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 2462512398  42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLN-KVLPYYSSYYWIGIRKNNKTWTWVGTKKALtNEAENWADN 120
Cdd:cd03592     1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNgFALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462512398 121 EPNNKRnNEDCVEIYIKspsAPGKWNDEHCLKKKHALCYT 160
Cdd:cd03592    80 EPNNGR-NENCLEIYIK---DNGKWNDEPCSKKKSAICYT 115

secreted complement-binding protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512398 299 VGPEVVQCTASGvWTAPAPvCKAISCEPLESPVHGSMDcspsLRAFQYDTNCSFRCAEGFMLRGADIVRCDnLGQ----- 373
Cdd:PHA02927   63 MGPIYAKCTGTG-WTLFNQ-CIKRRCPSPRDIDNGQLD----IGGVDFGSSITYSCNSGYQLIGESKSYCE-LGStgsmv 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512398 374 WTAPAPVCQALQCQDLPVPNEARVNCSHPFgaFRYQSVCSFTCNEGLLLVGASVLQClATGNWnSVPPECQAIPCtPLLS 453
Cdd:PHA02927  136 WNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSCNSGYSLIGNSGVLC-SGGEW-SDPPTCQIVKC-PHPT 210

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462512398 454 PQNGTMTCVQPLgSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMC 505
Cdd:PHA02927  211 ISNGYLSSGFKR-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 2462512398 200 CGELELPQHVLMNCShpLGNFSFNSQCSFHCTDGYQVNGPSKLECLASGIWTNKPPQC 257
Cdd:cd00033     1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 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 2462512398  42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLN-KVLPYYSSYYWIGIRKNNKTWTWVGTKKALtNEAENWADN 120
Cdd:cd03592     1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNgFALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462512398 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 2462512398   42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYY--SSYYWIGIR--KNNKTWTWVGTKKALTNeaENW 117
Cdd:smart00034  11 KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSgsSDYYWIGLSdpDSNGSWQWSDGSGPVSY--SNW 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2462512398  118 ADNEPNNkrNNEDCVEIYIKSpsapGKWNDEHCLKKKHALC 158
Cdd:smart00034  89 APGEPNN--SSGDCVVLSTSG----GKWNDVSCTSKLPFVC 123

secreted complement-binding protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512398 299 VGPEVVQCTASGvWTAPAPvCKAISCEPLESPVHGSMDcspsLRAFQYDTNCSFRCAEGFMLRGADIVRCDnLGQ----- 373
Cdd:PHA02927   63 MGPIYAKCTGTG-WTLFNQ-CIKRRCPSPRDIDNGQLD----IGGVDFGSSITYSCNSGYQLIGESKSYCE-LGStgsmv 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512398 374 WTAPAPVCQALQCQDLPVPNEARVNCSHPFgaFRYQSVCSFTCNEGLLLVGASVLQClATGNWnSVPPECQAIPCtPLLS 453
Cdd:PHA02927  136 WNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSCNSGYSLIGNSGVLC-SGGEW-SDPPTCQIVKC-PHPT 210

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462512398 454 PQNGTMTCVQPLgSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMC 505
Cdd:PHA02927  211 ISNGYLSSGFKR-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 2462512398 262 CPPLKIPERGNMTClhSAKAFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVCK 320
Cdd:cd00033     1 CPPPPVPENGTVTG--SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 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 2462512398 200 CGELELPQHVLMNCShpLGNFSFNSQCSFHCTDGYQVNGPSKLECLASGIWTNKPPQC 257
Cdd:cd00033     1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56

Sushi repeat (SCR repeat);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512398 510 CPELFAPEQGSLDCsdTRGEFNVGSTCHFSCNNGFKLEGPNNVECTTSGRWSATPPTC 567
Cdd:pfam00084   1 CPPPPDIPNGKVSA--TKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56

Sushi repeat (SCR repeat);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512398 262 CPPLKIPERGNMTCLHSAkaFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVC 319
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNE--YNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56

Sushi repeat (SCR repeat);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512398 200 CGELELPQHvlMNCSHPLGNFSFNSQCSFHCTDGYQVNGPSKLECLASGIWTNKPPQC 257
Cdd:pfam00084   1 CPPPPDIPN--GKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56

Sushi repeat (SCR repeat);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512398 386 CQDLPVPNEARVncSHPFGAFRYQSVCSFTCNEGLLLVGASVLQCLATGNWNSVPPEC 443
Cdd:pfam00084   1 CPPPPDIPNGKV--SATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56

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 2462512398 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 2462512398  42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLN-KVLPYYSSYYWIGIRKNNKTWTWVGTKKALtNEAENWADN 120
Cdd:cd03592     1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNgFALKYNLGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462512398 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 2462512398  42 WTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYL-NKVLPYYSSYYWIGIRKN--NKTWTWVGTKKALTNeaENWA 118
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLaSLLKKSSSSDVWIGLNDLssEGTWKWSDGSPLVDY--TNWA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462512398 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 2462512398  44 YHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPyYSSYYWIGIRKNNK--TWTWV-GTKkaLTNEAENWADN 120
Cdd:cd03590    13 YFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILS-GNRSYWIGLSDEETegEWKWVdGTP--LNSSKTFWHPG 89

