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 1958651174  601 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKN--TQQRVSPWVGLRKINISYWGWED 678
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHqmTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958651174  679 MSPFTNTSLQWLPGEPNDSGFCAYLERAAVAGLKANPCTSMADGLVCEK 727
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958651174  866 ACQCNGHSTciNNNVCEQ------CKNLTTGRQCQDCMPGYYGDPTNGGQCT 911
Cdd:cd00055      1 PCDCNGHGS--LSGQCDPgtgqceCKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651174    3 VYDGDSIYAPLVAVLSGlivpevrgNETVPEVVTTSGYALLHFFSDAAYNLTGFNIFYSI 62
Cdd:cd00041     62 IYDGPSTSSPLLGRFCG--------STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113

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 1958651174  601 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKN--TQQRVSPWVGLRKINISYWGWED 678
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHqmTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958651174  679 MSPFTNTSLQWLPGEPNDSGFCAYLERAAVAGLKANPCTSMADGLVCEK 727
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129

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

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651174   601 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKNTQQRvSPWVGLRKINISY-WGWEDM 679
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDPDSNGsWQWSDG 79

                            90       100
                    ....*....|....*....|....*
gi 1958651174   680 SPFTNTSLqWLPGEPNDS-GFCAYL 703
Cdd:smart00034   80 SGPVSYSN-WAPGEPNNSsGDCVVL 103

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958651174  866 ACQCNGHSTciNNNVCEQ------CKNLTTGRQCQDCMPGYYGDPTNGGQCT 911
Cdd:cd00055      1 PCDCNGHGS--LSGQCDPgtgqceCKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958651174  206 PLQRYGHSLALYQENIFMYGGrMETSDGNVTDELWVFNVRS 246
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGG-YTGGEGQPSDDVYVLSLPT 40

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958651174  867 CQCNGHSTciNNNVCEQ------CKNLTTGRQCQDCMPGYYGDP-TNGGQC 910
Cdd:pfam00053    1 CDCNPHGS--LSDTCDPetgqclCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49

Laminin-type epidermal growth factor-like domai;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1958651174   867 CQCNG----HSTCINNN-VCEqCKNLTTGRQCQDCMPGYYGDPTNG 907
Cdd:smart00180    1 CDCDPggsaSGTCDPDTgQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45

delta serrate ligand;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1958651174    88 ECDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKLCvcNDSWQGPDC 134
Cdd:smart00051   20 TCDENYYGEGCNK-FCRPRDDFFGHYTCDENGNKGC--LEGWMGPYC 63

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 1958651174  601 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKN--TQQRVSPWVGLRKINISYWGWED 678
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHqmTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958651174  679 MSPFTNTSLQWLPGEPNDSGFCAYLERAAVAGLKANPCTSMADGLVCEK 727
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651174  155 PSVGRASHKAVLHGKFMWVIGGYTFNYSSFQM---VLNYNLESSIWNVGAVSrgPLQRYGHSLALYQENIFMYGGRmetS 231
Cdd:COG3055     57 PGPPRHHAAAVAQDGKLYVFGGFTGANPSSTPlndVYVYDPATNTWTKLAPM--PTPRGGATALLLDGKIYVVGGW---D 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651174  232 DGNVTDELWVFNVRSQSWSTKTPTILghgqqyAVEGHSAHImeLDSGdvvMIVIFGysaiyGYTSSIqeyhiSSNTWlvp 311
Cdd:COG3055    132 DGGNVAWVEVYDPATGTWTQLAPLPT------PRDHLAAAV--LPDG---KILVIG-----GRNGSG-----FSNTW--- 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651174  312 ETKGAIVQGGYGHTSVYdeMTKSVYVHGGYkalpgnkYGLVDDLYKYEVNSRTWTILKESGFARYLHSAVLISGAVLVFG 391
Cdd:COG3055    188 TTLAPLPTARAGHAAAV--LGGKILVFGGE-------SGFSDEVEAYDPATNTWTALGELPTPRHGHAAVLTDGKVYVIG 258

                   ....*
gi 1958651174  392 GNTHN 396
Cdd:COG3055    259 GETKP 263

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651174  611 SCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKNTQQRVspWVGLRKINI-SYWGWEDMSPFTNTSlQW 689
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDV--WIGLNDLSSeGTWKWSDGSPLVDYT-NW 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958651174  690 LPGEPN--DSGFCAYLERAAVAGLKANPCTSMAdGLVCEK 727
Cdd:cd00037     78 APGEPNpgGSEDCVVLSSSSDGKWNDVSCSSKL-PFICEK 116

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651174  619 RESYDSAKLYCYNLSGNLASLTTSKEVGFVLDEIQKNTQqrvSPWVGLRKINIS-YWGWEDMSPFTNTSLQWLPGEPNDS 697
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNK---YFWIGLTDRKNEgTWKWVDGSPVNYTNWAPEPNNNGEN 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958651174  698 GFCAYLERAAvAGLKANPCTSMAdGLVCEK 727
Cdd:pfam00059   78 EDCVELSSSS-GKWNDENCNSKN-PFVCEK 105

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 1958651174  601 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFvldeIQKNTQQRVSPWVGLRKINI-SYWGWEDM 679
Cdd:cd03590      1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEF----ISKILSGNRSYWIGLSDEETeGEWKWVDG 76

                           90       100
                   ....*....|....*....|....*...
gi 1958651174  680 SPFTNTSLQWLPGEPNDSGF----CAYL 703
Cdd:cd03590     77 TPLNSSKTFWHPGEPNNWGGggedCAEL 104

