NCBI Conserved Domain Search

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: 231.87 E-value: 1.17e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   23 RQFLIYNEDHKRCVDAVSPSAVQTAACNQDAESQKFRWVSESQIMSVAFKLCLGVPSKTDWVAITLYACDSKSEFQKWEC 102
Cdd:cd23407    1 RSFLIYNEDHNRCVQARSSSSVTTATCNPNAESQKFRWVSGSQILSVAFKLCLGVPSKKDWVTVTLFPCNEKSELQKWEC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 55666046  103 KNDTLLGIKGEDLFFNYGNRQEKNIMLYKGSGLWSRWKIYGTT 145
Cdd:cd23407   81 KNDTLLALKGEDLYFNYGNRQEKNVMLYKGSGLWSRWKIYGTT 123

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: 130.41 E-value: 3.42e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   24 QFLIYNEDHKRCVDAVSP-SAVQTAACNQDAESQKFRWVSESQIMSVAFKLCLGVPSKTDWVAITLYACDSKSEFQKWEC 102
Cdd:cd23385    2 SFLIYNEDLGKCLAARSSsSKVSLSTCNPNSPNQQWKWTSGHRLFNVGTGKCLGVSSSSPSSPLRLFECDSEDELQKWKC 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 55666046  103 KNDTLLGIKGEDLFFNYgNRQEKNIMLYKGSGLWSRWKI 141
Cdd:cd23385   82 SKDGLLLLKGLGLLLLY-DKSGKNVVVSKGSGLSSRWKI 119

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: 122.71 E-value: 2.08e-32

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046     362 CPSQWWPYAGHCYKIHrDEKKIQRDALTTCRKEGSDLASIHTIEEFDFIISQLG-YEPNDELWIGLNDIKIQMYFEWSDG 440
Cdd:smart00034    1 CPSGWISYGGKCYKFS-TEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnSGSSDYYWIGLSDPDSNGSWQWSDG 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 55666046     441 TP-VTFTKWLRGEPsheNNRQEDCVVMKGKDGYWADRGCEWPLGYICK 487
Cdd:smart00034   80 SGpVSYSNWAPGEP---NNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 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: 120.40 E-value: 1.10e-31

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046     945 CKEGWNFYSNKCFKIFGfmeeERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFS--AWTGLNDVNSEHTFLW 1022
Cdd:smart00034    1 CPSGWISYGGKCYKFST----EKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQW 76

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 55666046    1023 TDGRG-VHYTNWGKGYPGGRRSslsyedaDCVVIiggaSNEAGKWMDDTCDSKRGYICQ 1080
Cdd:smart00034   77 SDGSGpVSYSNWAPGEPNNSSG-------DCVVL----STSGGKWNDVSCTSKLPFVCE 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: 119.24 E-value: 2.80e-31

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046    1230 CPESdhtaWIPFHGHCYYIeSSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEPLKSKTNFWIGLFR-NVEGTWL 1308
Cdd:smart00034    1 CPSG----WISYGGKCYKF-STEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWIGLSDpDSNGSWQ 75

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 55666046    1309 WINNSP-VSFVNWNTGDPSGERNDCVALHASSGFWSNIHCSSYKGYICK 1356
Cdd:smart00034   76 WSDGSGpVSYSNWAPGEPNNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 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: 116.95 E-value: 1.42e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  659 CFKLYakgkHEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYHklFWLGLTYGSPSEGFTWSDGSP-VSYE 737
Cdd:cd00037    2 CYKFS----TEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSD--VWIGLNDLSSEGTWKWSDGSPlVDYT 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 55666046  738 NWAYGEPNNYQNvEYCGELKGDPTMSWNDINCEHLNNWICQI 779
Cdd:cd00037   76 NWAPGEPNPGGS-EDCVVLSSSSDGKWNDVSCSSKLPFICEK 116

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: 115.79 E-value: 4.55e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  372 HCYKIHRdEKKIQRDALTTCRKEGSDLASIHTIEEFDFIISQLGYEPNDELWIGLNDIKIQMYFEWSDGTP-VTFTKWLR 450
Cdd:cd00037    1 SCYKFST-EKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAP 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 55666046  451 GEPSheNNRQEDCVVMK-GKDGYWADRGCEWPLGYICKM 488
Cdd:cd00037   80 GEPN--PGGSEDCVVLSsSSDGKWNDVSCSSKLPFICEK 116

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: 113.46 E-value: 3.44e-29

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046     802 DGWVIYKDYQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDAQSAYFIGL-LISLDKKFAWMDGSK- 879
Cdd:smart00034    3 SGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWIGLsDPDSNGSWQWSDGSGp 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 55666046     880 VDYVSWATGEPNfaNEDENCVTMYSNSGFWNDINCGYPNAFICQ 923
Cdd:smart00034   83 VSYSNWAPGEPN--NSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 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: 110.40 E-value: 3.25e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  955 KCFKIFgfmeEERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKD-STFSAWTGLNDVNSEHTFLWTDGRG-VHYTN 1032
Cdd:cd00037    1 SCYKFS----TEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKsSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTN 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 55666046 1033 WGKGYPGGRRSSlsyedaDCVVIiggASNEAGKWMDDTCDSKRGYICQ 1080
Cdd:cd00037   77 WAPGEPNPGGSE------DCVVL---SSSSDGKWNDVSCSSKLPFICE 115

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: 110.00 E-value: 6.38e-28

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046     646 CPEDWGASSRTslCFKLYakgkHEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYHKlFWLGLTYGSPSEG 725
Cdd:smart00034    1 CPSGWISYGGK--CYKFS----TEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDY-YWIGLSDPDSNGS 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 55666046     726 FTWSDGSP-VSYENWAYGEPNNyqNVEYCGELKGDPTmSWNDINCEHLNNWICQ 778
Cdd:smart00034   74 WQWSDGSGpVSYSNWAPGEPNN--SSGDCVVLSTSGG-KWNDVSCTSKLPFVCE 124

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 106.02 E-value: 8.41e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046    967 RKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFSAWTGLNDVNSEHTFLWTDGRGVHYTNWgkgypgGRRSSLS 1046
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNW------APEPNNN 74

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 55666046   1047 YEDADCVVIiggaSNEAGKWMDDTCDSKRGYICQT 1081
Cdd:pfam00059   75 GENEDCVEL----SSSSGKWNDENCNSKNPFVCEK 105

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: 105.37 E-value: 2.50e-26

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046     504 CRKGWKKHHFYCYMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFVG-LRPEKYFWTGLSDIQTKGTFQWT-IE 581
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnSGSSDYYWIGLSDPDSNGSWQWSdGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 55666046     582 EEVRFTHWNSDMPGRKPG-CVAMRTGiaGGLWDVLKCDEKAKFVCK 626
Cdd:smart00034   81 GPVSYSNWAPGEPNNSSGdCVVLSTS--GGKWNDVSCTSKLPFVCE 124

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 102.56 E-value: 1.11e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046    386 DALTTCRKEGSDLASIHTIEEFDFIISQLGyEPNDELWIGLNDIKIQMYFEWSDGTPVTFTKWlrGEPSHENNRQEDCVV 465
Cdd:pfam00059    6 EAREACRKLGGHLVSINSAEELDFLSSTLK-KSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNW--APEPNNNGENEDCVE 82

                           90       100
                   ....*....|....*....|...
gi 55666046    466 MKGKDGYWADRGCEWPLGYICKM 488
Cdd:pfam00059   83 LSSSSGKWNDENCNSKNPFVCEK 105

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: 102.70 E-value: 1.45e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  810 YQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDAQSaYFIGL-LISLDKKFAWMDGSK-VDYVSWAT 887
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSD-VWIGLnDLSSEGTWKWSDGSPlVDYTNWAP 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 55666046  888 GEPNFaNEDENCVTMYSNS-GFWNDINCGYPNAFICQR 924
Cdd:cd00037   80 GEPNP-GGSEDCVVLSSSSdGKWNDVSCSSKLPFICEK 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: 101.23 E-value: 7.32e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1230 CPESdhtaWIPFHGHCYYIeSSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEplkSKTNFWIGLF-RNVEGTWL 1308
Cdd:cd03590    1 CPTN----WKSFQSSCYFF-STEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILS---GNRSYWIGLSdEETEGEWK 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55666046 1309 WINNSPV--SFVNWNTGDPS---GERNDCVALHASSGFWSNIHCSSYKGYICKR 1357
Cdd:cd03590   73 WVDGTPLnsSKTFWHPGEPNnwgGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126

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: 100.84 E-value: 8.80e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  646 CPEDWGASsrTSLCFKLyakgKHEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYhklfWLGLTyGSPSEG 725
Cdd:cd03590    1 CPTNWKSF--QSSCYFF----STEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSY----WIGLS-DEETEG 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 55666046  726 -FTWSDGSPV--SYENWAYGEPNNYQNV-EYCGELKGDpTMSWNDINCEHLNNWICQ 778
Cdd:cd03590   70 eWKWVDGTPLnsSKTFWHPGEPNNWGGGgEDCAELVYD-SGGWNDVPCNLEYRWICE 125

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: 100.00 E-value: 1.23e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  234 SKSALTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSG-LWIGLNSLSFNSGWQWSDRSP-FRYLNWLPGSPSAE 311
Cdd:cd00037    6 STEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPGEPNPG 85

                         90       100       110
                 ....*....|....*....|....*....|.
gi 55666046  312 PGKSCVSLNPGKNAKWENLECVQKLGYICKK 342
Cdd:cd00037   86 GSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 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: 99.47 E-value: 1.38e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   1253 TRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEplKSKTNFWIGL-FRNVEGTWLWINNSPVSFVNWN-TGDPSGERN 1330
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLK--KSNKYFWIGLtDRKNEGTWKWVDGSPVNYTNWApEPNNNGENE 78

                           90       100
                   ....*....|....*....|....*..
gi 55666046   1331 DCVALHASSGFWSNIHCSSYKGYICKR 1357
Cdd:pfam00059   79 DCVELSSSSGKWNDENCNSKNPFVCEK 105

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: 98.08 E-value: 5.95e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  514 YCYMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFVGLRPEKYFWTGLSDIQTKGTFQWTI-EEEVRFTHWNSD 592
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKWSDgSPLVDYTNWAPG 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 55666046  593 MP--GRKPGCVAMRTGIAGGlWDVLKCDEKAKFVCKH 627
Cdd:cd00037   81 EPnpGGSEDCVVLSSSSDGK-WNDVSCSSKLPFICEK 116

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: 97.69 E-value: 7.81e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1244 HCYYIeSSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVePLKSKTNFWIGLFR-NVEGTWLWINNSP-VSFVNWN 1321
Cdd:cd00037    1 SCYKF-STEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLL-KKSSSSDVWIGLNDlSSEGTWKWSDGSPlVDYTNWA 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 55666046 1322 TGDPSGERN-DCVALHASS-GFWSNIHCSSYKGYICKR 1357
Cdd:cd00037   79 PGEPNPGGSeDCVVLSSSSdGKWNDVSCSSKLPFICEK 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: 96.01 E-value: 2.45e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046    670 KKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYhklFWLGLTYGSPSEGFTWSDGSPVSYENWAyGEPNNYQN 749
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY---FWIGLTDRKNEGTWKWVDGSPVNYTNWA-PEPNNNGE 76

                           90       100
                   ....*....|....*....|....*....
gi 55666046    750 VEYCGELKGDPTmSWNDINCEHLNNWICQ 778
Cdd:pfam00059   77 NEDCVELSSSSG-KWNDENCNSKNPFVCE 104

