNEARVNCSHPFgaFRYQSVCSFTCNEGLLLVGASVLQClA 494
Cdd:PHA02927 116 YQLIGESKSYCE-LGStgsmvWNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSCNSGYSLIGNSGVLC-S 191

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530365278 495 TGNWnSVPPECQAIPCtPLLSPQNGTMTCVQPLgSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMC 567
Cdd:PHA02927 192 GGEW-SDPPTCQIVKC-PHPTISNGYLSSGFKR-SYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530365278 572 CPELFAPEQGSLDCSdtRGEFNVGSTCHFSCDNGFKLEGPNNVECTTSGRWSATPPTCK 630
Cdd:cd00033    1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530365278 510 CTPLLSPQNGTMTCVQplGSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMCE 568
Cdd:cd00033    1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

Sushi repeat (SCR repeat);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530365278  572 CPELFAPEQGSLDCsdTRGEFNVGSTCHFSCDNGFKLEGPNNVECTTSGRWSATPPTC 629
Cdd:pfam00084   1 CPPPPDIPNGKVSA--TKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 530365278   510 CTPLLSPQNGTMTCVQplGSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMC 567
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56

Sushi repeat (SCR repeat);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530365278  448 CQDLPVPNEARVncSHPFGAFRYQSVCSFTCNEGLLLVGASVLQCLATGNWNSVPPEC 505
Cdd:pfam00084   1 CPPPPDIPNGKV--SATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56

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 530365278  42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLN-KVLPYYSSYYWIGIRKNNKTWTWVGTKKALtNEAENWADN 120
Cdd:cd03592    1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNgFALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 530365278 121 EPNNKRnNEDCVEIYIKspsAPGKWNDEHCLKKKHALCYT 160
Cdd:cd03592   80 EPNNGR-NENCLEIYIK---DNGKWNDEPCSKKKSAICYT 115

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 530365278  42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYL-NKVLPYYSSYYWIGIRKN--NKTWTWVGTKKALTNeaENWA 118
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLaSLLKKSSSSDVWIGLNDLssEGTWKWSDGSPLVDY--TNWA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530365278 119 DNEPNNKrNNEDCVEIYIkspSAPGKWNDEHCLKKKHALCY 159
Cdd:cd00037   79 PGEPNPG-GSEDCVVLSS---SSDGKWNDVSCSSKLPFICE 115

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 530365278  44 YHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPyYSSYYWIGIRKNNK--TWTWV-GTKkaLTNEAENWADN 120
Cdd:cd03590   13 YFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILS-GNRSYWIGLSDEETegEWKWVdGTP--LNSSKTFWHPG 89

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 530365278 121 EPNNKR-NNEDCVEIYikspSAPGKWNDEHCLKKKHALC 158
Cdd:cd03590   90 EPNNWGgGGEDCAELV----YDSGGWNDVPCNLEYRWIC 124

secreted complement-binding protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365278 342 TAFAYGSSCKFECQPGYRVRGLDML--RCIDSGhWSApLPTCEAISCEPLESPVHGSMDcspsLRAFQYDTNCSFRCAEG 419
Cdd:PHA02927  42 ANYNIGDTIEYLCLPGYRKQKMGPIyaKCTGTG-WTL-FNQCIKRRCPSPRDIDNGQLD----IGGVDFGSSITYSCNSG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365278 420 FMLRGADIVRCDnLGQ-----WTAPAPVCQALQCQDLPVPNEARVNCSHPFgaFRYQSVCSFTCNEGLLLVGASVLQClA 494
Cdd:PHA02927 116 YQLIGESKSYCE-LGStgsmvWNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSCNSGYSLIGNSGVLC-S 191

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530365278 495 TGNWnSVPPECQAIPCtPLLSPQNGTMTCVQPLgSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMC 567
Cdd:PHA02927 192 GGEW-SDPPTCQIVKC-PHPTISNGYLSSGFKR-SYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261