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 1958651174  601 CGEGWNHVGDSCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFvldeIQKNTQQRvSPWVGLRKINISY-WGWEDM 679
Cdd:cd03593      1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEF----LQSQIGSS-SYWIGLSREKSEKpWKWIDG 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1958651174  680 SPFTNtslqWL-PGEPNDSGFCAYLERaavAGLKANPCtSMADGLVCEK 727
Cdd:cd03593     76 SPLNN----LFnIRGSTKSGNCAYLSS---TGIYSEDC-STKKRWICEK 116

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958651174  206 PLQRYGHSLALYQENIFMYGGrMETSDGNVTDELWVFNVRS 246
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGG-YTGGEGQPSDDVYVLSLPT 40

C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS); CLECT_DGCR2_like: C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DGS is also known velo-cardio-facial syndrome (VCFS). DGS is a genetic abnormality that results in malformations of the heart, face, and limbs and is associated with schizophrenia and depressive disorders. DGCR2 is a candidate for involvement in the pathogenesis of DGS since the DGCR2 gene lies within the minimal DGS critical region (MDGRC) of 22q11, which when deleted gives rise to DGS, and the DGCR2 gene is in close proximity to the balanced translocation breakpoint in a DGS patient having a balanced translocation.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651174  601 CGEGWNHVGD--SCLRINSSRESYDSAKLYCYNLSGNLASLTTSKEVGFVL------DEIQKNTQQRVSPWVGLRKI--- 669
Cdd:cd03599      1 CPSGWHHYEGtaSCYKVYLSGENYWDAVQTCQKVNGSLATFTTDQELQFILaqewdfDERVFGRKDQCKFWVGYQYVitn 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958651174  670 -NISYWG-WEdmSPFTNTSLQWLPGEP--------NDSGFCAYLER 705
Cdd:cd03599     81 rNHSLEGrWE--VAYKGSMEVFLPPEPifatgmstNDNVFCAQLQC 124

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651174    3 VYDGDSIYAPLVAVLSGlivpevrgNETVPEVVTTSGYALLHFFSDAAYNLTGFNIFYSI 62
Cdd:cd00041     62 IYDGPSTSSPLLGRFCG--------STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113

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 1958651174  601 CGEGWNHVGDSCLRINSSRESYDSAKLYCYN-----LSGNLASLTTSKEVGFVLDEIQKNTQQRVSP--WVGL-RKINIS 672
Cdd:cd03589      1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDLFESSRGPDTPYglWIGLhDRTSEG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958651174  673 YWGWEDMSPFTNTslQWLPGEPNDSGF---CAYLERAAVAGLKAN--PCT 717
Cdd:cd03589     81 PFEWTDGSPVDFT--KWAGGQPDNYGGnedCVQMWRRGDAGQSWNdmPCD 128

epithiospecifier protein

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651174  308 WLVPETKGAIVQG---GYGHTSVYDEMtksvYVHGGykALPGNKYgLVDDLYKYEVNSRTWTILKESGFARYLHS----A 380
Cdd:PLN02153     9 WIKVEQKGGKGPGprcSHGIAVVGDKL----YSFGG--ELKPNEH-IDKDLYVFDFNTHTWSIAPANGDVPRISClgvrM 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958651174  381 VLISGAVLVFGGNTHNdtslsngaKCFSaDFLAYDIACDEWKTLPKPNLHRDVN-RFGHSAVVINGSMYIFGGFS 454
Cdd:PLN02153    82 VAVGTKLYIFGGRDEK--------REFS-DFYSYDTVKNEWTFLTKLDEEGGPEaRTFHSMASDENHVYVFGGVS 147

Galactose oxidase, central domain;

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958651174  332 TKSVYVHGGYKALPGNKYglvDDLYKYEVNSRTWTILKESGFARYLHSAVLI 383
Cdd:pfam13415    1 GDKLYIFGGLGFDGQTRL---NDLYVYDLDTNTWTQIGDLPPPRSGHSATYI 49

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651174  625 AKLYCYNLSGNLASLTTSKEvgfvLDEIQKNTQQRVSP-WVGLRKiNISYWGWEDMSPFTntSLQWLPGEPNDSGFCAYL 703
Cdd:cd03602     15 AQQYCRENYTDLATVQNQED----NALLSNLSRVSNSAaWIGLYR-DVDSWRWSDGSESS--FRNWNTFQPFGQGDCATM 87

Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain defined by structure.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958651174   89 CDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKlcVCNDSWQGPDCS 135
Cdd:pfam01414    1 CDENYYGSTCSK-FCRPRDDKFGHYTCDANGNK--VCLPGWTGPYCD 44

Kelch motif;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958651174  209 RYGHSLALYQENIFMYGGRmeTSDGNVTDELWVFNVRSQSWST 251
Cdd:pfam13964    2 RTFHSVVSVGGYIYVFGGY--TNASPALNKLEVYNPLTKSWEE 42

N-acetylneuraminate epimerase;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958651174  353 DDLYKYEVN--SRTWTILKE-SGFARYLHSAVLISGAVLVFGGNTHNDTSLSNGAkcFSaDFLAYDIACDEWKTLPKpnl 429
Cdd:PRK14131    50 TSWYKLDLNapSKGWTKIAAfPGGPREQAVAAFIDGKLYVFGGIGKTNSEGSPQV--FD-DVYKYDPKTNSWQKLDT--- 123

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958651174  430 HRDVNRFGHSAVVINGSM-YIFGGFSSVLLN 459
Cdd:PRK14131   124 RSPVGLAGHVAVSLHNGKaYITGGVNKNIFD 154

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.

                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958651174  435 RFGHSAVVINGSMYIFGGFSS---VLLNDILVYKPPS 468
Cdd:pfam13854    4 RYGHCAVTVGDYIYLYGGYTGgegQPSDDVYVLSLPT 40