NCBI Conserved Domain Search

ricin B-type lectin domain, beta-trefoil fold, found in secretory phospholipase A2 receptor (PLA2R1) and similar proteins; PLA2R1, also called PLA2-R, PLA2R, 180 kDa secretory phospholipase A2 receptor, C-type lectin domain family 13 member C (CLEC13C), or M-type receptor, is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine production during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. PLA2R1 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467788 Cd Length: 118 Bit Score: 147.97 E-value: 1.98e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190   34 KGIFIIQSENFSTCITAEMSELILENCNQVSKYMLWKWGSKQQLFNIGRSSCLGLNLSNPEPSLVMTQCDSPRYLLQWQC 113
Cdd:cd23410      1 KGMFILESESLKKCISADKSGLFLENCDQPSDSMLWKWVSRHRLFNLGSSMCLGLNLSYPQQPLGLFECDSTLRTLWWRC 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1663456190  114 HGKALIGASQFKLAVENSKfIVVKKISNYGWKQFMSHDD 152
Cdd:cd23410     81 NGKMLIGADQYKLTAVGSK-VVASRQSSHKWKPYGSQDE 118

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 112.69 E-value: 6.49e-29

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190   371 CDSNWYPYNNYCYKLHKEEKNWNEAFFSCQDDNSTLISITSLADSEMLINLL-EYENVTDIWIGLSCNKTPVEFEWSDGS 449
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLkNSGSSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 1663456190   450 -AVIFTYWNKQEPNilqKKGQICVSAQQHEGRWEIKNCKSRYFYICK 495
Cdd:smart00034   81 gPVSYSNWAPGEPN---NSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124

ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and similar proteins; Ly-75, also called C-type lectin domain family 13 member B, DEC-205, gp200-MR6, or CD205, acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. Ly-75 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467789 Cd Length: 116 Bit Score: 109.83 E-value: 4.14e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190   35 GIFIIQSENFSTCITAEMSELILENCNQVSKYMLWKWGSKQQLFNIGRSSCLGLNLSNPEPSLVMTQCDSPRYLLQWQCH 114
Cdd:cd23411      3 DIFTIQHENSGKCLKVENSQISAVDCKQSSESLQWKWVSEHRLFNLGSKQCLGLDITKPSNTLKMFECDSKSVMLWWRCE 82

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1663456190  115 GKALIGASQFKLAVENSKfIVVKKISNYGWKQ 146
Cdd:cd23411     83 GGSLYGASQYRLAVKNGS-VTASIDSNDTWKK 113

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.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 94.61 E-value: 8.22e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  381 YCYKLHKEEKNWNEAFFSCQDDNSTLISITSLADSEMLINLLEYENVTDIWIGLSCNKTPVEFEWSDGS-AVIFTYWNKQ 459
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKWSDGSpLVDYTNWAPG 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1663456190  460 EPNILQKKGqiCVS-AQQHEGRWEIKNCKSRYFYICKR 496
Cdd:cd00037     81 EPNPGGSED--CVVlSSSSDGKWNDVSCSSKLPFICEK 116

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.

Pssm-ID: 467784 [Multi-domain] Cd Length: 119 Bit Score: 86.88 E-value: 5.63e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190   36 IFIIQSENFSTCITA--EMSELILENCNQVSKYMLWKWGSKQQLFNIGRSSCLGLNLSNPEPSLVMTQCDSPRYLLQWQC 113
Cdd:cd23385      2 SFLIYNEDLGKCLAArsSSSKVSLSTCNPNSPNQQWKWTSGHRLFNVGTGKCLGVSSSSPSSPLRLFECDSEDELQKWKC 81

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1663456190  114 HGKALIGASQFKLAVENSKF---IVVKKISNYG--WK 145
Cdd:cd23385     82 SKDGLLLLKGLGLLLLYDKSgknVVVSKGSGLSsrWK 118

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 85.73 E-value: 1.40e-19

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190   511 CPEGWERHGEYCYKVDTIPRSFEHASNgyYC----PSLATITSRFEQDFLNSMIHHQGNTDspYFWIALQDLNNTGEYTW 586
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQA--FCqslgGHLASIHSEAENDFVASLLKNSGSSD--YYWIGLSDPDSNGSWQW 76

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1663456190   587 LTEDRkhhLAIYTNWGKHQPRYPGG-CVVMRQEEpiGMWEVKNCATFMaKSLCK 639
Cdd:smart00034   77 SDGSG---PVSYSNWAPGEPNNSSGdCVVLSTSG--GKWNDVSCTSKL-PFVCE 124

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 83.80 E-value: 8.33e-19

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190   956 CPKGWLYFGFKCFLVqipkdSAHLKSWHSAQKTCSYYDASLVSVENEVEQAFIA--MNLLGHKSNVWIGLQSDSYE---K 1030
Cdd:smart00034    1 CPSGWISYGGKCYKF-----STEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNgswQ 75

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1663456190  1031 WLNGQE-VEYANWSPAQVRHQNHYigdtekkdvlCTSILNNPsfslmGKWYLESCENKNGFVCQ 1093
Cdd:smart00034   76 WSDGSGpVSYSNWAPGEPNNSSGD----------CVVLSTSG-----GKWNDVSCTSKLPFVCE 124

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 83.05 E-value: 1.01e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190 1120 STYTLINGSMTWNMASQMCKKNGAELVSITDYYHQAFLTVIINRVGYAH-WIGLFTSDDGLPFEWSDGTRPF-FTFW--G 1195
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDvWIGLNDLSSEGTWKWSDGSPLVdYTNWapG 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1663456190 1196 EEETQGPGHCVYIDTN--GHWKNTDCEKLLsGAIC 1228
Cdd:cd00037     81 EPNPGGSEDCVVLSSSsdGKWNDVSCSSKL-PFIC 114

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 82.65 E-value: 1.69e-18

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190   663 CMHGWESdhYLLNCYKVFHSEKvlmkrTWEEAETLCQDFGAHLASFKQVLEKDFLNKLLNTMFHIDderQFWIGFNKRNp 742
Cdd:smart00034    1 CPSGWIS--YGGKCYKFSTEKK-----TWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD---YYWIGLSDPD- 69

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1663456190   743 lSGGSWQWSDGTPVSSA--FLEKASIEDVKNCAAYKTN-GTILPLHCNSEHEWICK 795
Cdd:smart00034   70 -SNGSWQWSDGSGPVSYsnWAPGEPNNSSGDCVVLSTSgGKWNDVSCTSKLPFVCE 124

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 81.51 E-value: 3.79e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  234 CYQINLlSVLSWNEARVACQGQGADLLSITDMREQKYIGGLIEQLNTKEamIWTGLNQLDETAGWQWSDGAPLA-LVNWL 312
Cdd:cd00037      2 CYKFST-EKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSD--VWIGLNDLSSEGTWKWSDGSPLVdYTNWA 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1663456190  313 KDPIDGSlGPAHCKAFNLKIQNDWPSYSCESRLPYVCKK 351
Cdd:cd00037     79 PGEPNPG-GSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.

