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 80475752  42 WTYNYSTKAYSWNNSRVFCRRHFTDLVAIQNKNEIAHLNDVIPFFN-SYYWIGIRKINNKWTWVGTNKTLtEEAENWADN 120
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNlGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 80475752 121 EPNNKKnNQDCVEIYIKSNsapGKWNDEPCFKRKRALCYT 160
Cdd:cd03592  80 EPNNGR-NENCLEIYIKDN---GKWNDEPCSKKKSAICYT 115

secreted complement-binding protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  462 VQPLGNSTYK--STCQFMCDEGFYLS--GPERLDCSPSGhWTgTPPTCEAIKCPGIFAPEQGNLDCshvhGEFGVGSICH 537
Cdd:PHA02927  36 VETDANANYNigDTIEYLCLPGYRKQkmGPIYAKCTGTG-WT-LFNQCIKRRCPSPRDIDNGQLDI----GGVDFGSSIT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  538 FSCNEDFELLGSENVEC----TVSGRWSAPPPTCKgitslpapAVRCPALTTPGQGTMSCQHHLGSFGPNTTcyFGCKTG 613
Cdd:PHA02927 110 YSCNSGYQLIGESKSYCelgsTGSMVWNPEAPICE--------SVKCQSPPSISNGRHNGYEDFYTDGSVVT--YSCNSG 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  614 FTLRGANSLRCrASGQWTAvTPMCRAVKCSelHMDTAVAMNCSNPWGNFSYGSTCTFQCPEGQSLNGSVRATCREDGHWS 693
Cdd:PHA02927 180 YSLIGNSGVLC-SGGEWSD-PPTCQIVKCP--HPTISNGYLSSGFKRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQ 255

                 ....*.
gi 80475752  694 DAMPTC 699
Cdd:PHA02927 256 PELPKC 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 80475752 168 CSNQGECIETIGSYTCSCYPGFYGPECE 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 80475752  42 WTYNYSTKAYSWNNSRVFCRRHFTDLVAIQNKNEIAHLNDVIPFFN-SYYWIGIRKINNKWTWVGTNKTLtEEAENWADN 120
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNlGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 80475752 121 EPNNKKnNQDCVEIYIKSNsapGKWNDEPCFKRKRALCYT 160
Cdd:cd03592  80 EPNNGR-NENCLEIYIKDN---GKWNDEPCSKKKSAICYT 115

secreted complement-binding protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  289 KFECQPGYRAR--GSNTLHCTGSGqWSEpLPTCEAIACEPPEIPIHGSMDcvpsTGTFGYNSSCTFLCAEGFVLKGNDAI 366
Cdd:PHA02927  51 EYLCLPGYRKQkmGPIYAKCTGTG-WTL-FNQCIKRRCPSPRDIDNGQLD----IGGVDFGSSITYSCNSGYQLIGESKS 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  367 QC----ADSGQWTAPAPFCEALQCPEFPVPSKAQVNCSDPFgtLTYQSVCSFSCDEGSLLVGASVIRClATGHWNGaPPE 442
Cdd:PHA02927 125 YCelgsTGSMVWNPEAPICESVKCQSPPSISNGRHNGYEDF--YTDGSVVTYSCNSGYSLIGNSGVLC-SGGEWSD-PPT 200

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 80475752  443 CQAVSCaPMLSPENGSMTCVQPLGNStYKSTCQFMCDEGFYLSGPERLDCSPSGHWTGTPPTC 505
Cdd:PHA02927 201 CQIVKC-PHPTISNGYLSSGFKRSYS-YNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 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 80475752 324 CEPPEIPIHGSMDCvpSTGTFGYNSSCTFLCAEGFVLKGNDAIQCADSGQWTAPAPFCE 382
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 80475752 200 CGKVNIPQHVLMNCShpLGEFSFNSQCTFSCAEGYELDGPGELQCLASGIWTNNPPKC 257
Cdd:cd00033   1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 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 80475752    262 CQSLEAPPHGTMACMHPIaaFAYDSSCKFECQPGYRARGSNTLHCTGSGQWSEPLPTC 319
Cdd:smart00032   1 CPPPPDIENGTVTSSSGT--YSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 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
                   ....*....|....*....|....*....|....*....|
gi 80475752    660 GNFSYGSTCTFQCPEGQSLNGSVRATCREDGHWSDAMPTC 699
Cdd:smart00032  17 GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56