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462512398 121 EPNNKR-NNEDCVEIYikspSAPGKWNDEHCLKKKHALC 158
Cdd:cd03590    90 EPNNWGgGGEDCAELV----YDSGGWNDVPCNLEYRWIC 124

secreted complement-binding protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512398 299 VGPEVVQCTASGvWTAPAPvCKAISCEPLESPVHGSMDcspsLRAFQYDTNCSFRCAEGFMLRGADIVRCDnLGQ----- 373
Cdd:PHA02927   63 MGPIYAKCTGTG-WTLFNQ-CIKRRCPSPRDIDNGQLD----IGGVDFGSSITYSCNSGYQLIGESKSYCE-LGStgsmv 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512398 374 WTAPAPVCQALQCQDLPVPNEARVNCSHPFgaFRYQSVCSFTCNEGLLLVGASVLQClATGNWnSVPPECQAIPCtPLLS 453
Cdd:PHA02927  136 WNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSCNSGYSLIGNSGVLC-SGGEW-SDPPTCQIVKC-PHPT 210

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462512398 454 PQNGTMTCVQPLgSSSYKSTCQFICDEGYSLSGPERLDCTRSGRWTDSPPMC 505
Cdd:PHA02927  211 ISNGYLSSGFKR-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 2462512398 510 CPELFAPEQGSLDCSdtRGEFNVGSTCHFSCNNGFKLEGPNNVECTTSGRWSATPPTCK 568
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 2462512398 262 CPPLKIPERGNMTClhSAKAFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVCK 320
Cdd:cd00033     1 CPPPPVPENGTVTG--SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

EEV host range protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512398 414 FTCNEGLLLVGASVLQCLATGN---WNSVPPECQAIPCTPLLSPQNGTMTCVQPL---GSSSYkstcqFICDE----GYS 483
Cdd:PHA02639   48 YTCNTDYALIGDRFRTCIKDKNnaiWSNKAPFCMLKECNDPPSIINGKIYNKREMykvGDEIY-----YVCNEhkgvQYS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512398 484 LSGPERLDCTRSGRWTDSPPMCEAIKCpELFAPEQGSLDCSDTRGEFNVGSTCHFSCNNGFKLEGPNNVECTTSGRWSAT 563
Cdd:PHA02639  123 LVGNEKITCIQDKSWKPDPPICKMINC-RFPALQNGYINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPS 201

                  ....
gi 2462512398 564 PPTC 567
Cdd:PHA02639  202 IPTC 205

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 2462512398  510 CPELFAPEQGSLDCSdtRGEFNVGSTCHFSCNNGFKLEGPNNVECTTSGRWSATPPTC 567
Cdd:smart00032   1 CPPPPDIENGTVTSS--SGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 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 2462512398 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 2462512398  44 YHYSTKA-YSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGI--RKNNKTWTWVgTKKALTneAENWADN 120
Cdd:cd03591     3 IFVTNGEeKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGItdLETEGQFVYL-DGGPLT--YTNWKPG 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462512398 121 EPNNKRNNEDCVEIYikspsAPGKWNDEHCLKKKHALC 158
Cdd:cd03591    80 EPNNAGGGEDCVEMY-----TSGKWNDVACNLTRLFVC 112

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 2462512398 324 CEPLESPVHGSMDCSPSLraFQYDTNCSFRCAEGFMLRGADIVRCDNLGQWTAPAPVCQ 382
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 2462512398 580 CPALTTPGQGTMYCRHhpGTFGFNTTCYFGCNAGFTLIGDSTLSCRPSGQWTAVTPACR 638
Cdd:cd00033     1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

Sushi repeat (SCR repeat);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462512398 262 CPPLKIPERGNMTCLHSAkaFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVC 319
Cdd:pfam00084   1 CPPPPDIPNGKVSATKNE--YNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 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 2462512398  200 CGELELPQHVLMNCSHplGNFSFNSQCSFHCTDGYQVNGPSKLECLASGIWTNKPPQC 257
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56

EEV host range protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512398 475 QFICDEGYSLSGPERLDCTR---SGRWTDSPPMCEAIKCPELFAPEQGSLdcSDTRGEFNVGSTCHFSCNN----GFKLE 547
Cdd:PHA02639   47 EYTCNTDYALIGDRFRTCIKdknNAIWSNKAPFCMLKECNDPPSIINGKI--YNKREMYKVGDEIYYVCNEhkgvQYSLV 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512398 548 GPNNVECTTSGRWSATPPTCKGIaslptpGVQCPALTtpgQGTMYCRHHPGTFGFNTTCYFGCNAGFTLIGDSTLSCRPS 627
Cdd:PHA02639  125 GNEKITCIQDKSWKPDPPICKMI------NCRFPALQ---NGYINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNIN 195

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2462512398 628 GQWTAVTPAC-RAVKCSELHVNKPIAMNCSNL 658
Cdd:PHA02639  196 ATWFPSIPTCvRNKPIDDIIYLKPVDDNFDDL 227

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 2462512398  324 CEPLESPVHGSMDCSPSLraFQYDTNCSFRCAEGFMLRGADIVRCDNLGQWTAPAPVC 381
Cdd:smart00032   1 CPPPPDIENGTVTSSSGT--YSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56

EEV Host range protein; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462512398 286 SSCSFSCEEG-----FALVGPEVVQCTASGVWTAPAPVCKAISCEpLESPVHGSMDCSPSLRAFQYDTNCSFRCAEGFML 360
Cdd:PHA02817   46 SNVTFFCGNNtrgvrYTLVGEKNIICEKDGKWNKEFPVCKIIRCR-FPALQNGFVNGIPDSKKFYYESEVSFSCKPGFVL 124

                          90       100
                  ....*....|....*....|.
gi 2462512398 361 RGADIVRCDNLGQWTAPAPVC 381
Cdd:PHA02817  125 IGTKYSVCGINSSWIPKVPIC 145