Pssm-ID: 128373 Cd Length: 49 Bit Score: 78.88 E-value: 4.16e-18

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1663456190   166 GNSLGLPCVFPFKHKNKWHYECIRDFREDGYPWCATTSHYEQDEKWGLC 214
Cdd:smart00059    1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49

Fibronectin type II domain;

Pssm-ID: 459645 Cd Length: 42 Bit Score: 77.61 E-value: 1.20e-17

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1663456190  173 CVFPFKHKNKWHYECIRDFREDGYPWCATTSHYEQDEKWGLC 214
Cdd:pfam00040    1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 79.44 E-value: 1.61e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190 1128 SMTWNMASQMCKKNGAELVSITDYYHQAFLTVIINRVGYAHWIGLFTSDDGLPFEWSDGTRPFFTFWGEEET--QGPGHC 1205
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNnnGENEDC 80

                           90       100
                   ....*....|....*....|....*
gi 1663456190 1206 VYID-TNGHWKNTDCEKLLsGAICH 1229
Cdd:pfam00059   81 VELSsSSGKWNDENCNSKN-PFVCE 104

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 79.57 E-value: 2.23e-17

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  1112 PDTLEYANSTYTLINGSMTWNMASQMCKKNGAELVSITDYYHQAFLTVIINRVGYA--HWIGLFTSDDGLPFEWSDGTRP 1189
Cdd:smart00034    3 SGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSDGSGP 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 1663456190  1190 F-FTFWGE-EETQGPGHCVYIDTN-GHWKNTDCEKLLsGAIC 1228
Cdd:smart00034   83 VsYSNWAPgEPNNSSGDCVVLSTSgGKWNDVSCTSKL-PFVC 123

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.

Pssm-ID: 238019 Cd Length: 48 Bit Score: 76.58 E-value: 3.07e-17

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1663456190  167 NSLGLPCVFPFKHKNKWHYECIRDFREDGYPWCATTSHYEQDEKWGLC 214
Cdd:cd00062      1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48

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.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 78.43 E-value: 4.78e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  675 NCYKVFHSekvlmKRTWEEAETLCQDFGAHLASFKQVLEKDFLNKLLNTmfhiDDERQFWIGFNKRNplSGGSWQWSDGT 754
Cdd:cd00037      1 SCYKFSTE-----KLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKK----SSSSDVWIGLNDLS--SEGTWKWSDGS 69

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1663456190  755 PVSSAFL---EKASIEDVKNCAA--YKTNGTILPLHCNSEHEWICKI 796
Cdd:cd00037     70 PLVDYTNwapGEPNPGGSEDCVVlsSSSDGKWNDVSCSSKLPFICEK 116

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 78.12 E-value: 6.73e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  371 CDSNWYPYNNYCYKLHKEEKNWNEAFFSCQDDNSTLISITSLADSEMLINLLEYENVTdiWIGLSCNKTPVEFEWSDGSA 450
Cdd:cd03590      1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSY--WIGLSDEETEGEWKWVDGTP 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1663456190  451 VI--FTYWNKQEPNILQKKGQICVSAQQHEGRWEIKNCKSRYFYICKR 496
Cdd:cd03590     79 LNssKTFWHPGEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 76.87 E-value: 2.08e-16

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190   221 CDIFWKINadTQICYQINLlSVLSWNEARVACQGQGADLLSITDMREQKYIGGLIeQLNTKEAMIWTGLNQLDETAGWQW 300
Cdd:smart00034    1 CPSGWISY--GGKCYKFST-EKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLL-KNSGSSDYYWIGLSDPDSNGSWQW 76

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1663456190   301 SDG-APLALVNWLKDPIDGSLGpaHCKAFNLKIQNdWPSYSCESRLPYVCK 350
Cdd:smart00034   77 SDGsGPVSYSNWAPGEPNNSSG--DCVVLSTSGGK-WNDVSCTSKLPFVCE 124

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 76.10 E-value: 3.72e-16

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190   814 WFYYQGAEYLFYDSPSNWDSFQFVCGWLHGDIATIQSFQEQEFIQNrIKKISKKSSSWWIALRSELPSEEFRWTDGS-LL 892
Cdd:smart00034    5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAS-LLKNSGSSDYYWIGLSDPDSNGSWQWSDGSgPV 83

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1663456190   893 SYQNWAGDkerPKPAQGPKCAFISSQTGQWGFANCTISLPCVCK 936
Cdd:smart00034   84 SYSNWAPG---EPNNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 72.27 E-value: 5.80e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  966 KCFLVqipkdSAHLKSWHSAQKTCSYYDASLVSVENEVEQAFIAMNLLGHKSN-VWIGLQSDSYE---KWLNGQE-VEYA 1040
Cdd:cd00037      1 SCYKF-----STEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSEgtwKWSDGSPlVDYT 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1663456190 1041 NWSPAQVRHQNhyigdtekkDVLCTSILNNPSfslmGKWYLESCENKNGFVCQK 1094
Cdd:cd00037     76 NWAPGEPNPGG---------SEDCVVLSSSSD----GKWNDVSCSSKLPFICEK 116

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 71.74 E-value: 8.05e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  390 KNWNEAFFSCQDDNSTLISITSLADSEMLINLLEYENvTDIWIGLSCNKTPVEFEWSDGSAVIFTYWNKqEPNILQKKGQ 469
Cdd:pfam00059    2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSN-KYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-EPNNNGENED 79

                           90       100
                   ....*....|....*....|....*..
gi 1663456190  470 iCVSAQQHEGRWEIKNCKSRYFYICKR 496
Cdd:pfam00059   80 -CVELSSSSGKWNDENCNSKNPFVCEK 105

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 69.81 E-value: 3.43e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  688 KRTWEEAETLCQDFGAHLASFKQVLEKDFLNKLLNtmfhiDDERQFWIGFNKRNplSGGSWQWSDGTPVSSAFLEKASIE 767
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLK-----KSNKYFWIGLTDRK--NEGTWKWVDGSPVNYTNWAPEPNN 73

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1663456190  768 DVKN--CAAY-KTNGTILPLHCNSEHEWICK 795
Cdd:pfam00059   74 NGENedCVELsSSSGKWNDENCNSKNPFVCE 104

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.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 69.57 E-value: 5.41e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  521 YCYKVDTIPRSFEHASNgyYCPS----LATITSRFEQDFLNSMIHHQGNTdspYFWIALQDLNNTGEYTWLTedrKHHLA 596
Cdd:cd00037      1 SCYKFSTEKLTWEEAQE--YCRSlgghLASIHSEEENDFLASLLKKSSSS---DVWIGLNDLSSEGTWKWSD---GSPLV 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1663456190  597 IYTNWGKHQPRYPGG--CVVMRQeEPIGMWEVKNCATFMAkSLCKQ 640
Cdd:cd00037     73 DYTNWAPGEPNPGGSedCVVLSS-SSDGKWNDVSCSSKLP-FICEK 116

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 68.27 E-value: 1.02e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  243 LSWNEARVACQGQGADLLSITDMREQKYIGGLIEQLNTKeamIWTGLNQLDETAGWQWSDGAPLALVNWLKDPIDGSLGP 322
Cdd:pfam00059    2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY---FWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGENE 78

                           90       100
                   ....*....|....*....|....*....
gi 1663456190  323 aHCKAFNLKiQNDWPSYSCESRLPYVCKK 351
Cdd:pfam00059   79 -DCVELSSS-SGKWNDENCNSKNPFVCEK 105

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 69.31 E-value: 1.07e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  371 CDSNWYPYNNYCYKLHKEEKNWNEAFFSCQD-----DNSTLISITSLADSEMLINLLEYENVTD----IWIGLSCNKTPV 441
Cdd:cd03589      1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDLFESSRGPDtpygLWIGLHDRTSEG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1663456190  442 EFEWSDGSAVIFTYWNKQEPNIlQKKGQICV---SAQQHEGRWEIKNCKSRYFYICK 495
Cdd:cd03589     81 PFEWTDGSPVDFTKWAGGQPDN-YGGNEDCVqmwRRGDAGQSWNDMPCDAVFPYICK 136

