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Conserved domains on  [gi|144446030|ref|NP_002340|]
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lymphocyte antigen 75 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
beta-trefoil_Ricin_LY75 cd23411
ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and ...
32-145 2.72e-56

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


:

Pssm-ID: 467789  Cd Length: 116  Bit Score: 190.72  E-value: 2.72e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   32 ANDPFTIVHGNTGKCIKPVYGWIVADDCDE-TEDKLWKWVSQHRLFHLHSQKCLGLDITKSVNELRMFSCDS-SAMLWWK 109
Cdd:cd23411     1 GNDIFTIQHENSGKCLKVENSQISAVDCKQsSESLQWKWVSEHRLFNLGSKQCLGLDITKPSNTLKMFECDSkSVMLWWR 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 144446030  110 CEHHSLYGAARYRLALKDGHGTAISNASDVWKKGGS 145
Cdd:cd23411    81 CEGGSLYGASQYRLAVKNGSVTASIDSNDTWKKGGS 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
361-486 1.50e-28

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


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 111.92  E-value: 1.50e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    361 CDAGWLPNNGFCYLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEDIKEEVWIGLKNINIPTLFQWSDGT 440
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWIGLSDPDSNGSWQWSDGS 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 144446030    441 E-VTLTYWDENEPNvpyNKTPNCVSYLGELGQWKVQSCEEKLKYVCK 486
Cdd:smart00034   81 GpVSYSNWAPGEPN---NSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
216-340 4.53e-27

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


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 107.69  E-value: 4.53e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    216 CEDNWEKNEqfGSCYQFNTqTALSWKEAYVSCQNQGADLLSINSAAELTYLKE---KEGIAKIFWIGLNQLYSARGWEWS 292
Cdd:smart00034    1 CPSGWISYG--GKCYKFST-EKKTWEDAQAFCQSLGGHLASIHSEAENDFVASllkNSGSSDYYWIGLSDPDSNGSWQWS 77
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 144446030    293 DHKPL-NFLNWDPDRPSAptiGGSSCARMDAESGLWQSFSCEAQLPYVC 340
Cdd:smart00034   78 DGSGPvSYSNWAPGEPNN---SSGDCVVLSTSGGKWNDVSCTSKLPFVC 123
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1539-1660 6.66e-20

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


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 87.27  E-value: 6.66e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   1539 WIQYKGHCYKSDQALHSFSEAKKLCSKhdHSATIVSIKDEDENKFVSRLMRENNNITMrVWLGLSQHSVDQSWSWLDGSE 1618
Cdd:smart00034    5 WISYGGKCYKFSTEKKTWEDAQAFCQS--LGGHLASIHSEAENDFVASLLKNSGSSDY-YWIGLSDPDSNGSWQWSDGSG 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 144446030   1619 -VTFVKW-ENKSKSGVGRCSMLIASNETWKKVECEHGFgRVVCK 1660
Cdd:smart00034   82 pVSYSNWaPGEPNNSSGDCVVLSTSGGKWNDVSCTSKL-PFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
951-1090 1.79e-19

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


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 85.73  E-value: 1.79e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    951 CSEQWIPFQNKCFlKIKPVSLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPD--MEATLWIGLRWTAYEKINKWTDN 1028
Cdd:smart00034    1 CPSGWISYGGKCY-KFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgSSDYYWIGLSDPDSNGSWQWSDG 79
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 144446030   1029 RELT-YSNFHPllvsgrlripenFFEEESRYHCALIlnlqkSPFTGTWNFTSCSERHFvSLCQ 1090
Cdd:smart00034   80 SGPVsYSNWAP------------GEPNNSSGDCVVL-----STSGGKWNDVSCTSKLP-FVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
643-791 3.06e-19

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


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 85.34  E-value: 3.06e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    643 CPEGWQSFpaSLSCYKVFHaerivRKRNWEEAERFCQALGAHLSSFSHVDEIKeFLHFLTDQFSGQHWLWIGLNKRSPDl 722
Cdd:smart00034    1 CPSGWISY--GGKCYKFST-----EKKTWEDAQAFCQSLGGHLASIHSEAEND-FVASLLKNSGSSDYYWIGLSDPDSN- 71
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 144446030    723 qGSWQWSDRTPVSTIIMPNEFQQDYDIRDCAAVKVFhrpwRRGWHFYDdrefiylrpfaCDTKLEWVCQ 791
Cdd:smart00034   72 -GSWQWSDGSGPVSYSNWAPGEPNNSSGDCVVLSTS----GGKWNDVS-----------CTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1115-1222 1.21e-18