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: 93.52 E-value: 3.18e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  362 CPSQWWPYAGHCYKIHRdEKKIQRDALTTCRKEGSDLASIHTIEEFDFIISQLGYepNDELWIGLNDIKIQMYFEWSDGT 441
Cdd:cd03590    1 CPTNWKSFQSSCYFFST-EKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSG--NRSYWIGLSDEETEGEWKWVDGT 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 55666046  442 PV--TFTKWLRGEPSHENNRQEDCVVMKGKDGYWADRGCEWPLGYICKM 488
Cdd:cd03590   78 PLnsSKTFWHPGEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 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: 92.66 E-value: 7.17e-22

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046     234 SKSALTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSG--LWIGLNSLSFNSGWQWSDRSP-FRYLNWLPGSPSA 310
Cdd:smart00034   16 STEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSDGSGpVSYSNWAPGEPNN 95

                            90       100       110
                    ....*....|....*....|....*....|.
gi 55666046     311 EPGkSCVSLNpGKNAKWENLECVQKLGYICK 341
Cdd:smart00034   96 SSG-DCVVLS-TSGGKWNDVSCTSKLPFVCE 124

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: 87.35 E-value: 5.01e-21

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 55666046     161 GNANGATCAFPFKFENKWYADCTSAGRSDGWLWCGTTTDYDTDKLFGYC 209
Cdd:smart00059    1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49

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: 89.94 E-value: 5.69e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  362 CPSQWWPYAGHCYKiHRDEKKIQRDALTTCRKEGSDLASIHTIEEFDFIISQlgyePNDELWIGLNDIKIQMYFEWSDGT 441
Cdd:cd03588    1 CEEGWDKFQGHCYR-HFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNN----AQDYQWIGLNDRTIEGDFRWSDGH 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 55666046  442 PVTFTKWLRGEPSHENNRQEDCVVMKGKD-GYWADRGCEWPLGYICKM 488
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: 89.29 E-value: 1.01e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  801 EDGWVIYKDYQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDaqsAYFIGLL-ISLDKKFAWMDGSK 879
Cdd:cd03590    2 PTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNR---SYWIGLSdEETEGEWKWVDGTP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 55666046  880 V--DYVSWATGEP-NFANEDENCVTMYSNSGFWNDINCGYPNAFICQR 924
Cdd:cd03590   79 LnsSKTFWHPGEPnNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126

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: 87.80 E-value: 4.32e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  362 CPSQWWPYAGHCYKIHRDEKKIQrDALTTCRKEGS-----DLASIHTIEEFDFII----SQLGYEPNDELWIGLNDIKIQ 432
Cdd:cd03589    1 CPTFWTAFGGYCYRFFGDRLTWE-EAELRCRSFSIpgliaHLVSIHSQEENDFVYdlfeSSRGPDTPYGLWIGLHDRTSE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 55666046  433 MYFEWSDGTPVTFTKWLRGEPSHENNrQEDCVVMK---GKDGYWADRGCEWPLGYICKM 488
Cdd:cd03589   80 GPFEWTDGSPVDFTKWAGGQPDNYGG-NEDCVQMWrrgDAGQSWNDMPCDAVFPYICKM 137

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: 86.64 E-value: 1.09e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  945 CKEGWNFYSNKCFKIFGfmeeERKNWQEARKACIGFG-----GNLVSIQNEKEQAFLtYHM------KDSTFSAWTGLND 1013
Cdd:cd03589    1 CPTFWTAFGGYCYRFFG----DRLTWEEAELRCRSFSipgliAHLVSIHSQEENDFV-YDLfessrgPDTPYGLWIGLHD 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55666046 1014 VNSEHTFLWTDGRGVHYTNWGKGYPGGRrsslsYEDADCVVIIGGASNEaGKWMDDTCDSKRGYICQT 1081
Cdd:cd03589   76 RTSEGPFEWTDGSPVDFTKWAGGQPDNY-----GGNEDCVQMWRRGDAG-QSWNDMPCDAVFPYICKM 137

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: 85.50 E-value: 2.13e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  362 CPSQWWPYAGHCYKIHRDEKKiQRDALTTCRK--EGSDLASIHTIEEFDFIISQL-GYEPNDE-LWIGLNDIKIQMYFEW 437
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLS-WSDAELFCQKygPGAHLASIHSPAEAAAIASLIsSYQKAYQpVWIGLHDPQQSRGWEW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 55666046  438 SDGTPVTFTKWLRGEPShenNRQEDCVVMKGKDGY--WADRGCEWPLGYICK 487
Cdd:cd03594   80 SDGSKLDYRSWDRNPPY---ARGGYCAELSRSTGFlkWNDANCEERNPFICK 128

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: 85.49 E-value: 3.30e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  646 CPEDWgaSSRTSLCFKLYAkgkhEKKTWFESRDFCRALG-----GDLASINNKEEQQ---TIWRLITASGSYHKLfWLGL 717
Cdd:cd03589    1 CPTFW--TAFGGYCYRFFG----DRLTWEEAELRCRSFSipgliAHLVSIHSQEENDfvyDLFESSRGPDTPYGL-WIGL 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55666046  718 tYGSPSEG-FTWSDGSPVSYENWAYGEPNNYQNVEYCGEL--KGDPTMSWNDINCEHLNNWICQI 779
Cdd:cd03589   74 -HDRTSEGpFEWTDGSPVDFTKWAGGQPDNYGGNEDCVQMwrRGDAGQSWNDMPCDAVFPYICKM 137

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: 84.96 E-value: 3.67e-19

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046    1097 DGFVKYGKSSYSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAFAW--LQMETSNERVWIALNSNLTDNQYTWTDKW-R 1173
Cdd:smart00034    3 SGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGSgP 82

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 55666046    1174 VRYTNWAADEPKLKSA-CVYLDLD-GYWKTAHCNESFYFLCK 1213
Cdd:smart00034   83 VSYSNWAPGEPNNSSGdCVVLSTSgGKWNDVSCTSKLPFVCE 124

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: 81.97 E-value: 4.01e-19

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 55666046  162 NANGATCAFPFKFENKWYADCTSAGRSDGWLWCGTTTDYDTDKLFGYC 209
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48

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: 84.28 E-value: 6.57e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  945 CKEGWNFYSNKCFkifgFMEEERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMkDSTFSAWTGLNDVNSEHTFLWTD 1024
Cdd:cd03590    1 CPTNWKSFQSSCY----FFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKIL-SGNRSYWIGLSDEETEGEWKWVD 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 55666046 1025 GRGVH--YTNWGKGYPggrrSSLSYEDADCVVIIGgasnEAGKWMDDTCDSKRGYICQT 1081
Cdd:cd03590   76 GTPLNssKTFWHPGEP----NNWGGGGEDCAELVY----DSGGWNDVPCNLEYRWICEK 126

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 82.91 E-value: 9.94e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046    524 TFAEANQTCNNENAYLTTIEDRYEQAFLTSFVGLRPeKYFWTGLSDIQTKGTFQWTIEEEVRFTHW--NSDMPGRKPGCV 601
Cdd:pfam00059    3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSN-KYFWIGLTDRKNEGTWKWVDGSPVNYTNWapEPNNNGENEDCV 81

                           90       100
                   ....*....|....*....|....*.
gi 55666046    602 AMRtgIAGGLWDVLKCDEKAKFVCKH 627
Cdd:pfam00059   82 ELS--SSSGKWNDENCNSKNPFVCEK 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: 82.53 E-value: 1.26e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046    818 KETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDaqSAYFIGLL-ISLDKKFAWMDGSKVDYVSWAtGEPNFANED 896
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSN--KYFWIGLTdRKNEGTWKWVDGSPVNYTNWA-PEPNNNGEN 77

                           90       100
                   ....*....|....*....|....*...
gi 55666046    897 ENCVTMYSNSGFWNDINCGYPNAFICQR 924
Cdd:pfam00059   78 EDCVELSSSSGKWNDENCNSKNPFVCEK 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: 82.14 E-value: 1.53e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046    237 ALTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSGLWIGLNSLSFNSGWQWSDRSPFRYLNWLPGSPSAEPGKSC 316
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGENEDC 80

                           90       100
                   ....*....|....*....|....*.
gi 55666046    317 VSLNPgKNAKWENLECVQKLGYICKK 342
Cdd:pfam00059   81 VELSS-SSGKWNDENCNSKNPFVCEK 105

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: 82.28 E-value: 2.13e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1107 YSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAFAWLQM-ETSNERVWIALNSNLTDNQYTWTDKWR-VRYTNWAADEP 1184
Cdd:cd00037    3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPGEP 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 55666046 1185 KLKSA--CVYLDL--DGYWKTAHCNESFYFLCKR 1214
Cdd:cd00037   83 NPGGSedCVVLSSssDGKWNDVSCSSKLPFICEK 116

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: 81.96 E-value: 3.03e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  812 YYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNrnDAQSAYFIGLlISLDK--KFAWMDGSKVDYVSWATGE 889
Cdd:cd03591    4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVK--KGNTYAFIGI-TDLETegQFVYLDGGPLTYTNWKPGE 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 55666046  890 PNFANEDENCVTMYSnSGFWNDINCGYPNAFICQ 923
Cdd:cd03591   81 PNNAGGGEDCVEMYT-SGKWNDVACNLTRLFVCE 113

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: 81.85 E-value: 3.54e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  945 CKEGWNFYSNKCFKIFgfmeEERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTfsaWTGLNDVNSEHTFLWTD 1024
Cdd:cd03588    1 CEEGWDKFQGHCYRHF----PDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ---WIGLNDRTIEGDFRWSD 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 55666046 1025 GRGVHYTNWGKGYPggrrSSLSYEDADCVVIIGgasNEAGKWMDDTCDSKRGYICQ 1080
Cdd:cd03588   74 GHPLQFENWRPNQP----DNFFATGEDCVVMIW---HEEGEWNDVPCNYHLPFTCK 122

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: 81.65 E-value: 4.52e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1238 WIPFHGHCY-YIesSYTRNWGQASLECLRMGSS--LVSIESAAESSFL-SYRVEPLKSKTNFWIGLFRNVEG-TWLWINN 1312
Cdd:cd03594    5 WLPYKGNCYgYF--RQPLSWSDAELFCQKYGPGahLASIHSPAEAAAIaSLISSYQKAYQPVWIGLHDPQQSrGWEWSDG 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 55666046 1313 SPVSFVNWNTGDPSGERNDCVALHASSGF--WSNIHCSSYKGYICK 1356
Cdd:cd03594   83 SKLDYRSWDRNPPYARGGYCAELSRSTGFlkWNDANCEERNPFICK 128

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: 82.02 E-value: 5.22e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  804 WVIYKDYQYYFSKEKETMDNARAFCK-----RNFGDLVSIQSESEKKF---LWKYVNRNDAQSAYFIGLLislDKK---- 871
Cdd:cd03589    5 WTAFGGYCYRFFGDRLTWEEAELRCRsfsipGLIAHLVSIHSQEENDFvydLFESSRGPDTPYGLWIGLH---DRTsegp 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55666046  872 FAWMDGSKVDYVSWATGEPNFANEDENCVTMYSNS---GFWNDINCGYPNAFIC 922
Cdd:cd03589   82 FEWTDGSPVDFTKWAGGQPDNYGGNEDCVQMWRRGdagQSWNDMPCDAVFPYIC 135