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 530365278  43 TYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGIRKNNKTWTWVGtkkALTNEAENWAdneP 122
Cdd:cd03602    2 TFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDSWRWSD---GSESSFRNWN---T 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 530365278 123 NNKRNNEDCVEIYIKspsapGKWNDEHCLKKKHALCY 159
Cdd:cd03602   76 FQPFGQGDCATMYSS-----GRWYAALCSALKPFICY 107

secreted complement-binding protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365278 217 LGNFSFNSQCSFHCTDGYQVNGPSKLEC----LASGIWTNKPPQCLAAQCPplKIPERGNMTCLHSAKAFQHQSSCSFSC 292
Cdd:PHA02927  99 IGGVDFGSSITYSCNSGYQLIGESKSYCelgsTGSMVWNPEAPICESVKCQ--SPPSISNGRHNGYEDFYTDGSVVTYSC 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530365278 293 EEGFALVGPEVVQCTAsGVWTAPaPVCKAVQCQHlEAPSEGTMDCVHPlTAFAYGSSCKFECQPGYRVRGLDMLRCIDSG 372
Cdd:PHA02927 177 NSGYSLIGNSGVLCSG-GEWSDP-PTCQIVKCPH-PTISNGYLSSGFK-RSYSYNDNVDFKCKYGYKLSGSSSSTCSPGN 252

                 ....*....
gi 530365278 373 HWSAPLPTC 381
Cdd:PHA02927 253 TWQPELPKC 261

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530365278 510 CTPLLSPQNGTMTCVQplGSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMCE 568
Cdd:cd00033    1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

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 530365278  43 TYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYsSYYWIGIRKNNKTWTWV---GTKKALTneaeNWAD 119
Cdd:cd03603    2 FYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGY-GASWIGASDAATEGTWKwsdGEESTYT----NWGS 76

                         90       100
                 ....*....|....*....|....*....
gi 530365278 120 NEP-NNKRNNEDCVEIYiKSPSAPGKWND 147
Cdd:cd03603   77 GEPhNNGGGNEDYAAIN-HFPGISGKWND 104

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530365278 200 CGELELPQHVLMNCShpLGNFSFNSQCSFHCTDGYQVNGPSKLECLASGIWTNKPPQC 257
Cdd:cd00033    1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56

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 530365278  44 YHYSTKA-YSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGI--RKNNKTWTWVgTKKALTneAENWADN 120
Cdd:cd03591    3 IFVTNGEeKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGItdLETEGQFVYL-DGGPLT--YTNWKPG 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 530365278 121 EPNNKRNNEDCVEIYikspsAPGKWNDEHCLKKKHALC 158
Cdd:cd03591   80 EPNNAGGGEDCVEMY-----TSGKWNDVACNLTRLFVC 112

Sushi repeat (SCR repeat);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530365278  572 CPELFAPEQGSLDCsdTRGEFNVGSTCHFSCDNGFKLEGPNNVECTTSGRWSATPPTC 629
Cdd:pfam00084   1 CPPPPDIPNGKVSA--TKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530365278 386 CEPLESPVHGSMDCSPSLraFQYDTNCSFRCAEGFMLRGADIVRCDNLGQWTAPAPVCQ 444
Cdd:cd00033    1 CPPPPVPENGTVTGSKGS--YSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530365278 642 CPALTTPGQGTMYCRHhpGTFGFNTTCYFGCNAGFTLIGDSTLSCRPSGQWTAVTPACR 700
Cdd:cd00033    1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

Sushi repeat (SCR repeat);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530365278  262 CPPLKIPERGNMTCLHSAkaFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVC 319
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNE--YNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530365278 704 CSELHVNKPIAMNCSNlwGNFSYGSICSFHCLEGQLLNGSAQTACQENGHWSTTVPTCQ 762
Cdd:cd00033    1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

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 530365278  58 KYCQNRYTDLVAIQNKN-EIDYL---NKVLPYYSsyYWIGI---RKNNKTWTWvGTKKALTNEAENWADNEPNNKRNNED 130
Cdd:cd03601   17 AFCRSRGMRLASLAMRDsEMRDAilaFTLVKGHG--YWVGAdnlQDGEYDFLW-NDGVSLPTDSDLWAPNEPSNPQSRQL 93

                         90       100
                 ....*....|....*....|....*...
gi 530365278 131 CVEIYIKspsaPGKWNDEHCLKKKHALC 158
Cdd:cd03601   94 CVQLWSK----YNLLDDEYCGRAKRVIC 117