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


:

Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 83.05  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1115 YKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLSVQALLHNSS-LWIGLFSQDDELNFGWSDG-KRLHFSRWAE--- 1189
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSEGTWKWSDGsPLVDYTNWAPgep 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 144446030 1190 TNGQLEDCVVLDT--DGFWKTVDCNDNQPgAICYY 1222
Cdd:cd00037    83 NPGGSEDCVVLSSssDGKWNDVSCSSKLP-FICEK 116
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
162-209 5.92e-18

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


:

Pssm-ID: 128373  Cd Length: 49  Bit Score: 78.88  E-value: 5.92e-18
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 144446030    162 GNSYGRPCEFPFLIDGTWHHDCILDEDHSG-PWCATTLNYEYDRKWGIC 209
Cdd:smart00059    1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGmLWCSTTPNYDRDGKWGFC 49
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1406-1513 1.10e-17

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


:

Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 80.36  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1406 YSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDG-FPLWVGLsSHDGSESSFEWSDGST-FDYIPWK--- 1480
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSsSDVWIGL-NDLSSEGTWKWSDGSPlVDYTNWApge 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 144446030 1481 -GQTSPGNCVLL--DPKGTWKHEKCNSvKDGAICYK 1513
Cdd:cd00037    82 pNPGGSEDCVVLssSSDGKWNDVSCSS-KLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
501-624 7.63e-17

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


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 78.41  E-value: 7.63e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    501 CPPdeGWKRHGETCYKIYEDEVPF---GTNCN------LTITSRFEQEYLNDLMKKYDKSlrKYFWTGLRDVDSCGEYNW 571
Cdd:smart00034    1 CPS--GWISYGGKCYKFSTEKKTWedaQAFCQslgghlASIHSEAENDFVASLLKNSGSS--DYYWIGLSDPDSNGSWQW 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 144446030    572 ATVGGrrrAVTFSNWNFLEP-ASPGGCVAMSTGKsvGKWEVKDCRSfKALSICK 624
Cdd:smart00034   77 SDGSG---PVSYSNWAPGEPnNSSGDCVVLSTSG--GKWNDVSCTS-KLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1239-1359 2.38e-12

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


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 65.70  E-value: 2.38e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   1239 CPSPvlntpWIPFQNCCYNFIITKNrhmatTQDEVHTKCQKLNpkSHILSIRDEKENNFVLEQL-LYFNYMASWVMLGIT 1317
Cdd:smart00034    1 CPSG-----WISYGGKCYKFSTEKK-----TWEDAQAFCQSLG--GHLASIHSEAENDFVASLLkNSGSSDYYWIGLSDP 68
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 144446030   1318 YRNKSLMWFDKTPL-SYTHWRAGRPTIKNEKFLAGLSTDGFWD 1359
Cdd:smart00034   69 DSNGSWQWSDGSGPvSYSNWAPGEPNNSSGDCVVLSTSGGKWN 111
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
821-932 2.06e-08

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


:

Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 54.16  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  821 SEYWFVADlHLNYEEAVLYCASNHSFLATITSFVGLKAIKNKIANisGDGQKWWIRISEWPIDDHF---------TYSRY 891
Cdd:cd00037     1 SCYKFSTE-KLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKK--SSSSDVWIGLNDLSSEGTWkwsdgsplvDYTNW 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 144446030  892 PWHRFPVTFGEECLYMSAKT---WlidlgKPTDCSTKLPFICEK 932
Cdd:cd00037    78 APGEPNPGGSEDCVVLSSSSdgkW-----NDVSCSSKLPFICEK 116
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_LY75 cd23411
ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and ...
32-145 2.72e-56