Fibronectin type II domain;

Pssm-ID: 459645 Cd Length: 42 Bit Score: 77.22 E-value: 1.73e-17

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 55666046    168 CAFPFKFENKWYADCTSAGRSDGWLWCGTTTDYDTDKLFGYC 209
Cdd:pfam00040    1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42

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: 79.26 E-value: 1.99e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  668 HEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYhklFWLGLTyGSPSEG-FTWSDGSPVSYENWAYGEPNN 746
Cdd:cd03591    8 GEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTY---AFIGIT-DLETEGqFVYLDGGPLTYTNWKPGEPNN 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 55666046  747 YQNVEYCGELKGDPTmsWNDINCEHLNNWICQI 779
Cdd:cd03591   84 AGGGEDCVEMYTSGK--WNDVACNLTRLFVCEF 114

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

Pssm-ID: 153061 [Multi-domain] Cd Length: 114 Bit Score: 78.11 E-value: 6.15e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  966 ERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFSAWTGLNDVNSEHTFLWTDGRGVHYTNWGKGYPGGRrssl 1045
Cdd:cd03591    9 EEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPNNA---- 84

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 55666046 1046 sYEDADCVVIIGGasneaGKWMDDTCDSKRGYICQ 1080
Cdd:cd03591   85 -GGGEDCVEMYTS-----GKWNDVACNLTRLFVCE 113

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: 77.76 E-value: 8.17e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1230 CPESdhtaWIPFHGHCYYIeSSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEPLksktNFWIGL-FRNVEGTWL 1308
Cdd:cd03593    1 CPKD----WICYGNKCYYF-SMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSS----SYWIGLsREKSEKPWK 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 55666046 1309 WINNSPVSfvNWNTGDPSGERNDCVALHaSSGFwSNIHCSSYKGYICKR 1357
Cdd:cd03593   72 WIDGSPLN--NLFNIRGSTKSGNCAYLS-STGI-YSEDCSTKKRWICEK 116

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: 77.80 E-value: 1.27e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  646 CPEDWgaSSRTSLCFKLYAKgkheKKTWFESRDFCRAL--GGDLASINNKEEQQTIWRLITASGSYHKLFWLGLTYGSPS 723
Cdd:cd03594    1 CPKGW--LPYKGNCYGYFRQ----PLSWSDAELFCQKYgpGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQS 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 55666046  724 EGFTWSDGSPVSYENWAYGEPnnYQNVEYCGELKgDPT--MSWNDINCEHLNNWICQ 778
Cdd:cd03594   75 RGWEWSDGSKLDYRSWDRNPP--YARGGYCAELS-RSTgfLKWNDANCEERNPFICK 128

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: 75.87 E-value: 3.15e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  812 YYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDAqSAYFIGLlisLDKKFAWM----DGSKVDYVSWAT 887
Cdd:cd03592    3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNL-GYYWIDG---NDINNEGTwvdtDKKELEYKNWAP 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 55666046  888 GEPNfANEDENCVTMYSN-SGFWNDINCGYPNAFICQR 924
Cdd:cd03592   79 GEPN-NGRNENCLEIYIKdNGKWNDEPCSKKKSAICYT 115

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

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 76.01 E-value: 3.82e-16

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046      27 IYNEDHKRCVDAVSPSA-VQTAACNQDAESQKFRWVSESQIMSVAFKLCLGVPSKTDWVaITLYACDSKSEFQKWECKND 105
Cdd:smart00458    1 IISGNTGKCLDVNGNKNpVGLFDCHGTGGNQLWKLTSDGAIRIKDTDLCLTANGNTGST-VTLYSCDGTNDNQYWEVNKD 79

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 55666046     106 TLLGIKGEDLFFN-YGNRQEKNIMLYKGSG-LWSRWKIY 142
Cdd:smart00458   80 GTIRNPDSGKCLDvKDGNTGTKVILWTCSGnPNQKWIFE 118

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

Pssm-ID: 459655 [Multi-domain] Cd Length: 105 Bit Score: 74.82 E-value: 5.86e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   1116 WHEAETYCKLHNSLIASILDPYSNAFAWLQMETSNERVWIALNSNLTDNQYTWTDKWRVRYTNWAA--DEPKLKSACVYL 1193
Cdd:pfam00059    4 WDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPepNNNGENEDCVEL 83

                           90       100
                   ....*....|....*....|..
gi 55666046   1194 DL-DGYWKTAHCNESFYFLCKR 1214
Cdd:pfam00059   84 SSsSGKWNDENCNSKNPFVCEK 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: 71.98 E-value: 7.47e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  945 CKEGWNFYSNKCFKIFgfmeEERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFsaWTGLNDVNSEHTFLWTD 1024
Cdd:cd03593    1 CPKDWICYGNKCYYFS----MEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY--WIGLSREKSEKPWKWID 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 55666046 1025 GRgvHYTNWGKgypggrrSSLSYEDADCVVIiggasnEAGKWMDDTCDSKRGYICQ 1080
Cdd:cd03593   75 GS--PLNNLFN-------IRGSTKSGNCAYL------SSTGIYSEDCSTKKRWICE 115

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: 72.04 E-value: 1.09e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  954 NKCFKIFgfmeEERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFSA---WTGLNDVNSEHTFLWTDGRGVHY 1030
Cdd:cd03596    9 KKCYLVS----EETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGNwevWLGINDMVAEGKWVDVNGSPISY 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55666046 1031 TNWGKGYP----GGRRSSlsyedadCVVIiggASNEAGKWMDDTCDSKRGYICQ 1080
Cdd:cd03596   85 FNWEREITaqpdGGKREN-------CVAL---SSSAQGKWFDEDCRREKPYVCE 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: 71.21 E-value: 1.86e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  646 CPEDWGASSRTSLCFKlyakgkHEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLItasgsYHKLFWLGLTYGSPSEG 725
Cdd:cd03593    1 CPKDWICYGNKCYYFS------MEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQI-----GSSSYWIGLSREKSEKP 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55666046  726 FTWSDGSPVSyeNWayGEPNNYQNVEYCGELKGDPTMSwndINCEHLNNWICQ 778
Cdd:cd03593   70 WKWIDGSPLN--NL--FNIRGSTKSGNCAYLSSTGIYS---EDCSTKKRWICE 115

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: 69.63 E-value: 6.20e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  379 DEKKIQRDALTTCRKEGSDLASIHTIEE----FDFIISQLGYepndeLWIGLNDIKIQMYFEWSDGTPVTFTKWLRGEPs 454
Cdd:cd03591    8 GEEKNFDDAQKLCSEAGGTLAMPRNAAEnaaiASYVKKGNTY-----AFIGITDLETEGQFVYLDGGPLTYTNWKPGEP- 81

                         90       100
                 ....*....|....*....|....*.
gi 55666046  455 heNNR--QEDCVVMKgKDGYWADRGC 478
Cdd:cd03591   82 --NNAggGEDCVEMY-TSGKWNDVAC 104

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: 70.69 E-value: 6.47e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  659 CFKL-YAKGKHEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYHKLFWLGL--------TYGSPSEGFTWS 729
Cdd:cd03595   12 CYKIaYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGDFWIGLrrssqynvTSSACSSLYYWL 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 55666046  730 DGSPVSYENWAYGEPNNyqNVEYCGELKGDPTMS----------WNDINCEHLNNWICQ 778
Cdd:cd03595   92 DGSISTFRNWYVDEPSC--GSEVCVVMYHQPSAPagqggpylfqWNDDNCNMKNNFICK 148

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: 69.14 E-value: 9.76e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  646 CPEDWGASSrtSLCFKLYakgkHEKKTWFESRDFCRALGGDLASINNKEEQQTIwrlitaSGSYHKLFWLGLTYGSPSEG 725
Cdd:cd03588    1 CEEGWDKFQ--GHCYRHF----PDRETWEDAERRCREQQGHLSSIVTPEEQEFV------NNNAQDYQWIGLNDRTIEGD 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55666046  726 FTWSDGSPVSYENWAYGEPNNY-QNVEYCGELKGDPTMSWNDINCEHLNNWICQ 778
Cdd:cd03588   69 FRWSDGHPLQFENWRPNQPDNFfATGEDCVVMIWHEEGEWNDVPCNYHLPFTCK 122

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: 68.94 E-value: 1.31e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  803 GWVIYKDYQY-YFSKEKeTMDNARAFCKRNF--GDLVSIQSESEKKFLWKYVNrnDAQSAY---FIGLL-ISLDKKFAWM 875
Cdd:cd03594    4 GWLPYKGNCYgYFRQPL-SWSDAELFCQKYGpgAHLASIHSPAEAAAIASLIS--SYQKAYqpvWIGLHdPQQSRGWEWS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 55666046  876 DGSKVDYVSWATGEPnfANEDENCVTMYSNSGF--WNDINCGYPNAFICQ 923
Cdd:cd03594   81 DGSKLDYRSWDRNPP--YARGGYCAELSRSTGFlkWNDANCEERNPFICK 128

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: 67.40 E-value: 3.24e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  668 HEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITA-SGSYHklfWLGLTygSPSEGFTW--SDGSPVSYENWAYGEP 744
Cdd:cd03592    7 TEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKyNLGYY---WIDGN--DINNEGTWvdTDKKELEYKNWAPGEP 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 55666046  745 NNYQNvEYCGELKGDPTMSWNDINCEHLNNWICQ 778
Cdd:cd03592   82 NNGRN-ENCLEIYIKDNGKWNDEPCSKKKSAICY 114

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: 67.60 E-value: 3.38e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  801 EDGWVIYKDYQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFlwkyVNRNdAQSAYFIGLL-ISLDKKFAWMDGSK 879
Cdd:cd03588    2 EEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEF----VNNN-AQDYQWIGLNdRTIEGDFRWSDGHP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 55666046  880 VDYVSWATGEP-NFANEDENCVTM-YSNSGFWNDINCGYPNAFICQR 924
Cdd:cd03588   77 LQFENWRPNQPdNFFATGEDCVVMiWHEEGEWNDVPCNYHLPFTCKK 123

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: 67.02 E-value: 4.29e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  966 ERKNWQEARKACIGFGGNLVSIQNEKEQAFLtyHMKDSTFSA---WTGLNDVNSEHTFLWTDGRGVHYTNWGKGYPGGRR 1042
Cdd:cd03592    8 EKMTFNEAVKYCKSRGTDLVAIQNAEENALL--NGFALKYNLgyyWIDGNDINNEGTWVDTDKKELEYKNWAPGEPNNGR 85

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 55666046 1043 SSlsyedaDCVVIiggASNEAGKWMDDTCDSKRGYICQT 1081
Cdd:cd03592   86 NE------NCLEI---YIKDNGKWNDEPCSKKKSAICYT 115

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: 66.32 E-value: 8.99e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  812 YYFSKEKETMDNARAFCKRNF-GDLVSIQSESEKKFLWKYVnRNDAQSAYFIGLLISLD---KKFAWMDGSKVDYVSWAT 887
Cdd:cd03598    4 YRFVKSPRTFRDAQVICRRCYrGNLASIHSFAFNYRVQRLV-STLNQAQVWIGGIITGKgrcRRFSWVDGSVWNYAYWAP 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 55666046  888 GEPnfANEDENCVTMYSNSGFWNDINCGYPNAFICQ 923
Cdd:cd03598   83 GQP--GNRRGHCVELCTRGGHWRRAHCKLRRPFICS 116