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.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 68.42 E-value: 1.30e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  822 YLFYDSPSNWDSFQFVCGWLHGDIATIQSFQEQEFIQNriKKISKKSSSWWIALRSELPSEEFRWTDGS-LLSYQNWAGD 900
Cdd:cd00037      3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLAS--LLKKSSSSDVWIGLNDLSSEGTWKWSDGSpLVDYTNWAPG 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1663456190  901 keRPKPAQGPKCAFIS-SQTGQWGFANCTISLPCVCKR 937
Cdd:cd00037     81 --EPNPGGSEDCVVLSsSSDGKWNDVSCSSKLPFICEK 116

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 68.13 E-value: 1.94e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  675 NCYKVFHSEKvlmkrTWEEAETLCQDFGAHLASFKQVLEKDFLNKLLNTMFHidderqfWIGFNKRNplSGGSWQWSDGT 754
Cdd:cd03593     11 KCYYFSMEKK-----TWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY-------WIGLSREK--SEKPWKWIDGS 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1663456190  755 PVSSAFLEKASiEDVKNCAAYKtNGTILPLHCNSEHEWICK 795
Cdd:cd03593     77 PLNNLFNIRGS-TKSGNCAYLS-STGIYSEDCSTKKRWICE 115

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 68.17 E-value: 2.49e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  371 CDSNWYPYNNYCYKLHKEEKNWNEAFFSCQD--DNSTLISITSLADSEMLINLL-----EYENVtdiWIGLSCNKTPVEF 443
Cdd:cd03594      1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLIssyqkAYQPV---WIGLHDPQQSRGW 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1663456190  444 EWSDGSAVIFTYWNKQEPnilQKKGQICVSAQQHEG--RWEIKNCKSRYFYICK 495
Cdd:cd03594     78 EWSDGSKLDYRSWDRNPP---YARGGYCAELSRSTGflKWNDANCEERNPFICK 128

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 66.94 E-value: 5.66e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  956 CPKGWLYFGFKCFLVqipkdSAHLKSWHSAQKTCSYYDASLVSVENEVEQAFIaMNLLGHKSNVWIGLqSDSYE----KW 1031
Cdd:cd03590      1 CPTNWKSFQSSCYFF-----STEKKSWEESRQFCEDMGAHLVIINSQEEQEFI-SKILSGNRSYWIGL-SDEETegewKW 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1663456190 1032 LNGQ--EVEYANWSPAQvrhQNHYIGDTEKkdvlCTSILNNPsfslmGKWYLESCENKNGFVCQK 1094
Cdd:cd03590     74 VDGTplNSSKTFWHPGE---PNNWGGGGED----CAELVYDS-----GGWNDVPCNLEYRWICEK 126

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 67.01 E-value: 6.89e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  234 CYQInLLSVLSWNEARVACQ--GQGADLLSITDMREQKYIGGLIEQLNTKEAMIWTGLNQLDETAGWQWSDGAPLALVNW 311
Cdd:cd03594     12 CYGY-FRQPLSWSDAELFCQkyGPGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSRGWEWSDGSKLDYRSW 90

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1663456190  312 LKDPidGSLGPAHCKAfnLKIQND---WPSYSCESRLPYVCK 350
Cdd:cd03594     91 DRNP--PYARGGYCAE--LSRSTGflkWNDANCEERNPFICK 128

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 65.58 E-value: 1.09e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  980 KSWHSAQKTCSYYDASLVSVENEVEQAFIAMNLLGHKSNVWIGL---QSDSYEKWLNGQEVEYANWSPAqvrhqnhyiGD 1056
Cdd:pfam00059    2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLtdrKNEGTWKWVDGSPVNYTNWAPE---------PN 72

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1663456190 1057 TEKKDVLCTSILNNpsfslMGKWYLESCENKNGFVCQK 1094
Cdd:pfam00059   73 NNGENEDCVELSSS-----SGKWNDENCNSKNPFVCEK 105

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 65.43 E-value: 1.60e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  371 CDSNWYPYNNYCYKLHKEEKNWNEAFFSCQDDNSTLISITslaDSEMLINLLEYENVTDIWIGLSCNKTPVEFEWSDGSa 450
Cdd:cd03593      1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKID---DEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGS- 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1663456190  451 vIFTYWNkqEPNILQKKGQiCVSaqQHEGRWEIKNCKSRYFYICKR 496
Cdd:cd03593     77 -PLNNLF--NIRGSTKSGN-CAY--LSSTGIYSEDCSTKKRWICEK 116

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 64.75 E-value: 2.47e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190 1120 STYTLINGSMTWNMASQMCKKNGAELVSITDYYHQAFLTVIINRVGYAhWIGLFTSDDGLPFEWSDGTRPFFTFWGEEET 1199
Cdd:cd03603      1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGAS-WIGASDAATEGTWKWSDGEESTYTNWGSGEP 79


                   ....
gi 1663456190 1200 QGPG 1203
Cdd:cd03603     80 HNNG 83

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.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 63.93 E-value: 3.68e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190 1121 TYTLINGSMTWNMASQMCKKNGAELVSITDYYHQAFLTVIINRVGYAHWIGLFtsDDGLPFEWSDGTRPFFTFWGEEETQ 1200
Cdd:cd03602      2 TFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLY--RDVDSWRWSDGSESSFRNWNTFQPF 79

                           90       100
                   ....*....|....*....|....
gi 1663456190 1201 GPGHCVYIDTNGHWKNTDCEKLLS 1224
Cdd:cd03602     80 GQGDCATMYSSGRWYAALCSALKP 103

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 62.77 E-value: 1.68e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  675 NCYKVFHSEKvlmkrTWEEAETLCQDF--GAHLASFKQVLEKDFLNKLLNTmFHIDDERqFWIGFNkrNPLSGGSWQWSD 752
Cdd:cd03594     11 NCYGYFRQPL-----SWSDAELFCQKYgpGAHLASIHSPAEAAAIASLISS-YQKAYQP-VWIGLH--DPQQSRGWEWSD 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1663456190  753 GT-PVSSAFLEKASIEDVKNCAAYKTNGTILPLH---CNSEHEWICK 795
Cdd:cd03594     82 GSkLDYRSWDRNPPYARGGYCAELSRSTGFLKWNdanCEERNPFICK 128

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 59.80 E-value: 1.09e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  830 NWDSFQFVCGWLHGDIATIQSFQEQEFIQNRIKKISKKSSSwwiALRSELPSEEFRWTDGSLLSYQNWAGdkERPKPAQG 909
Cdd:pfam00059    3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWI---GLTDRKNEGTWKWVDGSPVNYTNWAP--EPNNNGEN 77

                           90       100
                   ....*....|....*....|....*...
gi 1663456190  910 PKCAFISSQTGQWGFANCTISLPCVCKR 937
Cdd:pfam00059   78 EDCVELSSSSGKWNDENCNSKNPFVCEK 105

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 60.08 E-value: 1.50e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  956 CPKGWLYFGFKCF-LVQIPkdsahlKSWHSAQKTCSYYDAS--LVSVENEVEQAFIA---MNLLGHKSNVWIGL---QSD 1026
Cdd:cd03594      1 CPKGWLPYKGNCYgYFRQP------LSWSDAELFCQKYGPGahLASIHSPAEAAAIAsliSSYQKAYQPVWIGLhdpQQS 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1663456190 1027 SYEKWLNGQEVEYANWSPAQVRHQNHYigdtekkdvlCTSILNNPSFSlmgKWYLESCENKNGFVCQ 1093
Cdd:cd03594     75 RGWEWSDGSKLDYRSWDRNPPYARGGY----------CAELSRSTGFL---KWNDANCEERNPFICK 128

