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 71043880 607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKQTMGRESHWIGLTDSEQESEWKWLDGTPV- 685
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWKWVDGTPLn 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71043880 686 -DYKNWKAGQPDNWGsghGPGEDCAGLIY-AGQWNDFQCDEINNFICEK 732
Cdd:cd03590  81 sSKTFWHPGEPNNWG---GGGEDCAELVYdSGGWNDVPCNLEYRWICEK 126

mechanosensitive channel MscK;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880    85 AVESDLKKLGDQ----TGKKALSTNSE--LSTF------RSDILDLRQQLQEITEKTSKNKDMLEKLQANGD-------- 144
Cdd:PRK11281   40 DVQAQLDALNKQklleAEDKLVQQDLEqtLALLdkidrqKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDeetretls 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880   145 --SLVDRQSQLKETLQNnsflITTVNKTLQAYNGYVTNLQQDTSvlqgNLQSQMYSQNVVIMNLNN-------------- 208
Cdd:PRK11281  120 tlSLRQLESRLAQTLDQ----LQNAQNDLAEYNSQLVSLQTQPE----RAQAALYANSQRLQQIRNllkggkvggkalrp 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880   209 ------------LNLTQVQQRNLITN-------LQRSVDDTSLAIQQIKNDFQNLQQVFLQakkdtdwlKEKVQSLQTL- 268
Cdd:PRK11281  192 sqrvllqaeqalLNAQNDLQRKSLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQEAINS--------KRLTLSEKTVq 263

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 71043880   269 -AANNSALAKANNDTL----EDMNNQLSSF-TGQMDNITTISQAN 307
Cdd:PRK11281  264 eAQSQDEAARIQANPLvaqeLEINLQLSQRlLKATEKLNTLTQQN 308

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 71043880 607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKQTMGRESHWIGLTDSEQESEWKWLDGTPV- 685
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWKWVDGTPLn 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71043880 686 -DYKNWKAGQPDNWGsghGPGEDCAGLIY-AGQWNDFQCDEINNFICEK 732
Cdd:cd03590  81 sSKTFWHPGEPNNWG---GGGEDCAELVYdSGGWNDVPCNLEYRWICEK 126

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880   625 KEIFEDAKLFCEDKSSHLVFINSREEQQWIKKQTMGR-ESHWIGLTDSEQESEWKWLDGTPVDYKNWKAgqpdnWGSGHG 703
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-----EPNNNG 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 71043880   704 PGEDCAGLIYA-GQWNDFQCDEINNFICEK 732
Cdd:pfam00059  76 ENEDCVELSSSsGKWNDENCNSKNPFVCEK 105

mechanosensitive channel MscK;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880    85 AVESDLKKLGDQ----TGKKALSTNSE--LSTF------RSDILDLRQQLQEITEKTSKNKDMLEKLQANGD-------- 144
Cdd:PRK11281   40 DVQAQLDALNKQklleAEDKLVQQDLEqtLALLdkidrqKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDeetretls 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880   145 --SLVDRQSQLKETLQNnsflITTVNKTLQAYNGYVTNLQQDTSvlqgNLQSQMYSQNVVIMNLNN-------------- 208
Cdd:PRK11281  120 tlSLRQLESRLAQTLDQ----LQNAQNDLAEYNSQLVSLQTQPE----RAQAALYANSQRLQQIRNllkggkvggkalrp 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880   209 ------------LNLTQVQQRNLITN-------LQRSVDDTSLAIQQIKNDFQNLQQVFLQakkdtdwlKEKVQSLQTL- 268
Cdd:PRK11281  192 sqrvllqaeqalLNAQNDLQRKSLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQEAINS--------KRLTLSEKTVq 263

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 71043880   269 -AANNSALAKANNDTL----EDMNNQLSSF-TGQMDNITTISQAN 307
Cdd:PRK11281  264 eAQSQDEAARIQANPLvaqeLEINLQLSQRlLKATEKLNTLTQQN 308

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880  454 RGSQGPPGPTGNKGQKGEKGEPGPPGPAGERGTIGPVGPPGERGSKGSKGSQGPKGSRGSPGKPGPQGPSGDPGPPGPP- 532
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQg 207

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 71043880  533 -------GKDGLPGPQGPPGFQGLQGTVGEPGVPGPRG 563
Cdd:NF038329 208 pagpagpDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTG 245