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: 66.63 E-value: 9.28e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  945 CKEGWNFYSNKCFKIFGfmeeERKNWQEARKAC--IGFGGNLVSIQNEKEQAFLTYHMKDSTFS---AWTGLNDVNSEHT 1019
Cdd:cd03594    1 CPKGWLPYKGNCYGYFR----QPLSWSDAELFCqkYGPGAHLASIHSPAEAAAIASLISSYQKAyqpVWIGLHDPQQSRG 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55666046 1020 FLWTDGRGVHYTNWGKGYPGGRRSSlsyedadCVVIigGASNEAGKWMDDTCDSKRGYICQ 1080
Cdd:cd03594   77 WEWSDGSKLDYRSWDRNPPYARGGY-------CAEL--SRSTGFLKWNDANCEERNPFICK 128

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: 67.00 E-value: 9.29e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1230 CPesdhTAWIPFHGHCY-YIESSYTrnWGQASLECLRMGSS-----LVSIESAAESSFLSYRVEPLKSK---TNFWIGLF 1300
Cdd:cd03589    1 CP----TFWTAFGGYCYrFFGDRLT--WEEAELRCRSFSIPgliahLVSIHSQEENDFVYDLFESSRGPdtpYGLWIGLH 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55666046 1301 -RNVEGTWLWINNSPVSFVNWNTGDPS--GERNDCVAL---HASSGFWSNIHCSSYKGYICK 1356
Cdd:cd03589   75 dRTSEGPFEWTDGSPVDFTKWAGGQPDnyGGNEDCVQMwrrGDAGQSWNDMPCDAVFPYICK 136

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: 65.87 E-value: 1.47e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  504 CRKGWKKHHfYCYMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFV--GLRPEKYFWTGLSDIQTKGTFQWTIE 581
Cdd:cd03596    1 CLKGTKIHK-KCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVkaSVPGNWEVWLGINDMVAEGKWVDVNG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 55666046  582 EEVRFTHWNSDMP-----GRKPGCVAMRTGIAGGLWDVlKCDEKAKFVC 625
Cdd:cd03596   80 SPISYFNWEREITaqpdgGKRENCVALSSSAQGKWFDE-DCRREKPYVC 127

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: 66.45 E-value: 1.69e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  807 YKDYQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDAQSAYF-IGLLISLDK---------KFAWMD 876
Cdd:cd03595   13 YKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGDFwIGLRRSSQYnvtssacssLYYWLD 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 55666046  877 GSKVDYVSWATGEPNFANedENCVTMY----SNSGF-------WNDINCGYPNAFICQ 923
Cdd:cd03595   93 GSISTFRNWYVDEPSCGS--EVCVVMYhqpsAPAGQggpylfqWNDDNCNMKNNFICK 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: 65.79 E-value: 1.86e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  504 CRKGWKKHHFYCYMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFvgLRPEKYFWTGLSDIQTKGTFQW----T 579
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKI--LSGNRSYWIGLSDEETEGEWKWvdgtP 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55666046  580 IEEEVRFthWNSDMP--GRKPG--CVAMRTgiAGGLWDVLKCDEKAKFVCK 626
Cdd:cd03590   79 LNSSKTF--WHPGEPnnWGGGGedCAELVY--DSGGWNDVPCNLEYRWICE 125

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: 65.09 E-value: 2.15e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1247 YIESSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEPLKSKTnFWIGLF-RNVEGTWLWINNSPVSFVNWNTGDP 1325
Cdd:cd03592    3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGY-YWIDGNdINNEGTWVDTDKKELEYKNWAPGEP 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 55666046 1326 SGERN-DCVALH-ASSGFWSNIHCSSYKGYICKR 1357
Cdd:cd03592   82 NNGRNeNCLEIYiKDNGKWNDEPCSKKKSAICYT 115

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: 65.05 E-value: 2.17e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  803 GWVIYKDYQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDaqsaYFIGLLISLDKK-FAWMDGSKVD 881
Cdd:cd03593    4 DWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSS----YWIGLSREKSEKpWKWIDGSPLN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 55666046  882 YvswaTGEPNFANEDENCVTmYSNSGFwNDINCGYPNAFICQR 924
Cdd:cd03593   80 N----LFNIRGSTKSGNCAY-LSSTGI-YSEDCSTKKRWICEK 116

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: 64.70 E-value: 2.46e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  669 EKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYhklFWLGLTYGspSEGFTWSDGSPVSYENWAygePNNYQ 748
Cdd:cd03602    8 ESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSA---AWIGLYRD--VDSWRWSDGSESSFRNWN---TFQPF 79

                         90       100
                 ....*....|....*....|....*....
gi 55666046  749 NVEYCGELKGDPtmSWNDINCEHLNNWIC 777
Cdd:cd03602   80 GQGDCATMYSSG--RWYAALCSALKPFIC 106

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: 63.98 E-value: 6.30e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  965 EERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFSaWTGLNDVNSEHTFLWTDGRGVHYTNWGKGYPGGrrSS 1044
Cdd:cd03603    7 DGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGAS-WIGASDAATEGTWKWSDGEESTYTNWGSGEPHN--NG 83

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 55666046 1045 LSYEDadcVVIIGGASNEAGKWMDDTCDS-KRGYI 1078
Cdd:cd03603   84 GGNED---YAAINHFPGISGKWNDLANSYnTLGYV 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: 64.14 E-value: 6.38e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  239 TWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTsglWIGLNSLSFNSGWQWSDRSPFRYLNWLPGSPSA--EPGKSC 316
Cdd:cd03588   21 TWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ---WIGLNDRTIEGDFRWSDGHPLQFENWRPNQPDNffATGEDC 97

                         90       100
                 ....*....|....*....|....*..
gi 55666046  317 VSLNPGKNAKWENLECVQKLGYICKKG 343
Cdd:cd03588   98 VVMIWHEEGEWNDVPCNYHLPFTCKKG 124

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: 63.55 E-value: 7.04e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  234 SKSALTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSGL-WIGLNSLsfNSGWQW--SDRSPFRYLNWLPGSPSA 310
Cdd:cd03592    6 STEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYyWIDGNDI--NNEGTWvdTDKKELEYKNWAPGEPNN 83

                         90       100       110
                 ....*....|....*....|....*....|
gi 55666046  311 EPGKSCVSLNPGKNAKWENLECVQKLGYIC 340
Cdd:cd03592   84 GRNENCLEIYIKDNGKWNDEPCSKKKSAIC 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: 63.16 E-value: 8.54e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  379 DEKKIQRDALTTCRKEGSDLASIHTIEEFDfIISQLGYEPNDELWIGLndIKIQMYFEWSDGTPVTFTKWLRGEPShenn 458
Cdd:cd03602    7 NESKTWSEAQQYCRENYTDLATVQNQEDNA-LLSNLSRVSNSAAWIGL--YRDVDSWRWSDGSESSFRNWNTFQPF---- 79

                         90       100
                 ....*....|....*....|....*...
gi 55666046  459 RQEDCVVMkGKDGYWADRGCEWPLGYIC 486
Cdd:cd03602   80 GQGDCATM-YSSGRWYAALCSALKPFIC 106

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: 63.92 E-value: 8.76e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  504 CRKGWKKHHFYCYMIGHTLSTFAEANQTCNN-----ENAYLTTIEDRYEQAFLT----SFVGLRPEKYFWTGLSDIQTKG 574
Cdd:cd03589    1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYdlfeSSRGPDTPYGLWIGLHDRTSEG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 55666046  575 TFQWTIEEEVRFTHWNSDMPGRKPG---CVAM-RTGIAGGLWDVLKCDEKAKFVCKH 627
Cdd:cd03589   81 PFEWTDGSPVDFTKWAGGQPDNYGGnedCVQMwRRGDAGQSWNDMPCDAVFPYICKM 137

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: 63.56 E-value: 1.18e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1242 HGHCYYIeSSYTRNWGQASLECLRMGSSLVSIESAAESSFLS-YRVEPLKSKTNFWIGLFRNV-EGTWLWINNSPVSFVN 1319
Cdd:cd03596    8 HKKCYLV-SEETKHYHEASEDCIARGGTLATPRDSDENDALRdYVKASVPGNWEVWLGINDMVaEGKWVDVNGSPISYFN 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 55666046 1320 WNTGDPS----GERNDCVALHASS-GFWSNIHCSSYKGYIC 1355
Cdd:cd03596   87 WEREITAqpdgGKRENCVALSSSAqGKWFDEDCRREKPYVC 127

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: 63.16 E-value: 1.41e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  238 LTWHQARKSCQQ--QNAELLSITEIHEQTYLTGLTSSL---TSGLWIGLNSLSFNSGWQWSDRSPFRYLNWlPGSPSAEP 312
Cdd:cd03594   20 LSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISSYqkaYQPVWIGLHDPQQSRGWEWSDGSKLDYRSW-DRNPPYAR 98

                         90       100       110
                 ....*....|....*....|....*....|
gi 55666046  313 GKSCVSLNPGKN-AKWENLECVQKLGYICK 341
Cdd:cd03594   99 GGYCAELSRSTGfLKWNDANCEERNPFICK 128

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: 62.01 E-value: 2.17e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  810 YQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDaqSAYFIGLLISLDkKFAWMDGSKVDYVSWATGE 889
Cdd:cd03602    1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSN--SAAWIGLYRDVD-SWRWSDGSESSFRNWNTFQ 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 55666046  890 PnFANEDenCVTMYSNsGFWNDINCGYPNAFIC 922
Cdd:cd03602   78 P-FGQGD--CATMYSS-GRWYAALCSALKPFIC 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: 62.99 E-value: 2.63e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1246 YYIESSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEPLK-SKTNFWIGLFRNVEGT---------WLWINNSPV 1315
Cdd:cd03595   17 YFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRaSDGDFWIGLRRSSQYNvtssacsslYYWLDGSIS 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 55666046 1316 SFVNWNTGDPSGERNDCVALH----ASSGF-------WSNIHCSSYKGYICK 1356
Cdd:cd03595   97 TFRNWYVDEPSCGSEVCVVMYhqpsAPAGQggpylfqWNDDNCNMKNNFICK 148

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: 61.62 E-value: 2.74e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1247 YIESSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEplKSKTNFWIGLFRNVeGTWLWINNSPVSFVNWNTGDPS 1326
Cdd:cd03602    3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSR--VSNSAAWIGLYRDV-DSWRWSDGSESSFRNWNTFQPF 79

                         90       100
                 ....*....|....*....|....*....
gi 55666046 1327 GeRNDCVALhASSGFWSNIHCSSYKGYIC 1355
Cdd:cd03602   80 G-QGDCATM-YSSGRWYAALCSALKPFIC 106

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

Pssm-ID: 153068 Cd Length: 117 Bit Score: 61.70 E-value: 3.60e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  385 RDALTTCRK-EGSDLASIHTiEEFDFIISQLGYEPND-ELWIG--LNDIKIQMYFEWSDGTPVTFTKWLRGEPShenNRQ 460
Cdd:cd03598   14 RDAQVICRRcYRGNLASIHS-FAFNYRVQRLVSTLNQaQVWIGgiITGKGRCRRFSWVDGSVWNYAYWAPGQPG---NRR 89

                         90       100
                 ....*....|....*....|....*.
gi 55666046  461 EDCVVMKGKDGYWADRGCEWPLGYIC 486
Cdd:cd03598   90 GHCVELCTRGGHWRRAHCKLRRPFIC 115