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 59.65 E-value: 1.52e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  956 CPKGWLYFGFKCFLVqipkdSAHLKSWHSAQKTCSYYDASLVSVENEVEQAFIaMNLLGHkSNVWIGLQSDSYE---KWL 1032
Cdd:cd03593      1 CPKDWICYGNKCYYF-----SMEKKTWNESKEACSSKNSSLLKIDDEEELEFL-QSQIGS-SSYWIGLSREKSEkpwKWI 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1663456190 1033 NGqeveyanwSPaqVRHQNHYIGDTEKKDvlCTSILNNpsfslmgKWYLESCENKNGFVCQK 1094
Cdd:cd03593     74 DG--------SP--LNNLFNIRGSTKSGN--CAYLSST-------GIYSEDCSTKKRWICEK 116

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 60.06 E-value: 2.26e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  663 CMHGWEsdHYLLNCYKVFHSEKvlmkrTWEEAETLCQDFG-----AHLASFKQVLEKDFLNKLLNTMFHIDDERQFWIGF 737
Cdd:cd03589      1 CPTFWT--AFGGYCYRFFGDRL-----TWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFESSRGPDTPYGLWIGL 73

                           90
                   ....*....|....*....
gi 1663456190  738 NKRNplSGGSWQWSDGTPV 756
Cdd:cd03589     74 HDRT--SEGPFEWTDGSPV 90

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.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 59.13 E-value: 2.86e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  371 CDSNWYPYNNYCYKLHKEEKNWNEAFFSCQDDNSTLISITSLADSEMLINLL-EYEnvtdiWIGLSCNKTPVEFEWSDGS 449
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAqDYQ-----WIGLNDRTIEGDFRWSDGH 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1663456190  450 AVIFTYWNKQEPNILQKKGQICVSAQQHE-GRWEIKNCKSRYFYICKR 496
Cdd:cd03588     76 PLQFENWRPNQPDNFFATGEDCVVMIWHEeGEWNDVPCNYHLPFTCKK 123

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 58.08 E-value: 7.29e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  663 CMHGWEsdHYLLNCYkvFHSEKvlmKRTWEEAETLCQDFGAHLASFKQVLEKDFLNKLLNTMFHidderqFWIGFNKRNp 742
Cdd:cd03590      1 CPTNWK--SFQSSCY--FFSTE---KKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS------YWIGLSDEE- 66

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  743 lSGGSWQWSDGTPV--SSAFLEKASIEDVK----NCAAYKTN-GTILPLHCNSEHEWICK 795
Cdd:cd03590     67 -TEGEWKWVDGTPLnsSKTFWHPGEPNNWGgggeDCAELVYDsGGWNDVPCNLEYRWICE 125

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.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 55.38 E-value: 4.78e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  383 YKLHKEEKNWNEAFFSCQDDNSTLISITSLADSEMLINLLEYENvTDIWIGLSCNKTPVEFEWSDGSAVIFTYWNKQEPN 462
Cdd:cd03591      4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGN-TYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPN 82

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1663456190  463 IlQKKGQICVsAQQHEGRWEIKNCKSRYFYIC 494
Cdd:cd03591     83 N-AGGGEDCV-EMYTSGKWNDVACNLTRLFVC 112

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 2 (MRC2) and similar proteins; MRC2, also called C-type mannose receptor 2, C-type lectin domain family 13 member E (CLEC13E), endocytic receptor 180 (Endo180), urokinase-type plasminogen activator receptor-associated protein (UPARAP), UPAR-associated protein, urokinase receptor-associated protein, or CD280, may play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). MRC2 contains an atypical ricin B-type lectin domain at the N-terminus. The typical ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. In contrast, the ninth, tenth and eleventh beta strands, comprising the gamma subdomain, are missing in the ricin B-type lectin domain of MRC2.

Pssm-ID: 467786 Cd Length: 124 Bit Score: 55.57 E-value: 4.92e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190   35 GIFIIQSENFSTCITAEMSELILEN-CNQVSKYMLWKWGSKQQLFNIGRSSCLGL---NLSNPEPSLVMTQCDSPRYLLQ 110
Cdd:cd23408      1 DVFLIYSDGAQGCLEVRDSVVRLSPaCNTSSPAQQWKWVSRNRLFNLGSMQCLGVsgpNGSGTSATLGTYECDRESVNMR 80


                   ...
gi 1663456190  111 WQC 113
Cdd:cd23408     81 WHC 83

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 53.10 E-value: 3.58e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  234 CYQINLlSVLSWNEARVACQGQGADLLSITDMREQKYIgglieQLNTKEAMIWTGLNQLDETAGWQWSDGAPLAlvNWLK 313
Cdd:cd03593     12 CYYFSM-EKKTWNESKEACSSKNSSLLKIDDEEELEFL-----QSQIGSSSYWIGLSREKSEKPWKWIDGSPLN--NLFN 83

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1663456190  314 DPIDGSLGpaHCKAFNL-KIQNDwpsySCESRLPYVCKK 351
Cdd:cd03593     84 IRGSTKSG--NCAYLSStGIYSE----DCSTKKRWICEK 116

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 52.69 E-value: 6.44e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  511 CPEGWERHGEYCYKVDTIPRSFEHASNgyYCPS----LATITSRFEQDFLNSMIHHQGNtdspyFWIALQDLNNTGEYTW 586
Cdd:cd03590      1 CPTNWKSFQSSCYFFSTEKKSWEESRQ--FCEDmgahLVIINSQEEQEFISKILSGNRS-----YWIGLSDEETEGEWKW 73

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1663456190  587 LteDRKHHLAIYTNWGKHQPRYPGG----CVVMRQ 617
Cdd:cd03590     74 V--DGTPLNSSKTFWHPGEPNNWGGggedCAELVY 106

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 1 (MRC1) and similar proteins; MRC1, also called MMR, C-type lectin domain family 13 member D (CLEC13D), C-type lectin domain family 13 member D-like (CLEC13DL), macrophage mannose receptor 1-like protein 1 (MRC1L1), or CD206, mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains. MRC1 acts as phagocytic receptor for bacteria, fungi and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC1 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467785 Cd Length: 123 Bit Score: 51.98 E-value: 8.23e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190   35 GIFIIQSENFSTCITA-EMSELILENCNQVSKYMLWKWGSKQQLFNIGRSSCLGLNLSNPEPSLVMTQCDSPRYLLQWQC 113
Cdd:cd23407      1 RSFLIYNEDHNRCVQArSSSSVTTATCNPNAESQKFRWVSGSQILSVAFKLCLGVPSKKDWVTVTLFPCNEKSELQKWEC 80


                   ....*..
gi 1663456190  114 HGKALIG 120
Cdd:cd23407     81 KNDTLLA 87

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 52.31 E-value: 8.37e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  234 CYQINLLSvLSWNEARVACQGQGADLLSITDMREQKYIGGLIEqlntKEAMIWTGLNQLDETAGWQWSDGAPLAL--VNW 311
Cdd:cd03590     12 CYFFSTEK-KSWEESRQFCEDMGAHLVIINSQEEQEFISKILS----GNRSYWIGLSDEETEGEWKWVDGTPLNSskTFW 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1663456190  312 LKDPIDGSLGPA-HCKAFNlKIQNDWPSYSCESRLPYVCKK 351
Cdd:cd03590     87 HPGEPNNWGGGGeDCAELV-YDSGGWNDVPCNLEYRWICEK 126

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.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 51.61 E-value: 9.08e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  979 LKSWHSAQKTCSYYDASLVSVENEVEQAFIAMNLLGHKSNVWIGLQSDSYE-KWLNGQEVEYANWSPAQVRHQNHyigdt 1057
Cdd:cd03602      9 SKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDSwRWSDGSESSFRNWNTFQPFGQGD----- 83