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880 113 SDILDLRQQLQEITEKTSKNKDMLEKLQANGDSLVDRQSQLKETLQNNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNL 192
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880 193 QSQ-------------MYSQNVVIMNLNNLNLTQVQQRnlITNLQRSVDDTSLAIQQIKNDFQNLQQVFLQAKKDTDWLK 259
Cdd:COG4942 100 EAQkeelaellralyrLGRQPPLALLLSPEDFLDAVRR--LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71043880 260 EKVQSLQTLAANNSALAKANNDTLEDMNNQLSSFTGQMDNITTISQANEQSMKDLQDLHKDTENRTA 326
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880  455 GSQGPPGPTGNKGQKGEKGEPGPPGPAGERGTIGPVGPP-----GERGSKGSKGSQGPKGSRGSPGKPGPQGPSGDPGPP 529
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                         90       100       110
                 ....*....|....*....|....*....|....
gi 71043880  530 GPPGKDGLPGPQGPPGFQGLQGTVGEPGVPGPRG 563
Cdd:NF038329 272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880     59 YKVVEKMDTVTDGMETSRQTYDNKLIAVESDLKKL---GDQTGKKALSTNSELSTFRSDILDLRQQLQEItektskNKDM 135
Cdd:TIGR00606  687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKekrRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV------NRDI 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880    136 LEklqangdslvdrqsqLKETLQNNSFLITTVNKTLQAyngyVTNLQQDTSVLQgNLQSQM------YSQNVVIMNLNNL 209
Cdd:TIGR00606  761 QR---------------LKNDIEEQETLLGTIMPEEES----AKVCLTDVTIME-RFQMELkdverkIAQQAAKLQGSDL 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880    210 NLTQVQQRNLITNLQRSVDDTSLAIQQIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAkannDTLEDMNNQ 289
Cdd:TIGR00606  821 DRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFE----EQLVELSTE 896

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880    290 LSSFtgqmdnITTISQANEQSMKDLQDLHKD-TENRTAVkfSQLEERFQVFETDIVNIINNISYTAHHLRTLtsnLNDVR 368
Cdd:TIGR00606  897 VQSL------IREIKDAKEQDSPLETFLEKDqQEKEELI--SSKETSNKKAQDKVNDIKEKVKNIHGYMKDI---ENKIQ 965

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 71043880    369 TTCTDTLTRHTDDLTSLNNTLVniRLDSISLRMQQDM--MRSRLDTE 413
Cdd:TIGR00606  966 DGKDDYLKQKETELNTVNAQLE--ECEKHQEKINEDMrlMRQDIDTQ 1010

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 71043880 607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKQTMGRESHWIGLTDSEQESEWKWLDGTPV- 685
Cdd:cd03590   1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWKWVDGTPLn 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71043880 686 -DYKNWKAGQPDNWGsghGPGEDCAGLIY-AGQWNDFQCDEINNFICEK 732
Cdd:cd03590  81 sSKTFWHPGEPNNWG---GGGEDCAELVYdSGGWNDVPCNLEYRWICEK 126

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 71043880 617 KCYYFSVEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKQ--TMGRESHWIGLTDSEQESEWKWLDGTP-VDYKNWKAG 693
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLlkKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 71043880 694 QPDNwgsghGPGEDCAGLIY--AGQWNDFQCDEINNFICEK 732
Cdd:cd00037  81 EPNP-----GGSEDCVVLSSssDGKWNDVSCSSKLPFICEK 116

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880   625 KEIFEDAKLFCEDKSSHLVFINSREEQQWIKKQTMGR-ESHWIGLTDSEQESEWKWLDGTPVDYKNWKAgqpdnWGSGHG 703
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-----EPNNNG 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 71043880   704 PGEDCAGLIYA-GQWNDFQCDEINNFICEK 732
Cdd:pfam00059  76 ENEDCVELSSSsGKWNDENCNSKNPFVCEK 105

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880 619 YYFSVEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKQTMGRESHWIGLTDSEQESEWKWLDGTPVDYKNWKAGQPDNW 698
Cdd:cd03603   3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNN 82

                        90       100       110
                ....*....|....*....|....*....|....
gi 71043880 699 GSGhgpGEDCAGLIYA----GQWNDFQCDEINNF 728
Cdd:cd03603  83 GGG---NEDYAAINHFpgisGKWNDLANSYNTLG 113

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880 616 DKCYYFSVEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKK-QTMGRESHWIGLTDSEQESEWKWLDGTPVDYKNWKAGQ 694
Cdd:cd03591   1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASyVKKGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGE 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 71043880 695 PDNwgsgHGPGEDCAGLIYAGQWNDFQCDEINNFICE 731
Cdd:cd03591  81 PNN----AGGGEDCVEMYTSGKWNDVACNLTRLFVCE 113

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 71043880 619 YYFSVEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKQTMGRES--HWIGLTDSEQEseWKWLD--GTPVDYKNWKAGQ 694
Cdd:cd03592   3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLgyYWIDGNDINNE--GTWVDtdKKELEYKNWAPGE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 71043880 695 PDNWGsghgpGEDCA-GLIYA-GQWNDFQCDEINNFICEK 732
Cdd:cd03592  81 PNNGR-----NENCLeIYIKDnGKWNDEPCSKKKSAICYT 115

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 71043880 618 CY---YF--SVEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKK--QTMGRES--HWIGLTDSEQ--------ESEWKWL 680
Cdd:cd03595  12 CYkiaYFqdSRRRLNFEEARQACREDGGELLSIESENEQKLIERfiQTLRASDgdFWIGLRRSSQynvtssacSSLYYWL 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71043880 681 DGTPVDYKNWKAGQPdNWGSghgpgEDCAGLIY-----AG-------QWNDFQCDEINNFICE 731
Cdd:cd03595  92 DGSISTFRNWYVDEP-SCGS-----EVCVVMYHqpsapAGqggpylfQWNDDNCNMKNNFICK 148