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: 61.73 E-value: 3.82e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   25 FLIYNEDHKRCVdAVSPSAVQ-TAACNQDAESQKFRWVSESQIMSVAFKLCLGVP---SKTDWVAITLYACDSKSEFQKW 100
Cdd:cd23408    3 FLIYSDGAQGCL-EVRDSVVRlSPACNTSSPAQQWKWVSRNRLFNLGSMQCLGVSgpnGSGTSATLGTYECDRESVNMRW 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 55666046  101 ECKNdtllgiKGEDLFFNYGNRQekniMLYKGSGLW-------SRWKIYGTTD 146
Cdd:cd23408   82 HCRT------LGEQLSQHLGART----ANGNPSTLErgdqarsSQWRIYGSEQ 124

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: 62.21 E-value: 4.83e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  945 CKEGwnfYSNKCFKIFGFMEEERK-NWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFSA---WTGL--------N 1012
Cdd:cd03595    4 CRRG---TEKPCYKIAYFQDSRRRlNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDgdfWIGLrrssqynvT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55666046 1013 DVNSEHTFLWTDGRGVHYTNWGKGYPggrrsSLSYEdaDCVVIIGGASNEAG-------KWMDDTCDSKRGYICQ 1080
Cdd:cd03595   81 SSACSSLYYWLDGSISTFRNWYVDEP-----SCGSE--VCVVMYHQPSAPAGqggpylfQWNDDNCNMKNNFICK 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: 60.01 E-value: 1.78e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  234 SKSALTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSgLWIGLNSLSFNSGWQWSDRSPFR--YLNWLPGSPS-- 309
Cdd:cd03590   16 STEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS-YWIGLSDEETEGEWKWVDGTPLNssKTFWHPGEPNnw 94

                         90       100       110
                 ....*....|....*....|....*....|...
gi 55666046  310 AEPGKSCVSLNPGKNAkWENLECVQKLGYICKK 342
Cdd:cd03590   95 GGGGEDCAELVYDSGG-WNDVPCNLEYRWICEK 126

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: 1.80e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  362 CPSQWWPYAGHCYKIHRDEKKIQrDALTTCRKEGSDLASIHTIEEFDFIISQLGyepNDELWIGLNDIKIQMYFEWSDGT 441
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWN-ESKEACSSKNSSLLKIDDEEELEFLQSQIG---SSSYWIGLSREKSEKPWKWIDGS 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 55666046  442 PvtFTKWLRgepSHENNRQEDCVVMKGKDGYWADrgCEWPLGYICK 487
Cdd:cd03593   77 P--LNNLFN---IRGSTKSGNCAYLSSTGIYSED--CSTKKRWICE 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: 59.90 E-value: 1.95e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  504 CRKGWKKHHFYCYMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSfvglRPEKYFWTGLSDIQTKGTFQWTIEEE 583
Cdd:cd03588    1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNN----NAQDYQWIGLNDRTIEGDFRWSDGHP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 55666046  584 VRFTHWNSDMPGR----KPGCVAMrTGIAGGLWDVLKCDEKAKFVCK 626
Cdd:cd03588   77 LQFENWRPNQPDNffatGEDCVVM-IWHEEGEWNDVPCNYHLPFTCK 122

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: 58.93 E-value: 2.85e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  379 DEKKIQRDALTTCRKEGSDLASIHTIEEFDFIISQLGYEPNDELWIGLNDIKIQMYFEWSDGTPVTFTKWLRGEPSheNN 458
Cdd:cd03592    7 TEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYYWIDGNDINNEGTWVDTDKKELEYKNWAPGEPN--NG 84

                         90       100
                 ....*....|....*....|....*....
gi 55666046  459 RQEDCVVM-KGKDGYWADRGCEWPLGYIC 486
Cdd:cd03592   85 RNENCLEIyIKDNGKWNDEPCSKKKSAIC 113

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: 58.98 E-value: 2.94e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1246 YYIESSYTRNWGQASLECLRMGSSLVSIESAAESSFLsyrVEPLKSKTNFWIGLFR-NVEGTWLWINNSPVSFVNWNTGD 1324
Cdd:cd03603    2 FYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWL---LSNFGGYGASWIGASDaATEGTWKWSDGEESTYTNWGSGE 78

                         90       100
                 ....*....|....*....|....*.
gi 55666046 1325 PSGERN---DCVALHA---SSGFWSN 1344
Cdd:cd03603   79 PHNNGGgneDYAAINHfpgISGKWND 104

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: 58.54 E-value: 3.47e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1116 WHEAETYCKLHNSLIASILDPYSNAFAWLQMETSNERVWIALnSNLTDNqYTWTDKWRVRYTNWAADEPKLKSACVYLDL 1195
Cdd:cd03602   12 WSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGL-YRDVDS-WRWSDGSESSFRNWNTFQPFGQGDCATMYS 89

                         90
                 ....*....|....*..
gi 55666046 1196 DGYWKTAHCNESFYFLC 1212
Cdd:cd03602   90 SGRWYAALCSALKPFIC 106

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: 58.59 E-value: 4.30e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  668 HEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSyhklFWLGLTYGSPSEGFTWSDGSPVSYENWAYGEPNNY 747
Cdd:cd03603    7 DGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGA----SWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNN 82


                 ....*
gi 55666046  748 QNVEY 752
Cdd:cd03603   83 GGGNE 87

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: 58.52 E-value: 6.84e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  238 LTWHQARKSCQQ-----QNAELLSITEIHEQTYLTGLTSSL-----TSGLWIGLNSLSFNSGWQWSDRSPFRYLNWLPGS 307
Cdd:cd03589   20 LTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDLFESSrgpdtPYGLWIGLHDRTSEGPFEWTDGSPVDFTKWAGGQ 99

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 55666046  308 PSAEPG-KSCVSLNPGKNA--KWENLECVQKLGYICK 341
Cdd:cd03589  100 PDNYGGnEDCVQMWRRGDAgqSWNDMPCDAVFPYICK 136

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: 57.97 E-value: 8.19e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1238 WIPFHGHCYYiESSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEPLKsktnfWIGLF-RNVEGTWLWINNSPVS 1316
Cdd:cd03588    5 WDKFQGHCYR-HFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ-----WIGLNdRTIEGDFRWSDGHPLQ 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 55666046 1317 FVNWNTGDP-----SGErnDCVAL-HASSGFWSNIHCSSYKGYICKR 1357
Cdd:cd03588   79 FENWRPNQPdnffaTGE--DCVVMiWHEEGEWNDVPCNYHLPFTCKK 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: 57.82 E-value: 9.34e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  372 HCYKIhRDEKKIQRDALTTCRKEGSDLASIHTIEEFDFIISQLGYepNDELWIGLNDIKIQMYFEWSDGTPVTFTKWLRG 451
Cdd:cd03603    1 HFYKF-VDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGG--YGASWIGASDAATEGTWKWSDGEESTYTNWGSG 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 55666046  452 EPSHENNRQEDCVVM---KGKDGYWADRG-CEWPLGYI 485
Cdd:cd03603   78 EPHNNGGGNEDYAAInhfPGISGKWNDLAnSYNTLGYV 115

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: 56.15 E-value: 3.29e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1107 YSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAFAWLQMETSNERVWIALNSNLTDNQYTWTDKWRVRYTNWAADEP-- 1184
Cdd:cd03591    4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPnn 83

                         90       100
                 ....*....|....*....|....*....
gi 55666046 1185 -KLKSACVYLDLDGYWKTAHCNESFYFLC 1212
Cdd:cd03591   84 aGGGEDCVEMYTSGKWNDVACNLTRLFVC 112

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

Pssm-ID: 153071 Cd Length: 119 Bit Score: 55.62 E-value: 5.49e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  810 YQYYFSKEKETMDNARAFCKRNFGDLVSIQ---SESEKKFLWKYVNRNdaqSAYFIGLLISLDKK--FAWMDGSKV--DY 882
Cdd:cd03601    1 YEILCSDETMNYAKAGAFCRSRGMRLASLAmrdSEMRDAILAFTLVKG---HGYWVGADNLQDGEydFLWNDGVSLptDS 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 55666046  883 VSWATGEPNFANEDENCVTMYSNSGFWNDINCGYPNAFICQ 923
Cdd:cd03601   78 DLWAPNEPSNPQSRQLCVQLWSKYNLLDDEYCGRAKRVICE 118

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: 55.46 E-value: 6.65e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  504 CRKGWKKHHFYCYMIGHTLSTFAEANQTCNN--ENAYLTTIEDRYEQAFLTSFVG--LRPEKYFWTGLSDIQTKGTFQWT 579
Cdd:cd03594    1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKygPGAHLASIHSPAEAAAIASLISsyQKAYQPVWIGLHDPQQSRGWEWS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 55666046  580 IEEEVRFTHWNSDMPGRKPG-CVAMRTGIAGGLWDVLKCDEKAKFVCK 626
Cdd:cd03594   81 DGSKLDYRSWDRNPPYARGGyCAELSRSTGFLKWNDANCEERNPFICK 128

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: 55.51 E-value: 8.19e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  659 CFKLYakgkHEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYHK----LFWLGL--------TYGSPSEGF 726
Cdd:cd03600    6 CYTLH----PQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGRHGrgslRLWIGLqreprqcsDPSLPLRGF 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  727 TW-SDGSPVSYENWAyGEPNNYQNVEYCGELKGDPTMS----WNDINCE-HLNNWICQIQ 780
Cdd:cd03600   82 SWvTGDQDTDFSNWL-QEPAGTCTSPRCVALSAAGSTPdnlkWKDGPCSaRADGYLCKFS 140

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: 55.07 E-value: 1.12e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1098 GFVKYGKSSYSLMRQKFQWHEAETYCKLH--NSLIASILDPYSNAF-AWL--QMETSNERVWIALNSNLTDNQYTWTDKW 1172
Cdd:cd03594    4 GWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAiASLisSYQKAYQPVWIGLHDPQQSRGWEWSDGS 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 55666046 1173 RVRYTNWAADEPKL-KSACVYL-DLDGY--WKTAHCNESFYFLCK 1213
Cdd:cd03594   84 KLDYRSWDRNPPYArGGYCAELsRSTGFlkWNDANCEERNPFICK 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: 54.65 E-value: 1.14e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  234 SKSALTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSglWIGLNSLSFNSGWQWSDRSPFRylNWLPGSPSAEPG 313
Cdd:cd03593   16 SMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY--WIGLSREKSEKPWKWIDGSPLN--NLFNIRGSTKSG 91

                         90       100
                 ....*....|....*....|....*....
gi 55666046  314 kSCVSLNpgkNAKWENLECVQKLGYICKK 342
Cdd:cd03593   92 -NCAYLS---STGIYSEDCSTKKRWICEK 116

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

Pssm-ID: 153071 Cd Length: 119 Bit Score: 54.08 E-value: 1.58e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  679 FCRALGGDLASINNK--EEQQTIwrLITASGSYHKlFWLGLTYGSPSEG-FTWSDGS--PVSYENWAYGEPNNYQNVEYC 753
Cdd:cd03601   18 FCRSRGMRLASLAMRdsEMRDAI--LAFTLVKGHG-YWVGADNLQDGEYdFLWNDGVslPTDSDLWAPNEPSNPQSRQLC 94

                         90       100
                 ....*....|....*....|....*.
gi 55666046  754 GELKGDPTMsWNDINCEHLNNWICQI 779
Cdd:cd03601   95 VQLWSKYNL-LDDEYCGRAKRVICEK 119

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: 53.15 E-value: 2.50e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  238 LTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSGLWIGLnsLSFNSGWQWSDRSPFRYLNWLPGSPSAepGKSCV 317
Cdd:cd03602   10 KTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGL--YRDVDSWRWSDGSESSFRNWNTFQPFG--QGDCA 85

                         90       100
                 ....*....|....*....|...
gi 55666046  318 SLNPgkNAKWENLECVQKLGYIC 340
Cdd:cd03602   86 TMYS--SGRWYAALCSALKPFIC 106

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 3 (Pgant3) and similar proteins; Pgant3, also called pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant3 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers EA2 as a substrate and has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Pgant3 plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. It may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Together with Pgant35A, Pgant3 regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles. Members of this subfamily contain a ricin B-type lectin domain at the C-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 bears a potential sugar binding site.