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1663456190 1058 ekkdvlCTSILNNpsfslmGKWYLESCENKNGFVC 1092
Cdd:cd03602     84 ------CATMYSS------GRWYAALCSALKPFIC 106

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.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 52.19 E-value: 9.27e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  663 CMHGWesDHYLLNCYKVFHSekvlmKRTWEEAETLCQDFGAHLASFKQVLEKDFLNKLLNtmfhiddERQfWIGFNKRnp 742
Cdd:cd03588      1 CEEGW--DKFQGHCYRHFPD-----RETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQ-------DYQ-WIGLNDR-- 63

                           90
                   ....*....|....
gi 1663456190  743 LSGGSWQWSDGTPV 756
Cdd:cd03588     64 TIEGDFRWSDGHPL 77

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 52.36 E-value: 1.04e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  242 VLSWNEARVACQ-----GQGADLLSITDMREQKYIGGLIEQLNTKE--AMIWTGLNQLDETAGWQWSDGAPLALVNWLKD 314
Cdd:cd03589     19 RLTWEEAELRCRsfsipGLIAHLVSIHSQEENDFVYDLFESSRGPDtpYGLWIGLHDRTSEGPFEWTDGSPVDFTKWAGG 98

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1663456190  315 PIDGSLGPAHCKAF--NLKIQNDWPSYSCESRLPYVCK 350
Cdd:cd03589     99 QPDNYGGNEDCVQMwrRGDAGQSWNDMPCDAVFPYICK 136

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

Pssm-ID: 153068 Cd Length: 117 Bit Score: 51.68 E-value: 1.15e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  382 CYKLHKEEKNWNEAFFSCQD-DNSTLISITSLADSEMLINLLEYENVTDIWIG--LSCNKTPVEFEWSDGSAVIFTYWNK 458
Cdd:cd03598      3 CYRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWNYAYWAP 82

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1663456190  459 QEPNIlqkKGQICVSAQQHEGRWEIKNCKSRYFYIC 494
Cdd:cd03598     83 GQPGN---RRGHCVELCTRGGHWRRAHCKLRRPFIC 115

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.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 50.84 E-value: 1.63e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  383 YKLHKEEKNWNEAFFSCQDDNSTLISITSLADSEMLINLLEYENvTDIWIGLScnKTPVEFEWSDGSAVIFTYWNKQEPN 462
Cdd:cd03602      3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSN-SAAWIGLY--RDVDSWRWSDGSESSFRNWNTFQPF 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1663456190  463 IlqkkGQICVsAQQHEGRWEIKNCKSRYFYIC 494
Cdd:cd03602     80 G----QGDCA-TMYSSGRWYAALCSALKPFIC 106

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 51.22 E-value: 1.77e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  511 CPEGWERHGEYCYKVDTIPRSFEHASngYYCPS------LATITSRFEQDFLNSMIHHQGNTDSPyFWIALQDLNNTGEY 584
Cdd:cd03594      1 CPKGWLPYKGNCYGYFRQPLSWSDAE--LFCQKygpgahLASIHSPAEAAAIASLISSYQKAYQP-VWIGLHDPQQSRGW 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1663456190  585 TWLTEDRKHhlaiYTNWGKHQP-RYPGGCVVMRQEEPIGMWEVKNC 629
Cdd:cd03594     78 EWSDGSKLD----YRSWDRNPPyARGGYCAELSRSTGFLKWNDANC 119

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.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 50.89 E-value: 1.87e-07

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1663456190  544 LATITSRFEQDFLNSMIHHQGNtdspyFWIALQDLNNTGEYTWLTEDRKHhlaiYTNWGKHQPRYPGG 611
Cdd:cd03603     26 LVTINSAEENDWLLSNFGGYGA-----SWIGASDAATEGTWKWSDGEEST----YTNWGSGEPHNNGG 84

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 49.78 E-value: 3.21e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  529 PRSFEHASNgyYCPS----LATITSRFEQDFLNSMIHHQGNtdspYFWIALQDLNNTGEYTWLTEDRKHhlaiYTNWGKH 604
Cdd:pfam00059    1 SKTWDEARE--ACRKlgghLVSINSAEELDFLSSTLKKSNK----YFWIGLTDRKNEGTWKWVDGSPVN----YTNWAPE 70

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1663456190  605 QPRYPGG--CVVMRQeePIGMWEVKNCaTFMAKSLCKQ 640
Cdd:pfam00059   71 PNNNGENedCVELSS--SSGKWNDENC-NSKNPFVCEK 105

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.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 50.06 E-value: 3.44e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  243 LSWNEARVACQGQGADLLSITDMREQKYIGGLIEQLNTKeamIWTGLnqLDETAGWQWSDGAPLALVNWLKDPIDGSLgp 322
Cdd:cd03602     10 KTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSA---AWIGL--YRDVDSWRWSDGSESSFRNWNTFQPFGQG-- 82

                           90       100
                   ....*....|....*....|....*..
gi 1663456190  323 aHCKAfnLKIQNDWPSYSCESRLPYVC 349
Cdd:cd03602     83 -DCAT--MYSSGRWYAALCSALKPFIC 106

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 51.04 E-value: 3.79e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  234 CYQI----NLLSVLSWNEARVACQGQGADLLSITDMREQKYIGGLIEQLNTKEAMIWTGL--------NQLDETAGWQWS 301
Cdd:cd03595     12 CYKIayfqDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGDFWIGLrrssqynvTSSACSSLYYWL 91

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1663456190  302 DGAPLALVNWLKDpiDGSLGPAHCKAFNLKIQND----------WPSYSCESRLPYVCK 350
Cdd:cd03595     92 DGSISTFRNWYVD--EPSCGSEVCVVMYHQPSAPagqggpylfqWNDDNCNMKNNFICK 148

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 50.00 E-value: 5.25e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190 1126 NGSMTWNMASQMCKKNGAELVSITDYYHQAFLTVIINRvGYAHWIGLFTSDDGLPFEWSDGT--RPFFTFWGEEETQGPG 1203
Cdd:cd03590     17 TEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSG-NRSYWIGLSDEETEGEWKWVDGTplNSSKTFWHPGEPNNWG 95

                           90
                   ....*....|..
gi 1663456190 1204 H----CVYIDTN 1211
Cdd:cd03590     96 GggedCAELVYD 107

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.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 47.76 E-value: 2.20e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  383 YKLHKEEKNWNEAFFSCQDDNSTLISITSLADSEMLINLLEYENVTDIWIGLscNKTPVEFEWSDGSAVIFTY--WNKQE 460
Cdd:cd03592      3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYYWIDG--NDINNEGTWVDTDKKELEYknWAPGE 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1663456190  461 PNilQKKGQICV-SAQQHEGRWEIKNCKSRYFYICKR 496
Cdd:cd03592     81 PN--NGRNENCLeIYIKDNGKWNDEPCSKKKSAICYT 115

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.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 47.96 E-value: 2.42e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  814 WFYYQGAEYLFYDSPSNWDSFQFVCGWLHGDIATIQSFQEQEFIQNRIKKISKKssswwiALRSELPSEEFRWTDGSLLS 893
Cdd:cd03588      5 WDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWI------GLNDRTIEGDFRWSDGHPLQ 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1663456190  894 YQNWAGDKERPKPAQGPKC-AFISSQTGQWGFANCTISLPCVCKR 937
Cdd:cd03588     79 FENWRPNQPDNFFATGEDCvVMIWHEEGEWNDVPCNYHLPFTCKK 123

