C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051  186 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS-WIGLQDLNMEGEFVWSDGSPVG 264
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSyWIGLSDEETEGEWKWVDGTPLN 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 7305051  265 --YSNWNPGEPNN-GGQGEDCVMMRG-SGQWNDAFC-RSYLdaWVCE 306
Cdd:cd03590  81 ssKTFWHPGEPNNwGGGGEDCAELVYdSGGWNDVPCnLEYR--WICE 125

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051  186 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS-WIGLQDLNMEGEFVWSDGSPVG 264
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSyWIGLSDEETEGEWKWVDGTPLN 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 7305051  265 --YSNWNPGEPNN-GGQGEDCVMMRG-SGQWNDAFC-RSYLdaWVCE 306
Cdd:cd03590  81 ssKTFWHPGEPNNwGGGGEDCAELVYdSGGWNDVPCnLEYR--WICE 125

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051    204 SKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINK--KDSWIGLQDLNMEGEFVWSDGSPVGYSNWNPgEPNNGGQGED 281
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKsnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-EPNNNGENED 79

                          90       100
                  ....*....|....*....|....*..
gi 7305051    282 CVMM-RGSGQWNDAFCRSYLdAWVCEQ 307
Cdd:pfam00059  80 CVELsSSSGKWNDENCNSKN-PFVCEK 105

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051     139 LQDDLVNIKSLGLNekrtASDSLEKLQEEVAKlwieiliskgTACNICPKNWLHFQQ--KCYYFGKGSKQWIQARFACSD 216
Cdd:TIGR00864  285 LDLSIQNRGGSDLD----AAWKITAHGEEPAK----------ASHPHCPKDGEIFEEngHCFQIVPEEAAWLDAQEQCLA 350

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051     217 L-QGRLVSIHSQKEQDFLMQHINK---KDSWIGLQDLNM--EGEFVWSDGSPV-GYSNWNPGEPNNgGQGEDCVMMRGSG 289
Cdd:TIGR00864  351 RaGAALAIVDNDALQNFLARKVTHsldRGVWIGFSDVNGaeKGPAHQGEAFEAeECEEGLAGEPHP-ARAEHCVRLDPRG 429

                          170
                   ....*....|....*..
gi 7305051     290 QWNDAFCrSYLDAWVCE 306
Cdd:TIGR00864  430 QCNSDLC-NAPHAYVCE 445

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051      63 IQNVSHVTKDLQKF--QSNQLAQKSQ------VVQMSQNLQELQAEQKQMKAQDSRLSQNltglQEDLRNaQSQNSKLSQ 134
Cdd:pfam15921   80 LEEYSHQVKDLQRRlnESNELHEKQKfylrqsVIDLQTKLQEMQMERDAMADIRRRESQS----QEDLRN-QLQNTVHEL 154

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 7305051     135 NLNR-LQDDLVNIKSLGLNEKRTASDSLEKLQEEVAKLWIE 174
Cdd:pfam15921  155 EAAKcLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVD 195

Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051      62 AIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAE--------QKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLS 133
Cdd:smart00503  16 NIQKISQNVAELQKLHEELLTPPDADKELREKLERLIDDikrlakeiRAKLKELEKENLENRASGSASDRTRKAQTEKLR 95

                   ....*.
gi 7305051     134 QNLNRL 139
Cdd:smart00503  96 KKFKEV 101

family of the cytolysin A (ClyA) family alpha pore-forming toxins (alpha-PFT) including Bacillus cereus HblB, Aeromonas hydrophila AhlB, Bacillus thuringiensis Cry6Aa and similar proteins; This family belongs to the ClyA family of alpha-PFT bacterial toxins. PFTs form the major group of virulence factors in many pathogenic bacteria and in general are critical components of the molecular offensive and defensive machinery of cells in all kingdoms of life. Bacterial PFTs facilitate the takeover of host resources by puncturing holes in the membrane. PFTs can be classified as alpha-PFTs and beta-PFTs depending on the secondary structures of their membrane component. Alpha-PFTs use a ring of amphipathic helices while beta-PFTs use a beta-barrel to construct the pore. Members of this family include the toxins: Bacillus cereus hemolysin binding component B (HblB or HBL-B) of the diarrheal enterotoxin hemolysin BL, Aeromonas hydrophila hemolytic (Ahl) component B (AhlB) of the tripartite AhlABC toxin, Vibrio cholerae cytotoxin motility associated killing factor A (MakA) cytotoxin, Xenorhabdus nematophila alpha-xenorhabdolysin (XaxA), Bacillus thuringiensis crystal 6Aa (Cry6Aa) parasporal crystal (Cry) toxin, and Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA) of the non-hemolytic enterotoxin Nhe, which, despite its name, is hemolytic, among others. In solution, ClyA proteins have an elongated, almost entirely alpha-helical structure, except for a short hydrophobic beta-hairpin known as the beta-tongue. Pore formation by ClyA requires circular oligomerization of the toxin by a sequential mechanism. This, in turn, concentrates the amphipathic helices in the center of the ring-like structure, forming a helical barrel that inserts into the membrane by a wedge-like mechanism. Compared with ClyA, NheA is almost entirely alpha-helical with an enlarged "head" domain, and an enlarged beta-tongue; it has been proposed that NheA could even form beta-barrel pores. Alpha-PFTs with similar structures are increasingly being found in eukaryotes, in particular as components of the immune systems of animals. This family may be distantly related to Escherichia coli alpha-PFT hemolysin E (HlyE, also known as ClyA or SheA).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051   55 LKQLGDTAIQNVSHVTKDLQKFQSNqlaqKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQ 134
Cdd:cd21116 100 LEALQSQVTKKQTSVTSFINELTTF----KNDLDDDSRNLQTDATKAQAQVAVLNALKNQLNSLAEQIDAAIDALEKLSN 175