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


Pssm-ID: 467789  Cd Length: 116  Bit Score: 190.72  E-value: 2.72e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   32 ANDPFTIVHGNTGKCIKPVYGWIVADDCDE-TEDKLWKWVSQHRLFHLHSQKCLGLDITKSVNELRMFSCDS-SAMLWWK 109
Cdd:cd23411     1 GNDIFTIQHENSGKCLKVENSQISAVDCKQsSESLQWKWVSEHRLFNLGSKQCLGLDITKPSNTLKMFECDSkSVMLWWR 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 144446030  110 CEHHSLYGAARYRLALKDGHGTAISNASDVWKKGGS 145
Cdd:cd23411    81 CEGGSLYGASQYRLAVKNGSVTASIDSNDTWKKGGS 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
361-486 1.50e-28

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 111.92  E-value: 1.50e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    361 CDAGWLPNNGFCYLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEDIKEEVWIGLKNINIPTLFQWSDGT 440
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWIGLSDPDSNGSWQWSDGS 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 144446030    441 E-VTLTYWDENEPNvpyNKTPNCVSYLGELGQWKVQSCEEKLKYVCK 486
Cdd:smart00034   81 GpVSYSNWAPGEPN---NSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
216-340 4.53e-27

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 107.69  E-value: 4.53e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    216 CEDNWEKNEqfGSCYQFNTqTALSWKEAYVSCQNQGADLLSINSAAELTYLKE---KEGIAKIFWIGLNQLYSARGWEWS 292
Cdd:smart00034    1 CPSGWISYG--GKCYKFST-EKKTWEDAQAFCQSLGGHLASIHSEAENDFVASllkNSGSSDYYWIGLSDPDSNGSWQWS 77
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 144446030    293 DHKPL-NFLNWDPDRPSAptiGGSSCARMDAESGLWQSFSCEAQLPYVC 340
Cdd:smart00034   78 DGSGPvSYSNWAPGEPNN---SSGDCVVLSTSGGKWNDVSCTSKLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
228-342 5.09e-24

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 98.46  E-value: 5.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  228 SCYQFNTQTaLSWKEAYVSCQNQGADLLSINSAAELTYLKE--KEGIAKIFWIGLNQLYSARGWEWSDHKP-LNFLNWDP 304
Cdd:cd00037     1 SCYKFSTEK-LTWEEAQEYCRSLGGHLASIHSEEENDFLASllKKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAP 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 144446030  305 DRPSAPtiGGSSCARMDA-ESGLWQSFSCEAQLPYVCRK 342
Cdd:cd00037    80 GEPNPG--GSEDCVVLSSsSDGKWNDVSCSSKLPFICEK 116
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
371-487 4.30e-22

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 93.07  E-value: 4.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  371 FCYLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEDiKEEVWIGLKNINIPTLFQWSDGTE-VTLTYWDE 449
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSS-SSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAP 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 144446030  450 NEPNvpYNKTPNCVS-YLGELGQWKVQSCEEKLKYVCKR 487
Cdd:cd00037    80 GEPN--PGGSEDCVVlSSSSDGKWNDVSCSSKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1539-1660 6.66e-20

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 87.27  E-value: 6.66e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   1539 WIQYKGHCYKSDQALHSFSEAKKLCSKhdHSATIVSIKDEDENKFVSRLMRENNNITMrVWLGLSQHSVDQSWSWLDGSE 1618
Cdd:smart00034    5 WISYGGKCYKFSTEKKTWEDAQAFCQS--LGGHLASIHSEAENDFVASLLKNSGSSDY-YWIGLSDPDSNGSWQWSDGSG 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 144446030   1619 -VTFVKW-ENKSKSGVGRCSMLIASNETWKKVECEHGFgRVVCK 1660
Cdd:smart00034   82 pVSYSNWaPGEPNNSSGDCVVLSTSGGKWNDVSCTSKL-PFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
951-1090 1.79e-19

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 85.73  E-value: 1.79e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    951 CSEQWIPFQNKCFlKIKPVSLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPD--MEATLWIGLRWTAYEKINKWTDN 1028
Cdd:smart00034    1 CPSGWISYGGKCY-KFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgSSDYYWIGLSDPDSNGSWQWSDG 79
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 144446030   1029 RELT-YSNFHPllvsgrlripenFFEEESRYHCALIlnlqkSPFTGTWNFTSCSERHFvSLCQ 1090
Cdd:smart00034   80 SGPVsYSNWAP------------GEPNNSSGDCVVL-----STSGGKWNDVSCTSKLP-FVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
643-791 3.06e-19