Pssm-ID: 467338 [Multi-domain] Cd Length: 121 Bit Score: 53.60 E-value: 2.63e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   24 QFLIYNED-----HKRCVDAVSPSAVQTAACNQDAESQkfRWV---SESQIMSVAFKLCLGVPSKTDWVaiTLYACDSKS 95
Cdd:cd23460   38 QFWMYTGDgqirqDHLCLTADEGNKVTLRECADQLPSQ--EWSydeKTGTIRHRSTGLCLTLDANNDVV--ILKECDSNS 113


                 ....*
gi 55666046   96 EFQKW 100
Cdd:cd23460  114 LWQKW 118

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: 53.93 E-value: 2.64e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  659 CFKLYakgkHEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYHKLFWLGLTyGSPSEGfTWSD--GSPVSY 736
Cdd:cd03596   11 CYLVS----EETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGNWEVWLGIN-DMVAEG-KWVDvnGSPISY 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 55666046  737 ENW---AYGEPNNYQNvEYCGELKGDPTMSWNDINCEHLNNWICQ 778
Cdd:cd03596   85 FNWereITAQPDGGKR-ENCVALSSSAQGKWFDEDCRREKPYVCE 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: 52.72 E-value: 4.50e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  504 CRKGWKKHHFYCYMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFVGlrpEKYFWTGLSDIQTKGTFQWTIEEE 583
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIG---SSSYWIGLSREKSEKPWKWIDGSP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 55666046  584 vrFTHW-NSDMPGRKPGCVAM-RTGIAGGlwdvlKCDEKAKFVCKH 627
Cdd:cd03593   78 --LNNLfNIRGSTKSGNCAYLsSTGIYSE-----DCSTKKRWICEK 116

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

Pssm-ID: 153071 Cd Length: 119 Bit Score: 52.92 E-value: 4.82e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  379 DEKKIQRDALTTCRKEGSDLASIHT--IEEFDFIISQLGYEpNDELWIGLNDIKIQMY-FEWSDGT--PVTFTKWLRGEP 453
Cdd:cd03601    7 DETMNYAKAGAFCRSRGMRLASLAMrdSEMRDAILAFTLVK-GHGYWVGADNLQDGEYdFLWNDGVslPTDSDLWAPNEP 85

                         90       100       110
                 ....*....|....*....|....*....|....
gi 55666046  454 SHENNRQeDCVVMKGKDGYWADRGCEWPLGYICK 487
Cdd:cd03601   86 SNPQSRQ-LCVQLWSKYNLLDDEYCGRAKRVICE 118

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.

Pssm-ID: 153072 Cd Length: 108 Bit Score: 52.38 E-value: 5.40e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  965 EERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFSAWTGLNDVNSEhtFLWTDGRGVHYTNWGKGYPGGrrss 1044
Cdd:cd03602    7 NESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLYRDVDS--WRWSDGSESSFRNWNTFQPFG---- 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 55666046 1045 lsyeDADCVVIiggasNEAGKWMDDTCDSKRGYIC 1079
Cdd:cd03602   81 ----QGDCATM-----YSSGRWYAALCSALKPFIC 106

ricin B-type lectin domain, beta-trefoil fold, found in uncharacterized macrophage mannose receptor (MRC)-like proteins; The subfamily corresponds to a group of uncharacterized ricin B-type lectin beta-trefoil domain-containing proteins from Gnathostomata. They show high sequence similarity with macrophage mannose receptor (MRC) family proteins.

Pssm-ID: 467790 Cd Length: 127 Bit Score: 52.41 E-value: 7.67e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   21 DTRQFLIYNEDHKRCVDAVSPSA--VQTAACNQDAESQKFRWVSESQ-IMSVAFKLCLGVPSKTDWVAITLYACDSKsEF 97
Cdd:cd23412    1 EVQGFMIRNVQLEKCIQVDHGESerVSLAECKPHSEHQQWSWDPETRaLSSLHTGECLTVLKIQEFGSVRLEPCGSR-EP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 55666046   98 QKWECKNDTLLGIKGEDLFFNyGNRQEKNIMLYKGSGLWSRWKI 141
Cdd:cd23412   80 QAWSCSKKGHLTLQGLGLHLS-ARHSSHKVFVSKEKGKFSKWKT 122

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: 52.39 E-value: 8.68e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  375 KIHR------DEKKIQRDALTTCRKEGSDLASIHTIEE----FDFIISQLGyePNDELWIGLNDIKIQMYFEWSDGTPVT 444
Cdd:cd03596    6 KIHKkcylvsEETKHYHEASEDCIARGGTLATPRDSDEndalRDYVKASVP--GNWEVWLGINDMVAEGKWVDVNGSPIS 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 55666046  445 FTKWLRGEPSHEN-NRQEDCVVMKG-KDGYWADRGCEWPLGYIC 486
Cdd:cd03596   84 YFNWEREITAQPDgGKRENCVALSSsAQGKWFDEDCRREKPYVC 127

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: 1.18e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1243 GHCYYIESSyTRNWGQASLECLRM-GSSLVSIESAAessfLSYRVEPLKSKTN---FWIGLFRNVEG---TWLWINNSPV 1315
Cdd:cd03598    1 GRCYRFVKS-PRTFRDAQVICRRCyRGNLASIHSFA----FNYRVQRLVSTLNqaqVWIGGIITGKGrcrRFSWVDGSVW 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 55666046 1316 SFVNWNTGDPSGERNDCVALHASSGFWSNIHCSSYKGYIC 1355
Cdd:cd03598   76 NYAYWAPGQPGNRRGHCVELCTRGGHWRRAHCKLRRPFIC 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: 51.42 E-value: 1.50e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1098 GFVKYGKSSYSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAFAwlqMETSNERVWIALNSNLTDNQYTWTDKWRVRYT 1177
Cdd:cd03588    4 GWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFV---NNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 55666046 1178 NWAADEPK----LKSACVYL--DLDGYWKTAHCNESFYFLCKR 1214
Cdd:cd03588   81 NWRPNQPDnffaTGEDCVVMiwHEEGEWNDVPCNYHLPFTCKK 123

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: 51.14 E-value: 1.71e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1246 YYIESSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEplKSKTNFWIGLF-RNVEGTWLWINNSPVSFVNWNTGD 1324
Cdd:cd03591    3 IFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVK--KGNTYAFIGITdLETEGQFVYLDGGPLTYTNWKPGE 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 55666046 1325 PSGERN--DCVALhASSGFWSNIHCSSYKGYIC 1355
Cdd:cd03591   81 PNNAGGgeDCVEM-YTSGKWNDVACNLTRLFVC 112

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: 51.59 E-value: 2.19e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1116 WHEAETYCKLH--NSLIA---SILDPYSNAFAWLQMETSN-----ERVWIALNSNLTDNQYTWTDKWRVRYTNWAADEP- 1184
Cdd:cd03589   22 WEEAELRCRSFsiPGLIAhlvSIHSQEENDFVYDLFESSRgpdtpYGLWIGLHDRTSEGPFEWTDGSPVDFTKWAGGQPd 101

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 55666046 1185 --KLKSACVYL----DLDGYWKTAHCNESFYFLCK 1213
Cdd:cd03589  102 nyGGNEDCVQMwrrgDAGQSWNDMPCDAVFPYICK 136

C-type lectin-like protein; Provisional

Pssm-ID: 165024 [Multi-domain] Cd Length: 216 Bit Score: 53.20 E-value: 2.30e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   928 SINATTVMPTMPSVPsgCKEGWNFYSNKCFkifgFMEEERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHmKDSTfSA 1007
Cdd:PHA02642   73 AFKSDTQEPTIKYVT--CPKGWIGFGYKCF----YFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRY-KDSS-DH 144

                          90
                  ....*....|....*..
gi 55666046  1008 WTGLNDVNSEHTFLWTD 1024
Cdd:PHA02642  145 WIGLNRESSNHPWKWAD 161

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: 50.12 E-value: 3.60e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  516 YMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFVGLRpeKYFWTGLSDIQTKGTFQWTIEEEVRFTHWNSDMPG 595
Cdd:cd03603    3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGY--GASWIGASDAATEGTWKWSDGEESTYTNWGSGEPH 80


                 .
gi 55666046  596 R 596
Cdd:cd03603   81 N 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: 50.12 E-value: 4.54e-07

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55666046 1107 YSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAFAWLQMETsNERVWIALNSNLTDNQYTWTDKWRVRYTNWAADEP 1184
Cdd:cd03603    3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGG-YGASWIGASDAATEGTWKWSDGEESTYTNWGSGEP 79

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: 50.12 E-value: 4.57e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   25 FLIYNEDHKRCVDAVSpSAVQTAACNQDAESQKFRWVSESQIMSVAFKLCLGVPSKTDWVAITLYACDSKSEFQKWECKN 104
Cdd:cd23411    5 FTIQHENSGKCLKVEN-SQISAVDCKQSSESLQWKWVSEHRLFNLGSKQCLGLDITKPSNTLKMFECDSKSVMLWWRCEG 83


                 ....*
gi 55666046  105 DTLLG 109
Cdd:cd23411   84 GSLYG 88

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: 50.66 E-value: 5.67e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  373 CYKI---HRDEKKIQ-RDALTTCRKEGSDLASIHTIEEFDFI---ISQLGYEPNDeLWIGL--------NDIKIQMYFEW 437
Cdd:cd03595   12 CYKIayfQDSRRRLNfEEARQACREDGGELLSIESENEQKLIerfIQTLRASDGD-FWIGLrrssqynvTSSACSSLYYW 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55666046  438 SDGTPVTFTKWLRGEPSHENnrqEDCVVM-------KGKDGY----WADRGCEWPLGYICK 487
Cdd:cd03595   91 LDGSISTFRNWYVDEPSCGS---EVCVVMyhqpsapAGQGGPylfqWNDDNCNMKNNFICK 148

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: 49.35 E-value: 7.03e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  810 YQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNdaqSAYFIGLLISLDKK-FAWMDGSKVDYVSWATG 888
Cdd:cd03603    1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGY---GASWIGASDAATEGtWKWSDGEESTYTNWGSG 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 55666046  889 EPnFANEDENCVTMYSN-----SGFWNDINCGYPN 918
Cdd:cd03603   78 EP-HNNGGGNEDYAAINhfpgiSGKWNDLANSYNT 111