                        90
                ....*....|..
gi 7305051  135 NLNRLQDDLVNI 146
Cdd:cd21116 176 DWQTLDSDIKEL 187

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051  186 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS-WIGLQDLNMEGEFVWSDGSPVG 264
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSyWIGLSDEETEGEWKWVDGTPLN 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 7305051  265 --YSNWNPGEPNN-GGQGEDCVMMRG-SGQWNDAFC-RSYLdaWVCE 306
Cdd:cd03590  81 ssKTFWHPGEPNNwGGGGEDCAELVYdSGGWNDVPCnLEYR--WICE 125

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051  186 CPKNWLHFQQKCYYFGKGSKQWIQARFACSD-----LQGRLVSIHSQKEQDF---LMQHINKKDS----WIGLQDLNMEG 253
Cdd:cd03589   1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFvydLFESSRGPDTpyglWIGLHDRTSEG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7305051  254 EFVWSDGSPVGYSNWNPGEPNNGGQGEDCVMMR----GSGQWNDAFCrSYLDAWVC 305
Cdd:cd03589  81 PFEWTDGSPVDFTKWAGGQPDNYGGNEDCVQMWrrgdAGQSWNDMPC-DAVFPYIC 135

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051    204 SKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINK--KDSWIGLQDLNMEGEFVWSDGSPVGYSNWNPgEPNNGGQGED 281
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKsnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-EPNNNGENED 79

                          90       100
                  ....*....|....*....|....*..
gi 7305051    282 CVMM-RGSGQWNDAFCRSYLdAWVCEQ 307
Cdd:pfam00059  80 CVELsSSSGKWNDENCNSKN-PFVCEK 105

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051  186 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKdSWIGLQDLNMEGEFVWSDGSPVGY 265
Cdd:cd03588   1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDY-QWIGLNDRTIEGDFRWSDGHPLQF 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 7305051  266 SNWNPGEPNNG-GQGEDCVMMRG--SGQWNDAFCRSYL 300
Cdd:cd03588  80 ENWRPNQPDNFfATGEDCVVMIWheEGEWNDVPCNYHL 117

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051  186 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDSWIGLQDLNMEGEFVWSDGSPvgY 265
Cdd:cd03593   1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSP--L 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 7305051  266 SNWNpgEPNNGGQGEDCVMMrGSGQWNDAFCrSYLDAWVCEQ 307
Cdd:cd03593  79 NNLF--NIRGSTKSGNCAYL-SSTGIYSEDC-STKKRWICEK 116

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051  198 YYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS---WIGLQDLNMEGEFVWSDGSPVGYSNWNPGEPN 274
Cdd:cd03592   3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLgyyWIDGNDINNEGTWVDTDKKELEYKNWAPGEPN 82

                        90       100       110
                ....*....|....*....|....*....|....
gi 7305051  275 NGGqGEDCVMM--RGSGQWNDAFCRSYLDAwVCE 306
Cdd:cd03592  83 NGR-NENCLEIyiKDNGKWNDEPCSKKKSA-ICY 114

C-type lectin-like protein; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7305051   186 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDSWIGLQDLNMEGEFVWSDGS 261
Cdd:PHA02642  88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNRESSNHPWKWADNS 163

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051  196 KCYYFGKGSKQWIQARFACSDL-QGRLVSIHSQkeqDFLMQ------HINKKDSWIGLQDLNMEG--EFVWSDGSPVGYS 266
Cdd:cd03598   2 RCYRFVKSPRTFRDAQVICRRCyRGNLASIHSF---AFNYRvqrlvsTLNQAQVWIGGIITGKGRcrRFSWVDGSVWNYA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 7305051  267 NWNPGEPnnGGQGEDCVMM--RGsGQWNDAFCrSYLDAWVC 305
Cdd:cd03598  79 YWAPGQP--GNRRGHCVELctRG-GHWRRAHC-KLRRPFIC 115

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051  186 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDS-------WIGLQDLNMEgEFVWS 258
Cdd:cd03597   1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMtkqkltpWVGLRKINVS-YWCWE 79