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880 620 YFSVEKEIFEDAKLFCEDKSSHLVFINSR--EEQQWIKKQTMGR-ESHWIGLTDSEQ-ESEWKWLDGT--PVDYKNWKAG 693
Cdd:cd03601   4 LCSDETMNYAKAGAFCRSRGMRLASLAMRdsEMRDAILAFTLVKgHGYWVGADNLQDgEYDFLWNDGVslPTDSDLWAPN 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 71043880 694 QPDNWGSghgpGEDCAGLIYA-GQWNDFQCDEINNFICEK 732
Cdd:cd03601  84 EPSNPQS----RQLCVQLWSKyNLLDDEYCGRAKRVICEK 119

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71043880   454 RGSQGPPGPTGNKGQKgekgepgppgpagergtiGPVGPPGERGSKGSKGSQGPKGSRGSPG 515
Cdd:pfam01391   9 PGPPGPPGPPGPPGPP------------------GPPGPPGEPGPPGPPGPPGPPGPPGAPG 52

mechanosensitive channel MscK;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880    85 AVESDLKKLGDQ----TGKKALSTNSE--LSTF------RSDILDLRQQLQEITEKTSKNKDMLEKLQANGD-------- 144
Cdd:PRK11281   40 DVQAQLDALNKQklleAEDKLVQQDLEqtLALLdkidrqKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDeetretls 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880   145 --SLVDRQSQLKETLQNnsflITTVNKTLQAYNGYVTNLQQDTSvlqgNLQSQMYSQNVVIMNLNN-------------- 208
Cdd:PRK11281  120 tlSLRQLESRLAQTLDQ----LQNAQNDLAEYNSQLVSLQTQPE----RAQAALYANSQRLQQIRNllkggkvggkalrp 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880   209 ------------LNLTQVQQRNLITN-------LQRSVDDTSLAIQQIKNDFQNLQQVFLQakkdtdwlKEKVQSLQTL- 268
Cdd:PRK11281  192 sqrvllqaeqalLNAQNDLQRKSLEGntqlqdlLQKQRDYLTARIQRLEHQLQLLQEAINS--------KRLTLSEKTVq 263

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 71043880   269 -AANNSALAKANNDTL----EDMNNQLSSF-TGQMDNITTISQAN 307
Cdd:PRK11281  264 eAQSQDEAARIQANPLvaqeLEINLQLSQRlLKATEKLNTLTQQN 308

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880  454 RGSQGPPGPTGNKGQKGEKGEPGPPGPAGERGTIGPVGPPGERGSKGSKGSQGPKGSRGSPGKPGPQGPSGDPGPPGPP- 532
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQg 207

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 71043880  533 -------GKDGLPGPQGPPGFQGLQGTVGEPGVPGPRG 563
Cdd:NF038329 208 pagpagpDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTG 245

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880 113 SDILDLRQQLQEITEKTSKNKDMLEKLQANGDSLVDRQSQLKETLQNNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNL 192
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880 193 QSQ-------------MYSQNVVIMNLNNLNLTQVQQRnlITNLQRSVDDTSLAIQQIKNDFQNLQQVFLQAKKDTDWLK 259
Cdd:COG4942 100 EAQkeelaellralyrLGRQPPLALLLSPEDFLDAVRR--LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71043880 260 EKVQSLQTLAANNSALAKANNDTLEDMNNQLSSFTGQMDNITTISQANEQSMKDLQDLHKDTENRTA 326
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880  455 GSQGPPGPTGNKGQKGEKGEPGPPGPAGERGTIGPVGPP-----GERGSKGSKGSQGPKGSRGSPGKPGPQGPSGDPGPP 529
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                         90       100       110
                 ....*....|....*....|....*....|....
gi 71043880  530 GPPGKDGLPGPQGPPGFQGLQGTVGEPGVPGPRG 563
Cdd:NF038329 272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305

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 71043880 607 CPPHWKNFTDKCYYFSVEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKQTMGRE------SHWIGLTDSEQeSEWKWL 680
Cdd:cd03597   1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQmtkqklTPWVGLRKINV-SYWCWE 79

                        90       100
                ....*....|....*....|...
gi 71043880 681 DGTPvdYKN----WKAGQPDNWG 699
Cdd:cd03597  80 DMSP--FTNttlqWLPGEPSDAG 100

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880   117 DLRQQLQEITEKTSKNKDMLEKLQANGDSLVDRQSQLKETLQNNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNLQSQM 196
Cdd:pfam06008  23 NLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEIN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71043880   197 YSqnVVIMNLNNLNLTQVQQRNLITNLQRsvddtSLAIQQIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALA 276
Cdd:pfam06008 103 EK--VATLGENDFALPSSDLSRMLAEAQR-----MLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALA 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 71043880   277 KANNDTLEDMNNQLSSF-------TGQMDNITTISQANEQSMKDLQD 316
Cdd:pfam06008 176 NALRDSLAEYEAKLSDLrellreaAAKTRDANRLNLANQANLREFQR 222