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: 50.27 E-value: 8.00e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  222 KDPLTSVSYQINSKSALTWHQARKSCQQQNAELLSITEIHEQ----TYLTGLTSSlTSGLWIGL--------NSLSFNSG 289
Cdd:cd03595    9 EKPCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQklieRFIQTLRAS-DGDFWIGLrrssqynvTSSACSSL 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55666046  290 WQWSDRSPFRYLNWLPGSPSAEpGKSCV------SLNPGKNA----KWENLECVQKLGYICK 341
Cdd:cd03595   88 YYWLDGSISTFRNWYVDEPSCG-SEVCVvmyhqpSAPAGQGGpylfQWNDDNCNMKNNFICK 148

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 49.45 E-value: 8.47e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046     23 RQFLIYNEDHKRCVDA----VSPSAVQTAACNQDAESQKFRWVSESQIMSVAFKLCLGVPSKTDWVAITLYACDSKSEFQ 98
Cdd:pfam00652    1 ATGRIRNRASGKCLDVpggsSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVASDLCLDVGSTADGAKVVLWPCHPGNGNQ 80


                   ....*...
gi 55666046     99 KWECKNDT 106
Cdd:pfam00652   81 RWRYDEDG 88

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: 48.14 E-value: 1.77e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1106 SYSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAF-AWLQMETSNERVWIALNSNltDNQYTW--TDKWRVRYTNWAAD 1182
Cdd:cd03592    2 TYHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALlNGFALKYNLGYYWIDGNDI--NNEGTWvdTDKKELEYKNWAPG 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 55666046 1183 EP--KLKSACV--YLDLDGYWKTAHCNESFYFLCKR 1214
Cdd:cd03592   80 EPnnGRNENCLeiYIKDNGKWNDEPCSKKKSAICYT 115

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: 48.06 E-value: 2.11e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  516 YMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFV--GLRpekYFWTGLSDIQTKGTFQWTIEEEVRFTHWNSDM 593
Cdd:cd03591    4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVkkGNT---YAFIGITDLETEGQFVYLDGGPLTYTNWKPGE 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 55666046  594 P---GRKPGCVAMRTgiaGGLWDVLKCDEKAKFVC 625
Cdd:cd03591   81 PnnaGGGEDCVEMYT---SGKWNDVACNLTRLFVC 112

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: 48.22 E-value: 2.18e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  679 FCRAL-GGDLASINNKEEQQTIWRLitASGSYHKLFWLG--LTYGSPSEGFTWSDGSPVSYENWAYGEPNNyqNVEYCGE 755
Cdd:cd03598   19 ICRRCyRGNLASIHSFAFNYRVQRL--VSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWNYAYWAPGQPGN--RRGHCVE 94

                         90       100
                 ....*....|....*....|....*
gi 55666046  756 L--KGDptmSWNDINCEHLNNWICQ 778
Cdd:cd03598   95 LctRGG---HWRRAHCKLRRPFICS 116

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: 48.35 E-value: 3.30e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  501 EKGCRKGWKKHhfyCYMIGHTLST-----FAEANQTCNNENAYLTTIEDRYEQAFLTSFV-GLRP-EKYFWTGLSDIQTK 573
Cdd:cd03595    1 QRICRRGTEKP---CYKIAYFQDSrrrlnFEEARQACREDGGELLSIESENEQKLIERFIqTLRAsDGDFWIGLRRSSQY 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55666046  574 GT--------FQWTIEEEVRFTHWNSDMPG-RKPGCVAM------RTGIAGGL---WDVLKCDEKAKFVCKH 627
Cdd:cd03595   78 NVtssacsslYYWLDGSISTFRNWYVDEPScGSEVCVVMyhqpsaPAGQGGPYlfqWNDDNCNMKNNFICKY 149

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: 47.06 E-value: 5.47e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  235 KSALTWHQARKSCQQ-QNAELLSITEIHEQTYLTGLTSSLTSG-LWIG--LNSLSFNSGWQWSDRSPFRYLNWLPGSPSA 310
Cdd:cd03598    8 KSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTLNQAqVWIGgiITGKGRCRRFSWVDGSVWNYAYWAPGQPGN 87

                         90       100       110
                 ....*....|....*....|....*....|
gi 55666046  311 EPGkSCVSLNPgKNAKWENLECVQKLGYIC 340
Cdd:cd03598   88 RRG-HCVELCT-RGGHWRRAHCKLRRPFIC 115

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

Pssm-ID: 153071 Cd Length: 119 Bit Score: 46.76 E-value: 7.36e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  962 FMEEERKNWQEARKACIGFGGNLVSIQN---EKEQAFLTYHMKdSTFSAWTGLNDV-NSEHTFLWTDGRGV--HYTNWGK 1035
Cdd:cd03601    4 LCSDETMNYAKAGAFCRSRGMRLASLAMrdsEMRDAILAFTLV-KGHGYWVGADNLqDGEYDFLWNDGVSLptDSDLWAP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 55666046 1036 GYPGGRRSSlsyedADCVVIIggasNEAGKWMDDTCDSKRGYICQ 1080
Cdd:cd03601   83 NEPSNPQSR-----QLCVQLW----SKYNLLDDEYCGRAKRVICE 118

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: 46.53 E-value: 9.78e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1097 DGFVKYGKSSYSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAFAWLQMEtSNERVWIALNSNLTDNQYTWTDK--WRV 1174
Cdd:cd03590    3 TNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILS-GNRSYWIGLSDEETEGEWKWVDGtpLNS 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 55666046 1175 RYTNWAADEP----KLKSACVYLDLD-GYWKTAHCNESFYFLCKR 1214
Cdd:cd03590   82 SKTFWHPGEPnnwgGGGEDCAELVYDsGGWNDVPCNLEYRWICEK 126

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

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 50.08 E-value: 1.49e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046    643 EPKCPEDWGASSRTSLCFKLYAkgkhEKKTWFESRDFCRAL-GGDLASINNKEEQQTIWRLITAsgSYHKLFWLGLT--Y 719
Cdd:TIGR00864  315 HPHCPKDGEIFEENGHCFQIVP----EEAAWLDAQEQCLARaGAALAIVDNDALQNFLARKVTH--SLDRGVWIGFSdvN 388

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55666046    720 GSPSEGFTWSDGSPV-SYENWAYGEPnNYQNVEYCGELkgDPTMSWNDINCEHLNNWICQIQKG 782
Cdd:TIGR00864  389 GAEKGPAHQGEAFEAeECEEGLAGEP-HPARAEHCVRL--DPRGQCNSDLCNAPHAYVCELNPG 449

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: 45.51 E-value: 1.57e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   25 FLIYNEDHKRCVDAVSpSAVQTAACNQDAESQKFRWVSESQIMSVAFKLCLGVPSKTDWVAITLYACDSKSEFQKWECKN 104
Cdd:cd23410    4 FILESESLKKCISADK-SGLFLENCDQPSDSMLWKWVSRHRLFNLGSSMCLGLNLSYPQQPLGLFECDSTLRTLWWRCNG 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 55666046  105 DTLLGikgedlffNYGNR-QEKNIMLYKGSGLWSRWKIYGTTD 146
Cdd:cd23410   83 KMLIG--------ADQYKlTAVGSKVVASRQSSHKWKPYGSQD 117

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

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 48.93 E-value: 3.34e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046    238 LTWHQARKSCQQQNAELLSITEIHE-QTYLTG-LTSSLTSGLWIGL---NSLSFNSGWQWSDRSPFRYLNWLPGSPSAEP 312
Cdd:TIGR00864  339 AAWLDAQEQCLARAGAALAIVDNDAlQNFLARkVTHSLDRGVWIGFsdvNGAEKGPAHQGEAFEAEECEEGLAGEPHPAR 418

                           90       100       110
                   ....*....|....*....|....*....|
gi 55666046    313 GKSCVSLNPgknAKWENLE-CVQKLGYICK 341
Cdd:TIGR00864  419 AEHCVRLDP---RGQCNSDlCNAPHAYVCE 445

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

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 48.15 E-value: 5.26e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046    928 SINATTVMPTMPSVPSGCKEGWNFYSN-KCFKIFgfmeEERKNWQEARKACIGFGG-NLVSIQNEKEQAFLTYHMKDST- 1004
Cdd:TIGR00864  302 KITAHGEEPAKASHPHCPKDGEIFEENgHCFQIV----PEEAAWLDAQEQCLARAGaALAIVDNDALQNFLARKVTHSLd 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   1005 FSAWTGLNDVNS--EHTFLWTDGRGVHY-TNWGKGYPGGRRSSLsyedadCVVIiggasNEAGKWMDDTCDSKRGYICQt 1081
Cdd:TIGR00864  378 RGVWIGFSDVNGaeKGPAHQGEAFEAEEcEEGLAGEPHPARAEH------CVRL-----DPRGQCNSDLCNAPHAYVCE- 445

                          170       180
                   ....*....|....*....|....*...
gi 55666046   1082 rsdpslTNPPATIQTDGFVKYGKSSYSL 1109
Cdd:TIGR00864  446 ------LNPGGPVPDAENFAMGAASFDL 467

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

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 48.15 E-value: 5.26e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   1230 CPESdhTAWIPFHGHCYYIESSYTrNWGQASLECL-RMGSSLVSIESAAESSFLSYRVEPlKSKTNFWIGlFRNVEGTWL 1308
Cdd:TIGR00864  318 CPKD--GEIFEENGHCFQIVPEEA-AWLDAQEQCLaRAGAALAIVDNDALQNFLARKVTH-SLDRGVWIG-FSDVNGAEK 392

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 55666046   1309 ----WINNSPV-SFVNWNTGDPSGER-NDCVALHASSgfWSNIH-CSSYKGYICK 1356
Cdd:TIGR00864  393 gpahQGEAFEAeECEEGLAGEPHPARaEHCVRLDPRG--QCNSDlCNAPHAYVCE 445

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 43.67 E-value: 1.02e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046     21 DTRQFLIYNEDH-------KRCVDAVSP---SAVQTAACNQDAESQKFRW-VSESQIMSVAFKLCLGV-PSKTDWVAITL 88
Cdd:pfam00652   35 NGNQLWTLTGDGtirsvasDLCLDVGSTadgAKVVLWPCHPGNGNQRWRYdEDGTQIRNPQSGKCLDVsGAGTSNGKVIL 114

                           90
                   ....*....|..
gi 55666046     89 YACDSKSEFQKW 100
Cdd:pfam00652  115 WTCDSGNPNQQW 126

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: 42.82 E-value: 1.27e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1104 KSSYSLMRQKFQWHEAETYC-KLHNSLIASIldpYSNAFAW----LQMETSNERVWIA--LNSNLTDNQYTWTDKWRVRY 1176
Cdd:cd03598    1 GRCYRFVKSPRTFRDAQVICrRCYRGNLASI---HSFAFNYrvqrLVSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWNY 77

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 55666046 1177 TNWAADEPKL-KSACVYL-DLDGYWKTAHCNESFYFLC 1212
Cdd:cd03598   78 AYWAPGQPGNrRGHCVELcTRGGHWRRAHCKLRRPFIC 115

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1)-like subfamily; The GALNT1-like subfamily includes GALNT1 and GALNT13. They catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT1 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT13 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with 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. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467311 [Multi-domain] Cd Length: 127 Bit Score: 43.07 E-value: 1.51e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55666046   35 CVDAVSP-SAVQTAACNQDAESQKFRWVSES-QIMSVAFKLCLGVPSKTDWVAITLYACDSKSEfQKWECKN 104
Cdd:cd23433   57 CLDASRKgGPVKLEKCHGMGGNQEWEYDKETkQIRHVNSGLCLTAPNEDDPNEPVLRPCDGGPS-QKWELEG 127