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.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 47.96 E-value: 2.44e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  244 SWNEARVACQGQGADLLSITDMREQKYIGglieqlNTKEAMIWTGLNQLDETAGWQWSDGAPLALVNWLKDPIDGSLGPA 323
Cdd:cd03588     21 TWEDAERRCREQQGHLSSIVTPEEQEFVN------NNAQDYQWIGLNDRTIEGDFRWSDGHPLQFENWRPNQPDNFFATG 94

                           90       100
                   ....*....|....*....|....*....
gi 1663456190  324 H-CKAFNLKIQNDWPSYSCESRLPYVCKK 351
Cdd:cd03588     95 EdCVVMIWHEEGEWNDVPCNYHLPFTCKK 123

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.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 47.80 E-value: 2.58e-06

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1663456190  244 SWNEARVACQGQGADLLSITDMREQKYIGgliEQLNTKEAmIWTGLNQLDETAGWQWSDGAPLALVNW 311
Cdd:cd03603     11 TWEAAQTLAESLGGHLVTINSAEENDWLL---SNFGGYGA-SWIGASDAATEGTWKWSDGEESTYTNW 74

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 49.34 E-value: 4.22e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1663456190  955 TCPKGWLYFGFKCFLvqIPKDSahlKSWHSAQKTCSYYDASLVSVENEVEQAFiaMNLLGHKSNVWIGLQSDS 1027
Cdd:PHA02642    87 TCPKGWIGFGYKCFY--FSEDS---KNWTFGNTFCTSLGATLVKVETEEELNF--LKRYKDSSDHWIGLNRES 152

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 46.98 E-value: 5.39e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190 1112 PDTLEYANSTYTLINGSMTWNMASQMCKK--NGAELVSITDYYHQAFLTVIINRVGYAH---WIGLFTSDDGLPFEWSDG 1186
Cdd:cd03594      3 KGWLPYKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYQKAYqpvWIGLHDPQQSRGWEWSDG 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1663456190 1187 TRP-FFTFWGEEETQGPGHCVYI-DTNGH--WKNTDCEKLL 1223
Cdd:cd03594     83 SKLdYRSWDRNPPYARGGYCAELsRSTGFlkWNDANCEERN 123

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

Pssm-ID: 214480 [Multi-domain] Cd Length: 124 Bit Score: 46.82 E-value: 5.79e-06

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1663456190  1250 WIRFDRNCYSFSTvfENLNFYEALEFCSRQDSNLLTIKGRDENIFILEELHSFGSvVEMIWL 1311
Cdd:smart00034    5 WISYGGKCYKFST--EKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGS-SDYYWI 63

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 47.19 E-value: 7.89e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  967 CFLVQIPKDSAHLKSWHSAQKTCSYYDASLVSVENEVEQAFIA---MNLLGHKSNVWIGLQSDSYEKWLNG---QEVEYA 1040
Cdd:cd03595     12 CYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIErfiQTLRASDGDFWIGLRRSSQYNVTSSacsSLYYWL 91

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1663456190 1041 NWSPAQVRhqNHYIGDTEKKDVLCTSILNNPSFS------LMGKWYLESCENKNGFVCQ 1093
Cdd:cd03595     92 DGSISTFR--NWYVDEPSCGSEVCVVMYHQPSAPagqggpYLFQWNDDNCNMKNNFICK 148

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 46.58 E-value: 1.00e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190 1116 EYANSTYTLINGSMTWNMASQMCKKNG-----AELVSITDYYHQAFLTVIINRVG-----YAHWIGLF-TSDDGlPFEWS 1184
Cdd:cd03589      7 AFGGYCYRFFGDRLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFESSRgpdtpYGLWIGLHdRTSEG-PFEWT 85

                           90
                   ....*....|.
gi 1663456190 1185 DGTRPFFTFWG 1195
Cdd:cd03589     86 DGSPVDFTKWA 96

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.

Pssm-ID: 153059 Cd Length: 137 Bit Score: 45.43 E-value: 2.12e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  511 CPEGWERHGEYCYKVDTIPRSFEHASNgyYCPS---------LATITSRFEQDFLNSMIHHQGNTDSPY-FWIALQDLNN 580
Cdd:cd03589      1 CPTFWTAFGGYCYRFFGDRLTWEEAEL--RCRSfsipgliahLVSIHSQEENDFVYDLFESSRGPDTPYgLWIGLHDRTS 78

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1663456190  581 TGEYTWlTEDRKHHlaiYTNWGKHQP-RYPGG--CVVMRQEEPIG-MWEVKNCATFMaKSLCK 639
Cdd:cd03589     79 EGPFEW-TDGSPVD---FTKWAGGQPdNYGGNedCVQMWRRGDAGqSWNDMPCDAVF-PYICK 136

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 44.81 E-value: 2.37e-05

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1663456190    39 IQSENFSTCITAEMSE--LILENCNQVSKYMLWKWGSKQQLFNIGRSSCLGLNLSNPEPsLVMTQCDSPRYLLQWQC 113
Cdd:smart00458    1 IISGNTGKCLDVNGNKnpVGLFDCHGTGGNQLWKLTSDGAIRIKDTDLCLTANGNTGST-VTLYSCDGTNDNQYWEV 76

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.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 45.11 E-value: 2.42e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1663456190  383 YKLHKEEKNWNEAFFSCQDDNSTLISITSLADSEMLINLLEYENvtDIWIGLSCNKTPVEFEWSDGSAVIFTYWNKQEP 461
Cdd:cd03603      3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYG--ASWIGASDAATEGTWKWSDGEESTYTNWGSGEP 79

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 44.63 E-value: 3.02e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1663456190 1250 WIRFDRNCYSFSTvfENLNFYEALEFCSRQDSNLLTIKGRDENIFILE 1297
Cdd:cd03593      5 WICYGNKCYYFSM--EKKTWNESKEACSSKNSSLLKIDDEEELEFLQS 50

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 44.63 E-value: 3.24e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  814 WFYYQGAEYLFYDSPSNWDSFQFVCGWLHGDIATIQSFQEQEFIQNRIKKISKKSsswwiALRSELPSEEFRWTDGSLLS 893
Cdd:cd03593      5 WICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWI-----GLSREKSEKPWKWIDGSPLN 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1663456190  894 yqNWAgdkERPKPAQGPKCAFISSqtgqWGF--ANCTISLPCVCKR 937
Cdd:cd03593     80 --NLF---NIRGSTKSGNCAYLSS----TGIysEDCSTKKRWICEK 116

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

Pssm-ID: 153068 Cd Length: 117 Bit Score: 43.98 E-value: 4.62e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  822 YLFYDSPSNWDSFQFVCGWLH-GDIATIQSFQEQEFIQNRIKKISKKSSSWWIALRSELPSEEFRWTDGSLLSYQNWAGD 900
Cdd:cd03598      4 YRFVKSPRTFRDAQVICRRCYrGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIITGKGRCRRFSWVDGSVWNYAYWAPG 83

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1663456190  901 keRPKPAQGpKCAFISSQTGQWGFANCTISLPCVC 935
Cdd:cd03598     84 --QPGNRRG-HCVELCTRGGHWRRAHCKLRRPFIC 115

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.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 43.90 E-value: 5.60e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190 1121 TYTLINGSMTWNMASQMCKKNGAELVSITDYYHQAFLTVIINRV--GYaHWIGLFTSDDGLPFEWSDGTRPFFTFWGEEE 1198
Cdd:cd03592      2 TYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYnlGY-YWIDGNDINNEGTWVDTDKKELEYKNWAPGE 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1663456190 1199 TQGPG--HCV--YIDTNGHWKNTDCEKLLSgAICH 1229
Cdd:cd03592     81 PNNGRneNCLeiYIKDNGKWNDEPCSKKKS-AICY 114

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.