                        90       100
                ....*....|....*....|.
gi 7305051  259 DGSPVGYS--NWNPGEPNNGG 277
Cdd:cd03597  80 DMSPFTNTtlQWLPGEPSDAG 100

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051  193 FQQKCY---YFGKGSKQ--WIQARFACSDLQGRLVSIHSQKEQDFLMQHI-----NKKDSWIGL--------QDLNMEGE 254
Cdd:cd03595   8 TEKPCYkiaYFQDSRRRlnFEEARQACREDGGELLSIESENEQKLIERFIqtlraSDGDFWIGLrrssqynvTSSACSSL 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7305051  255 FVWSDGSPVGYSNWNPGEPNNGgqGEDCVMM-------RGSG-----QWNDAFCRS 298
Cdd:cd03595  88 YYWLDGSISTFRNWYVDEPSCG--SEVCVVMyhqpsapAGQGgpylfQWNDDNCNM 141

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051   50 ETEKNLKQLG---DTAIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQ 126
Cdd:COG4372  42 KLQEELEQLReelEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 7305051  127 SQNSKLSQNLNRLQDDLVNIKSlglnEKRTASDSLEKLQEEVAKLWIEI 175
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQS----EIAEREEELKELEEQLESLQEEL 166

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051   64 QNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRLQDdl 143
Cdd:COG4372  31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE-- 108

                        90       100       110
                ....*....|....*....|....*....|.
gi 7305051  144 vnikslglnEKRTASDSLEKLQEEVAKLWIE 174
Cdd:COG4372 109 ---------EAEELQEELEELQKERQDLEQQ 130

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051   60 DTAIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRL 139
Cdd:COG4372  34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 7305051  140 QDDLVNIKslglNEKRTASDSLEKLQEEVAKLWIEI 175
Cdd:COG4372 114 QEELEELQ----KERQDLEQQRKQLEAQIAELQSEI 145

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051   82 AQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRLQDDLVNIKSLGL---NEKRTAS 158
Cdd:COG4372  28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAqaqEELESLQ 107

                        90
                ....*....|....*..
gi 7305051  159 DSLEKLQEEVAKLWIEI 175
Cdd:COG4372 108 EEAEELQEELEELQKER 124

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051     49 WETEKNLKQLgDTAIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQ-NLTGLQEDLRNAQS 127
Cdd:TIGR04320 254 NSLAALQAKL-ATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQnNLATAQAALANAEA 332

                          90
                  ....*....|....*.
gi 7305051    128 QNSKLSQNLNRLQDDL 143
Cdd:TIGR04320 333 RLAKAKEALANLNADL 348

C-type lectin-like protein; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305051   186 CPKNWLHFQQKCYYFGKGSKQWIQARFACSDLQGRLVSIHSQKEQDFLMQHINKKDSWIGLQDLNMEGEFVWSDGSPVG 264
Cdd:PHA03097  46 CRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGIEKKKGDDDDREVLDKVVK 124

Syntaxin N-terminal domain; Three-helix domain that (in Sso1p) slows the rate of its reaction with the SNAP-25 homologue Sec9p

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051      62 AIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAE--------QKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLS 133
Cdd:smart00503  16 NIQKISQNVAELQKLHEELLTPPDADKELREKLERLIDDikrlakeiRAKLKELEKENLENRASGSASDRTRKAQTEKLR 95

                   ....*.
gi 7305051     134 QNLNRL 139
Cdd:smart00503  96 KKFKEV 101

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051   50 ETEKNLKQLG---DTAIQNVSHVTKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQ 126
Cdd:COG4372  77 QLEEELEELNeqlQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156

                        90       100
                ....*....|....*....|....*...
gi 7305051  127 SQNSKLSQNLNRLQDDLVNIKSLGLNEK 154
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQA 184

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051   70 TKDLQKFQSNQLAQKSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRLQDDLVNIKSl 149
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE- 337

                        90       100
                ....*....|....*....|..
gi 7305051  150 glnEKRTASDSLEKLQEEVAKL 171
Cdd:COG1196 338 ---ELEELEEELEEAEEELEEA 356

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051      50 ETEKNLKQLGDTAIQNVSHvTKDLQKFQSnQLAQ-KSQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQ 128
Cdd:TIGR02168  240 ELEELQEELKEAEEELEEL-TAELQELEE-KLEElRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 7305051     129 NSKLS----QNLNRLQDDLVNIKSLG--LNEKRTASDSLEKLQEEVAKLWIE 174
Cdd:TIGR02168  318 LEELEaqleELESKLDELAEELAELEekLEELKEELESLEAELEELEAELEE 369

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305051   85 SQVVQMSQNLQELQAEQKQMKAQDSRLSQNLTGLQEDLRNAQSQNSKLSQNLNRLQDDLVnikslglnekrTASDSLEKL 164
Cdd:COG3883  16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-----------EAEAEIEER 84

                ....*..
gi 7305051  165 QEEVAKL 171
Cdd:COG3883  85 REELGER 91