Sushi repeat (SCR repeat);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 80475752   200 CGKVNIPQHvlMNCSHPLGEFSFNSQCTFSCAEGYELDGPGELQCLASGIWTNNPPKC 257
Cdd:pfam00084   1 CPPPPDIPN--GKVSATKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 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 80475752 168 CSNQGECIETIGSYTCSCYPGFYGPECE 195
Cdd:cd00054  11 CQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                           10        20
                   ....*....|....*....|....*....
gi 80475752    168 CSNQGECIETIGSYTCSCYPGFY-GPECE 195
Cdd:smart00179  11 CQNGGTCVNTVGSYRCECPPGYTdGRNCE 39

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 80475752  42 WTYNYSTKAYSWNNSRVFCRRHFTDLVAIQNKNEIAHLNDVIPFFN-SYYWIGIRKINNKWTWVGTNKTLtEEAENWADN 120
Cdd:cd03592   1 WTYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNlGYYWIDGNDINNEGTWVDTDKKE-LEYKNWAPG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 80475752 121 EPNNKKnNQDCVEIYIKSNsapGKWNDEPCFKRKRALCYT 160
Cdd:cd03592  80 EPNNGR-NENCLEIYIKDN---GKWNDEPCSKKKSAICYT 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 80475752  42 WTYNYSTKAYSWNNSRVFCRRHFTDLVAIQNKNEIAHLNDVIPFF-NSYYWIGIRKINNKWTWVGTNKTLTEEAENWADN 120
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSsSSDVWIGLNDLSSEGTWKWSDGSPLVDYTNWAPG 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 80475752 121 EPNNkKNNQDCVEIYIKSNsapGKWNDEPCFKRKRALCY 159
Cdd:cd00037  81 EPNP-GGSEDCVVLSSSSD---GKWNDVSCSSKLPFICE 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 80475752  44 YNYSTKAYSWNNSRVFCRRHFTDLVAIQNKNEIAHLNDVIPfFNSYYWIGIRKIN--NKWTWV-GTnkTLTEEAENWADN 120
Cdd:cd03590  13 YFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILS-GNRSYWIGLSDEEteGEWKWVdGT--PLNSSKTFWHPG 89

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 80475752 121 EPNN-KKNNQDCVEIyiksNSAPGKWNDEPCFKRKRALC 158
Cdd:cd03590  90 EPNNwGGGGEDCAEL----VYDSGGWNDVPCNLEYRWIC 124

secreted complement-binding protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  217 LGEFSFNSQCTFSCAEGYELDGPGELQC----LASGIWTNNPPKCDAVQCQSleaPPHGTMACMHPIAAFAYDSSC-KFE 291
Cdd:PHA02927  99 IGGVDFGSSITYSCNSGYQLIGESKSYCelgsTGSMVWNPEAPICESVKCQS---PPSISNGRHNGYEDFYTDGSVvTYS 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  292 CQPGYRARGSNTLHCTGsGQWSEPlPTCEAIACEPPEIpIHGSMdcvpSTG---TFGYNSSCTFLCAEGFVLKGNDAIQC 368
Cdd:PHA02927 176 CNSGYSLIGNSGVLCSG-GEWSDP-PTCQIVKCPHPTI-SNGYL----SSGfkrSYSYNDNVDFKCKYGYKLSGSSSSTC 248

                        170
                 ....*....|...
gi 80475752  369 ADSGQWTAPAPFC 381
Cdd:PHA02927 249 SPGNTWQPELPKC 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 80475752 324 CEPPEIPIHGSMDCvpSTGTFGYNSSCTFLCAEGFVLKGNDAIQCADSGQWTAPAPFCE 382
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 80475752 448 CAPMLSPENGSMTCVQplGNSTYKSTCQFMCDEGFYLSGPERLDCSPSGHWTGTPPTCE 506
Cdd:cd00033   1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 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 80475752 200 CGKVNIPQHVLMNCShpLGEFSFNSQCTFSCAEGYELDGPGELQCLASGIWTNNPPKC 257
Cdd:cd00033   1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 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 80475752 386 CPEFPVPSKAQVNCSdpFGTLTYQSVCSFSCDEGSLLVGASVIRCLATGHWNGAPPECQ 444
Cdd:cd00033   1 CPPPPVPENGTVTGS--KGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

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 80475752    262 CQSLEAPPHGTMACMHPIaaFAYDSSCKFECQPGYRARGSNTLHCTGSGQWSEPLPTC 319
Cdd:smart00032   1 CPPPPDIENGTVTSSSGT--YSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 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 80475752 642 CSELHMDTAVAMNCSNpwGNFSYGSTCTFQCPEGQSLNGSVRATCREDGHWSDAMPTCQ 700
Cdd:cd00033   1 CPPPPVPENGTVTGSK--GSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