Pssm-ID: 153064 [Multi-domain] Cd Length: 129 Bit Score: 43.90 E-value: 6.93e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  814 WFYYQGAEYLFYDSPSNWDSFQFVCGWLH--GDIATIQSFQEQEFIQNRIKKISKKSSSWWIALRSELPSEEFRWTDGSL 891
Cdd:cd03594      5 WLPYKGNCYGYFRQPLSWSDAELFCQKYGpgAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSRGWEWSDGSK 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1663456190  892 LSYQNWAGDkerPKPAQGPKCAFISSQTG--QWGFANCTISLPCVCK 936
Cdd:cd03594     85 LDYRSWDRN---PPYARGGYCAELSRSTGflKWNDANCEERNPFICK 128

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.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 43.57 E-value: 7.96e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1663456190  690 TWEEAETLCQDFGAHLASFKQVLEKDFLNKLLNTmfhiddERQFWIGFNKRNplSGGSWQWSDGTPVSSAF 760
Cdd:cd03603     11 TWEAAQTLAESLGGHLVTINSAEENDWLLSNFGG------YGASWIGASDAA--TEGTWKWSDGEESTYTN 73

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.

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 43.05 E-value: 8.78e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190 1122 YTLING-SMTWNMASQMCKKNGAELVSITDYYHQAFLTVIINRVGYAHWIGLftSDDGLP--FEWSDGTRPFFTFWGEEE 1198
Cdd:cd03591      3 IFVTNGeEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGI--TDLETEgqFVYLDGGPLTYTNWKPGE 80

                           90       100
                   ....*....|....*....|....
gi 1663456190 1199 TQGPGH---CVYIDTNGHWKNTDC 1219
Cdd:cd03591     81 PNNAGGgedCVEMYTSGKWNDVAC 104

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.

Pssm-ID: 153070 Cd Length: 141 Bit Score: 43.96 E-value: 9.07e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  676 CYKVFHSekvlmKRTWEEAETLCQDFGAHLASFKQVLEKDFLNKLLNTM--FHIDDERQFWIGFNKR--------NPLSG 745
Cdd:cd03600      6 CYTLHPQ-----KLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGpgRHGRGSLRLWIGLQREprqcsdpsLPLRG 80


                   ....*..
gi 1663456190  746 GSWQWSD 752
Cdd:cd03600     81 FSWVTGD 87

ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e and similar proteins; PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, R-PTP-beta, vascular endothelial protein tyrosine phosphatase, or VE-PTP, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells, which requires the presence of plakoglobin. The subfamily corresponds to PTPRB isoform e, which contains an extra ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467787 Cd Length: 117 Bit Score: 43.20 E-value: 9.45e-05

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1663456190   55 LILENCNQVSKYMLWKWGSKQQLFNIGRSSCLGLNLSNPEPS--LVMTQC-DSPRyllqWQCHGK 116
Cdd:cd23409     21 VSVGKCNATSPNQQWQWTEDGKLLHVKSGQCLGISNSSAFHSrrAILLDCsQAPR----WTCHEN 81

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.

Pssm-ID: 153073 [Multi-domain] Cd Length: 118 Bit Score: 43.18 E-value: 9.94e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  981 SWHSAQKTCSYYDASLVSVENEVEQAFIAmNLLGHKSNVWIGLQSDSYE---KWLNGQEVEYANWSPAQVRHQN----HY 1053
Cdd:cd03603     11 TWEAAQTLAESLGGHLVTINSAEENDWLL-SNFGGYGASWIGASDAATEgtwKWSDGEESTYTNWGSGEPHNNGggneDY 89

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1663456190 1054 IGDtekkdvlctsilnNPSFSLMGKWY-LESCENKNGFV 1091
Cdd:cd03603     90 AAI-------------NHFPGISGKWNdLANSYNTLGYV 115

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.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 42.75 E-value: 1.03e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  820 AEYLFYDSPSNWDSFQFVCGWLHGDIATIQSFQEQEFIQNrikkiskkssswwiALRSELP---------SEEFRWTDGS 890
Cdd:cd03602      1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSN--------------LSRVSNSaawiglyrdVDSWRWSDGS 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1663456190  891 LLSYQNWAgdkeRPKPAQGPKCAFISSqTGQWGFANCTISLPCVC 935
Cdd:cd03602     67 ESSFRNWN----TFQPFGQGDCATMYS-SGRWYAALCSALKPFIC 106

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.

Pssm-ID: 153065 Cd Length: 149 Bit Score: 43.34 E-value: 1.79e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  382 CYKLH-----KEEKNWNEAFFSCQDDNSTLISITSLADSEMLINLLEYENVTD--IWIGL--------SCNKTPVEFEWS 446
Cdd:cd03595     12 CYKIAyfqdsRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDgdFWIGLrrssqynvTSSACSSLYYWL 91

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  447 DGSAVIFTYWNKQEPNIlqkKGQICV------SAQQHEG-----RWEIKNCKSRYFYICK 495
Cdd:cd03595     92 DGSISTFRNWYVDEPSC---GSEVCVvmyhqpSAPAGQGgpylfQWNDDNCNMKNNFICK 148

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

Pssm-ID: 153068 Cd Length: 117 Bit Score: 42.44 E-value: 2.05e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190 1119 NSTYTLINGSMTWNMASQMCKK-NGAELVSITDYYHQAFLTVIINRVGYAH-WIGLFTSDDGL--PFEWSDGTRPFFTFW 1194
Cdd:cd03598      1 GRCYRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTLNQAQvWIGGIITGKGRcrRFSWVDGSVWNYAYW 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1663456190 1195 GEEE-TQGPGHCVYIDT-NGHWKNTDCEKLL 1223
Cdd:cd03598     81 APGQpGNRRGHCVELCTrGGHWRRAHCKLRR 111

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

Pssm-ID: 153066 Cd Length: 129 Bit Score: 42.38 E-value: 2.24e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  956 CPKGwLYFGFKCFLVqipkdSAHLKSWHSAQKTCSYYDASLV----SVENEVEQAFiAMNLLGHKSNVWIGLQSDSYE-K 1030
Cdd:cd03596      1 CLKG-TKIHKKCYLV-----SEETKHYHEASEDCIARGGTLAtprdSDENDALRDY-VKASVPGNWEVWLGINDMVAEgK 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1663456190 1031 WL--NGQEVEYANWSPAQVRHQNHyiGDTEKKDVLctsilnnpSFSLMGKWYLESCENKNGFVCQ 1093
Cdd:cd03596     74 WVdvNGSPISYFNWEREITAQPDG--GKRENCVAL--------SSSAQGKWFDEDCRREKPYVCE 128

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.