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

Pssm-ID: 188093 [Multi-domain] Cd Length: 2740 Bit Score: 46.61 E-value: 1.77e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046    353 PSESDVPtHCPS--QWWPYAGHCYKIhRDEKKIQRDALTTCR-KEGSDLASIHTIEEFDFIISQLGYEPNDELWIGLNDI 429
Cdd:TIGR00864  310 PAKASHP-HCPKdgEIFEENGHCFQI-VPEEAAWLDAQEQCLaRAGAALAIVDNDALQNFLARKVTHSLDRGVWIGFSDV 387

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55666046    430 KI--QMYFEWSDGTPV-TFTKWLRGEPSHEnnRQEDCVVMkGKDGYWADRGCEWPLGYICKMKsrSQGP 495
Cdd:TIGR00864  388 NGaeKGPAHQGEAFEAeECEEGLAGEPHPA--RAEHCVRL-DPRGQCNSDLCNAPHAYVCELN--PGGP 451

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: 42.80 E-value: 2.14e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  953 SNKCFKIFgfmeEERKNWQEARKACIGFGGNLVSIQNEKE---------QAFLTYHMKDSTFsaWTGLNDVNSEHT---- 1019
Cdd:cd03600    3 SDACYTLH----PQKLTFLEAQRSCIELGGNLATVRSGEEadvvslllaAGPGRHGRGSLRL--WIGLQREPRQCSdpsl 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55666046 1020 ----FLW-TDGRGVHYTNWGKGYPGGRRSSLsyedadCVVI--IGGASNEAgKWMDDTCDSK-RGYICQ 1080
Cdd:cd03600   77 plrgFSWvTGDQDTDFSNWLQEPAGTCTSPR------CVALsaAGSTPDNL-KWKDGPCSARaDGYLCK 138

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: 42.42 E-value: 3.29e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  373 CYKIHRdEKKIQRDALTTCRKEGSDLASIHTIEEFDFIISQLGYEPNDE------LWIGLNDIKIQMY--------FEWS 438
Cdd:cd03600    6 CYTLHP-QKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGRHgrgslrLWIGLQREPRQCSdpslplrgFSWV 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 55666046  439 DGTPVT-FTKWLRgePSHENNRQEDCVVM-----KGKDGYWADRGCEWPL-GYICK 487
Cdd:cd03600   85 TGDQDTdFSNWLQ--EPAGTCTSPRCVALsaagsTPDNLKWKDGPCSARAdGYLCK 138

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.

Pssm-ID: 153067 Cd Length: 129 Bit Score: 41.80 E-value: 4.13e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  391 CRKEGSDLASIHTIEEFDFIISQLGYEPNDEL----WIGLNDIKIQmYFEWSDGTPVTFT--KWLRGEPS 454
Cdd:cd03597   29 CRNLNAVLASLTTQKKVEFVLKELQKHQMTKQkltpWVGLRKINVS-YWCWEDMSPFTNTtlQWLPGEPS 97

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: 42.03 E-value: 4.56e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  238 LTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSG-------LWIGLN------SLSFN--SGWQW-SDRSPFRYL 301
Cdd:cd03600   14 LTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGRhgrgslrLWIGLQreprqcSDPSLplRGFSWvTGDQDTDFS 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 55666046  302 NWLPGSPSAEPGKSCVSLNP----GKNAKWENLECVQKL-GYICK 341
Cdd:cd03600   94 NWLQEPAGTCTSPRCVALSAagstPDNLKWKDGPCSARAdGYLCK 138

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: 41.61 E-value: 4.59e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  239 TWHQARKSCQQQNAELLSITEIHEQTYLTG-LTSSLTSG--LWIGLNSLSFNSGWQWSDRSPFRYLNW---LPGSPSAEP 312
Cdd:cd03596   20 HYHEASEDCIARGGTLATPRDSDENDALRDyVKASVPGNweVWLGINDMVAEGKWVDVNGSPISYFNWereITAQPDGGK 99

                         90       100
                 ....*....|....*....|....*...
gi 55666046  313 GKSCVSLNPGKNAKWENLECVQKLGYIC 340
Cdd:cd03596  100 RENCVALSSSAQGKWFDEDCRREKPYVC 127

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

Pssm-ID: 153071 Cd Length: 119 Bit Score: 40.60 E-value: 8.65e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55666046 1294 NFWIGL--FRNVEGTWLWINNS--PVSFVNWNTGDPSG--ERNDCVALHASSGFWSNIHCSSYKGYICK 1356
Cdd:cd03601   50 GYWVGAdnLQDGEYDFLWNDGVslPTDSDLWAPNEPSNpqSRQLCVQLWSKYNLLDDEYCGRAKRVICE 118

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, 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 contain a potential sugar-binding pocket.

Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 40.80 E-value: 9.97e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55666046   34 RCVDA-----VSPSAVQTAACNQDAEsQKFRWVSESQIMSVAFKLCLGVP--SKTDWVAITLYACDSKSEfQKW 100
Cdd:cd23418   57 KCLDAagggtTNGTPVVIWPCNGGAN-QKWRFNSDGTIRNVNSGLCLDVAggGTANGTRLILWSCNGGSN-QRW 128

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: 39.66 E-value: 1.29e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  521 TLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFVGLRPEkYFWTGLSDIQtkGTFQWTIEEEVRFTHWNSDMPGRKPGC 600
Cdd:cd03602    8 ESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNS-AAWIGLYRDV--DSWRWSDGSESSFRNWNTFQPFGQGDC 84

                         90       100
                 ....*....|....*....|....*
gi 55666046  601 VAMRTgiaGGLWDVLKCDEKAKFVC 625
Cdd:cd03602   85 ATMYS---SGRWYAALCSALKPFIC 106

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: 39.62 E-value: 1.91e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046 1100 VKYGKSSYSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAFAWLQMETSNerVWIALNSNLTDNQYTWTDkwRVRYTNW 1179
Cdd:cd03593    6 ICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSS--YWIGLSREKSEKPWKWID--GSPLNNL 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 55666046 1180 AADEPKLKS-ACVYLDLDGYwKTAHCNESFYFLCKR 1214
Cdd:cd03593   82 FNIRGSTKSgNCAYLSSTGI-YSEDCSTKKRWICEK 116

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.

Pssm-ID: 153067 Cd Length: 129 Bit Score: 39.87 E-value: 2.02e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  231 QINSkSALTWHQARKSCQQQNAELLSIT----------EIHEQTYLTGLTSSltsglWIGLNSLSFnSGWQWSDRSPF-- 298
Cdd:cd03597   14 KINT-ARESYDNAKLYCRNLNAVLASLTtqkkvefvlkELQKHQMTKQKLTP-----WVGLRKINV-SYWCWEDMSPFtn 86

                         90
                 ....*....|.
gi 55666046  299 RYLNWLPGSPS 309
Cdd:cd03597   87 TTLQWLPGEPS 97

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: 39.28 E-value: 2.68e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  516 YMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFVGLRPEKYFWTGLSDIQTKGTFQWTIEEEVRFTHWNSDMP- 594
Cdd:cd03592    3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYYWIDGNDINNEGTWVDTDKKELEYKNWAPGEPn 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 55666046  595 -GRKPGCVAMRTgIAGGLWDVLKCDEKAKFVC 625
Cdd:cd03592   83 nGRNENCLEIYI-KDNGKWNDEPCSKKKSAIC 113

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: 39.33 E-value: 2.78e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  230 YQInSKSALTWHQARKSCQQQNAELLSITEIHEQTYLtGLTSSLTSGLWIGLNSLSFNSGWQWSDRSPFRYLNWLPGSPS 309
Cdd:cd03603    3 YKF-VDGGMTWEAAQTLAESLGGHLVTINSAEENDWL-LSNFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPH 80


                 ....
gi 55666046  310 AEPG 313
Cdd:cd03603   81 NNGG 84

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.

Pssm-ID: 153067 Cd Length: 129 Bit Score: 39.10 E-value: 3.35e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55666046  945 CKEGWNFYSNKCFKIfgfmEEERKNWQEARKACIGFGGNLVSIQNEKEQAFL-----TYHMKDSTFSAWTGLNDVN 1015
Cdd:cd03597    1 CGEGWHLVGNSCLKI----NTARESYDNAKLYCRNLNAVLASLTTQKKVEFVlkelqKHQMTKQKLTPWVGLRKIN 72

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the C-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 bears a potential sugar binding site.

Pssm-ID: 467340 [Multi-domain] Cd Length: 126 Bit Score: 38.50 E-value: 5.01e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   24 QFLIYNED-----HKRCVD-AVSPSAVQTAACNQDAESQKFRWVSES-QIMSVAFKLCLGVPSKTDwvAITLYACDSKSE 96
Cdd:cd23462   42 QYWMLTKDgeirrDDLCLDyAGGSGDVTLYPCHGMKGNQFWIYDEETkQIVHGTSKKCLELSDDSS--KLVMEPCNGSSP 119


                 ....*
gi 55666046   97 FQKWE 101
Cdd:cd23462  120 RQQWE 124

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: 38.20 E-value: 5.31e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  954 NKCFKIFGfmeeERKNWQEARKACIG-FGGNLVSIQNekeQAFltyHMKDSTFSA-------WTG--LNDVNSEHTFLWT 1023
Cdd:cd03598    1 GRCYRFVK----SPRTFRDAQVICRRcYRGNLASIHS---FAF---NYRVQRLVStlnqaqvWIGgiITGKGRCRRFSWV 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 55666046 1024 DGRGVHYTNWGKGYPGGRRSSlsyedadCVVIiggaSNEAGKWMDDTCDSKRGYICQ 1080
Cdd:cd03598   71 DGSVWNYAYWAPGQPGNRRGH-------CVEL----CTRGGHWRRAHCKLRRPFICS 116

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: 38.05 E-value: 5.56e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046  230 YQINSKSaLTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSGLWIGLNSLSFNSGWQWSDRSPFRYLNWLPGSPS 309
Cdd:cd03591    4 FVTNGEE-KNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPN 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 55666046  310 -AEPGKSCVSLNpgKNAKWENLECVQKLGYIC 340
Cdd:cd03591   83 nAGGGEDCVEMY--TSGKWNDVACNLTRLFVC 112

ricin B-type lectin domain, beta-trefoil fold, found in Actinomycete actinohivin and similar proteins; Actinohivin is an actinomycete lectin with a potent specific anti-human immunodeficiency virus (anti-HIV) activity. It inhibits viral entry to cells by binding the high-mannose type sugar chains of gp120. Actinohivin contains a ricin B-type lectin domain with 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 contains a sugar-binding pocket.

Pssm-ID: 467294 [Multi-domain] Cd Length: 120 Bit Score: 37.80 E-value: 7.75e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55666046   23 RQFLIYNEDHKRCVDAVSPSAVQTAACNQDAeSQKFRWVSES----QIMSVAFKLCLGVpskTDWVAITLYACDSkSEFQ 98
Cdd:cd23415    1 GTVRLRNVATGRCLDSNAGGNVYTGPCNGGP-YQRWTWSGVGdgtvTLRNAATGRCLDS---NGNGGVYTLPCNG-GSYQ 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 55666046   99 KWECKNDTLLGIKgedlFFNYGNRQ------EKNIMLYK-GSGLWSRWK 140
Cdd:cd23415   76 RWRVTSTSGGGVT----LRNVATGRcldsngSGGVYTRPcNGGSYQRWR 120