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 80475752    324 CEPPEIPIHGSMdcVPSTGTFGYNSSCTFLCAEGFVLKGNDAIQCADSGQWTAPAPFC 381
Cdd:smart00032   1 CPPPPDIENGTV--TSSSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 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 80475752 580 CPALTTPGQGTMSCqhHLGSFGPNTTCYFGCKTGFTLRGANSLRCRASGQWTAVTPMCR 638
Cdd:cd00033   1 CPPPPVPENGTVTG--SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

Sushi repeat (SCR repeat);

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 80475752   262 CQSLEAPPHGTMACMHPIaaFAYDSSCKFECQPGYRARGSNTLHCTGSGQWSEPLPTC 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 80475752    386 CPEFPVPSKAQVNCSDpfGTLTYQSVCSFSCDEGSLLVGASVIRCLATGHWNGAPPEC 443
Cdd:smart00032   1 CPPPPDIENGTVTSSS--GTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56

EEV Host range protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  296 YRARGSNTLHCTGSGQWSEPLPTCEAIACEPPEIPiHGSMDCVPSTGTFGYNSSCTFLCAEGFVLKGNDAIQCADSGQWT 375
Cdd:PHA02817  61 YTLVGEKNIICEKDGKWNKEFPVCKIIRCRFPALQ-NGFVNGIPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWI 139

                 ....*.
gi 80475752  376 APAPFC 381
Cdd:PHA02817 140 PKVPIC 145

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  44 YNYSTKAYSWNNSRVFCRRHFTDLVAIQNKNEIAHLNDVipfFNSYYWIGI--RKINNKWTWVGTNKTLTEeaeNWADNE 121
Cdd:cd03588  13 YRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNN---AQDYQWIGLndRTIEGDFRWSDGHPLQFE---NWRPNQ 86

                        90       100       110
                ....*....|....*....|....*....|
gi 80475752 122 PNNK-KNNQDCVeIYIKSNSapGKWNDEPC 150
Cdd:cd03588  87 PDNFfATGEDCV-VMIWHEE--GEWNDVPC 113

EEV host range protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  475 QFMCDEGFYLSGPERLDCSPSGH---WTGTPPTCEAIKCPGifAPEQGNLDCSHVHGEFGVGSICHFSCNE----DFELL 547
Cdd:PHA02639  47 EYTCNTDYALIGDRFRTCIKDKNnaiWSNKAPFCMLKECND--PPSIINGKIYNKREMYKVGDEIYYVCNEhkgvQYSLV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  548 GSENVECTVSGRWSAPPPTCKGITslpapaVRCPALTtpgQGTMSCQHHLGSFGPNTTCYFGCKTGFTLRGANSLRCRAS 627
Cdd:PHA02639 125 GNEKITCIQDKSWKPDPPICKMIN------CRFPALQ---NGYINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNIN 195

                        170
                 ....*....|
gi 80475752  628 GQWTAVTPMC 637
Cdd:PHA02639 196 ATWFPSIPTC 205

EEV host range protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  228 FSCAEGYELDGPGELQCLA---SGIWTNNPPKCDAVQCQSLEAPPHGTMAC---MHPIAAFAYdSSCKFECQPGYRARGS 301
Cdd:PHA02639  48 YTCNTDYALIGDRFRTCIKdknNAIWSNKAPFCMLKECNDPPSIINGKIYNkreMYKVGDEIY-YVCNEHKGVQYSLVGN 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  302 NTLHCTGSGQWSEPLPTCEAIACEPPEIPiHGSMDCVPSTGTFGYNSSCTFLCAEGFVLKGNDAIQCADSGQWTAPAPFC 381
Cdd:PHA02639 127 EKITCIQDKSWKPDPPICKMINCRFPALQ-NGYINGIPSNKKFYYKTRVGFSCKSGFDLVGEKYSTCNINATWFPSIPTC 205

EEV host range protein; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 80475752  352 FLCAEGFVLKGNDAIQC---ADSGQWTAPAPFCEALQCPEFPVPSKAQV-NCSDPF--GTLTYQsVCSFSCDEGSLLVGA 425
Cdd:PHA02639  48 YTCNTDYALIGDRFRTCikdKNNAIWSNKAPFCMLKECNDPPSIINGKIyNKREMYkvGDEIYY-VCNEHKGVQYSLVGN 126