Pssm-ID: 153057 [Multi-domain] Cd Length: 116 Bit Score: 41.07 E-value: 4.98e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1663456190 1256 NCYSFSTvfENLNFYEALEFCSRQDSNLLTIKGRDENIFILEELHSFGSvvEMIWL 1311
Cdd:cd00037      1 SCYKFST--EKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSS--SDVWI 52

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.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 41.41 E-value: 5.17e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  956 CPKGWLYFGFKCFlvqipKDSAHLKSWHSAQKTCSYYDASLVSVENEVEQAFIAMNLLGHKsnvWIGLQSDSYE---KWL 1032
Cdd:cd03588      1 CEEGWDKFQGHCY-----RHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ---WIGLNDRTIEgdfRWS 72

                           90
                   ....*....|....
gi 1663456190 1033 NGQEVEYANWSPAQ 1046
Cdd:cd03588     73 DGHPLQFENWRPNQ 86

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 40.75 E-value: 7.02e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1663456190 1250 WIRFDRNCYSFSTvfENLNFYEALEFCSRQDSNLLTIKGRDENIFI 1295
Cdd:cd03590      5 WKSFQSSCYFFST--EKKSWEESRQFCEDMGAHLVIINSQEEQEFI 48

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.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 40.44 E-value: 7.65e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  243 LSWNEARVACQGQGADLLSITDMREQKYIGGLIEQLNTKeaMIWTGLNQLDETAGWQWSDGAPLALVNWLKDPIDGSLGp 322
Cdd:cd03592     10 MTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLG--YYWIDGNDINNEGTWVDTDKKELEYKNWAPGEPNNGRN- 86

                           90       100
                   ....*....|....*....|....*..
gi 1663456190  323 AHCKAFNLKIQNDWPSYSCESRLPYVC 349
Cdd:cd03592     87 ENCLEIYIKDNGKWNDEPCSKKKSAIC 113

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.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 40.05 E-value: 9.81e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  689 RTWEEAETLCQDFGAHLASFKQVLEKDFLNKLLNTMFHidderQFWIGFNKRNplsgGSWQWSDGTPvsSAFLEKASIED 768
Cdd:cd03602     10 KTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNS-----AAWIGLYRDV----DSWRWSDGSE--SSFRNWNTFQP 78

                           90       100
                   ....*....|....*....|....*...
gi 1663456190  769 --VKNCAAYKTNGTILPLHCNSEHEWIC 794
Cdd:cd03602     79 fgQGDCATMYSSGRWYAALCSALKPFIC 106

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 42.02 E-value: 1.02e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  647 KSDTnKQPNYEesFNSCMHGWESDHYllNCYkvFHSEKvlmKRTWEEAETLCQDFGAHLASFKQVLEKDFLNKLLNTMFH 726
Cdd:PHA02642    75 KSDT-QEPTIK--YVTCPKGWIGFGY--KCF--YFSED---SKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDH 144

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1663456190  727 idderqfWIGFNKRNplSGGSWQWSDGTPVSSAFLEKASIEdvkncAAYKTNGTILPLHCNSEHEWIC 794
Cdd:PHA02642   145 -------WIGLNRES--SNHPWKWADNSNYNASFVITGTGE-----CAYLNDIRISSSRVYANRKWIC 198

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.

Pssm-ID: 153062 Cd Length: 115 Bit Score: 39.67 E-value: 1.48e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  980 KSWHSAQKTCSYYDASLVSVENEVEQAFIAMNLLGHKSNV-WIGLQSDSYE-KWL--NGQEVEYANWSPAQ---VRHQNh 1052
Cdd:cd03592     10 MTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYyWIDGNDINNEgTWVdtDKKELEYKNWAPGEpnnGRNEN- 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1663456190 1053 yigdtekkdvlCTSILNNPSfslmGKWYLESCENKNGFVCQK 1094
Cdd:cd03592     89 -----------CLEIYIKDN----GKWNDEPCSKKKSAICYT 115

Extracellular link domain;

Pssm-ID: 459706 Cd Length: 92 Bit Score: 39.09 E-value: 1.63e-03

                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1663456190  678 KVFHSEKvlMKR---TWEEAETLCQDFGAHLASFKQVLE 713
Cdd:pfam00193    1 GVFHLES--PGRyklTFQEAQAACAALGATLATPEQLYA 37

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 41.25 E-value: 1.73e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  368 PTI----CDSNWYPYNNYCYKLHKEEKNWNEAFFSCQDDNSTLISItslaDSEMLINLLE-YENVTDIWIGLSCNKTPVE 442
Cdd:PHA02642    81 PTIkyvtCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKV----ETEEELNFLKrYKDSSDHWIGLNRESSNHP 156


                   ....*...
gi 1663456190  443 FEWSDGSA 450
Cdd:PHA02642   157 WKWADNSN 164

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

Pssm-ID: 153066 Cd Length: 129 Bit Score: 39.29 E-value: 2.45e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  244 SWNEARVACQGQGADLLSITDMREQKYIGGLIEQLNTKEAMIWTGLNQLDETAGWQWSDGAPLALVNW---LKDPIDGsl 320
Cdd:cd03596     20 HYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGNWEVWLGINDMVAEGKWVDVNGSPISYFNWereITAQPDG-- 97

                           90       100       110
                   ....*....|....*....|....*....|
gi 1663456190  321 GPAH-CKAFNLKIQNDWPSYSCESRLPYVC 349
Cdd:cd03596     98 GKREnCVALSSSAQGKWFDEDCRREKPYVC 127

C-type lectin-like protein; Provisional

Pssm-ID: 222982 [Multi-domain] Cd Length: 157 Bit Score: 39.85 E-value: 3.20e-03

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1663456190  371 CDSNWYPYNNYCYKLHKEEKNWNEAFFSCQDDNSTLISItsLADSEMLInLLEYENVTDIWIGLS 435
Cdd:PHA03097    46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLI--DDQKEVLF-VSRYKGGQDLWIGIE 107

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

Pssm-ID: 153066 Cd Length: 129 Bit Score: 38.91 E-value: 3.66e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  382 CYKLHKEEKNWNEAFFSCQDDNSTLISITSLADSEMLINLLE--YENVTDIWIGLscNKTPVEFEWSD--GSAVIFTYWN 457
Cdd:cd03596     11 CYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKasVPGNWEVWLGI--NDMVAEGKWVDvnGSPISYFNWE 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1663456190  458 KQEPNilQKKG---QICVS-AQQHEGRWEIKNCKSRYFYIC 494
Cdd:cd03596     89 REITA--QPDGgkrENCVAlSSSAQGKWFDEDCRREKPYVC 127

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.

Pssm-ID: 153058 Cd Length: 124 Bit Score: 38.71 E-value: 4.02e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  511 CPEGWERHGEYCYKVDTIPRSFEHASNgyYC----PSLATITSRFEQDFLNSMIHHqgntdspYFWIALQDLNNTGEYTW 586
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAER--RCreqqGHLSSIVTPEEQEFVNNNAQD-------YQWIGLNDRTIEGDFRW 71

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1663456190  587 ltedRKHHLAIYTNWGKHQPR--YPGG--CVVM 615
Cdd:cd03588     72 ----SDGHPLQFENWRPNQPDnfFATGedCVVM 100

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.

Pssm-ID: 153063 Cd Length: 116 Bit Score: 38.08 E-value: 6.31e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190 1117 YANSTYTLINGSMTWNMASQMCKKNGAELVSITDYYHQAFLTVIINRvgYAHWIGLFTSDDGLPFEWSDGTRPFFTFwGE 1196
Cdd:cd03593      8 YGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--SSYWIGLSREKSEKPWKWIDGSPLNNLF-NI 84

                           90       100
                   ....*....|....*....|....*
gi 1663456190 1197 EETQGPGHCVYIDTNGhWKNTDCEK 1221
Cdd:cd03593     85 RGSTKSGNCAYLSSTG-IYSEDCST 108

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.

Pssm-ID: 153060 [Multi-domain] Cd Length: 126 Bit Score: 38.05 E-value: 6.66e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663456190  814 WFYYQGAEYLFYDSPSNWDSFQFVCGWLHGDIATIQSFQEQEFIQnrikKISKKSSSWWIALRSELPSEEFRWTDGSLL- 892
Cdd:cd03590      5 WKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS----KILSGNRSYWIGLSDEETEGEWKWVDGTPLn 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1663456190  893 -SYQNWagDKERPKPAQGP--KCAFISSQTGQWGFANCTISLPCVCKR 937
Cdd:cd03590     81 sSKTFW--HPGEPNNWGGGgeDCAELVYDSGGWNDVPCNLEYRWICEK 126