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 85.34  E-value: 3.06e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    643 CPEGWQSFpaSLSCYKVFHaerivRKRNWEEAERFCQALGAHLSSFSHVDEIKeFLHFLTDQFSGQHWLWIGLNKRSPDl 722
Cdd:smart00034    1 CPSGWISY--GGKCYKFST-----EKKTWEDAQAFCQSLGGHLASIHSEAEND-FVASLLKNSGSSDYYWIGLSDPDSN- 71
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 144446030    723 qGSWQWSDRTPVSTIIMPNEFQQDYDIRDCAAVKVFhrpwRRGWHFYDdrefiylrpfaCDTKLEWVCQ 791
Cdd:smart00034   72 -GSWQWSDGSGPVSYSNWAPGEPNNSSGDCVVLSTS----GGKWNDVS-----------CTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1115-1222 1.21e-18

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 83.05  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1115 YKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLSVQALLHNSS-LWIGLFSQDDELNFGWSDG-KRLHFSRWAE--- 1189
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSEGTWKWSDGsPLVDYTNWAPgep 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 144446030 1190 TNGQLEDCVVLDT--DGFWKTVDCNDNQPgAICYY 1222
Cdd:cd00037    83 NPGGSEDCVVLSSssDGKWNDVSCSSKLP-FICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1108-1220 3.05e-18

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 82.26  E-value: 3.05e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   1108 VKYLNNLYKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLS--VQALLHNSSLWIGLFSQDDELNFGWSDGKRL-HF 1184
Cdd:smart00034    6 ISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGSGPvSY 85
                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 144446030   1185 SRWA--ETNGQLEDCVVLDTD-GFWKTVDCNDNQPgAIC 1220
Cdd:smart00034   86 SNWApgEPNNSSGDCVVLSTSgGKWNDVSCTSKLP-FVC 123
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
162-209 5.92e-18

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


Pssm-ID: 128373  Cd Length: 49  Bit Score: 78.88  E-value: 5.92e-18
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 144446030    162 GNSYGRPCEFPFLIDGTWHHDCILDEDHSG-PWCATTLNYEYDRKWGIC 209
Cdd:smart00059    1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGmLWCSTTPNYDRDGKWGFC 49
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1406-1513 1.10e-17

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 80.36  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1406 YSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDG-FPLWVGLsSHDGSESSFEWSDGST-FDYIPWK--- 1480
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSsSDVWIGL-NDLSSEGTWKWSDGSPlVDYTNWApge 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 144446030 1481 -GQTSPGNCVLL--DPKGTWKHEKCNSvKDGAICYK 1513
Cdd:cd00037    82 pNPGGSEDCVVLssSSDGKWNDVSCSS-KLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
1121-1222 1.83e-17

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 79.44  E-value: 1.83e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  1121 TLTWHSAKRECLKSNMQLVSITDPYQQAFLSVQALLHNSSLWIGLFSQDDELNFGWSDGKRLHFSRWAE---TNGQLEDC 1197
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPepnNNGENEDC 80
                           90       100
                   ....*....|....*....|....*.
gi 144446030  1198 VVLD-TDGFWKTVDCNdNQPGAICYY 1222
Cdd:pfam00059   81 VELSsSSGKWNDENCN-SKNPFVCEK 105
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
1412-1513 6.18e-17

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 77.90  E-value: 6.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  1412 KVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGFPLWVGLSSHDgSESSFEWSDGSTFDYIPWKGQTSP----GN 1487
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRK-NEGTWKWVDGSPVNYTNWAPEPNNngenED 79
                           90       100
                   ....*....|....*....|....*..
gi 144446030  1488 CVLLDPK-GTWKHEKCNSVKdGAICYK 1513
Cdd:pfam00059   80 CVELSSSsGKWNDENCNSKN-PFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
501-624 7.63e-17

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 78.41  E-value: 7.63e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    501 CPPdeGWKRHGETCYKIYEDEVPF---GTNCN------LTITSRFEQEYLNDLMKKYDKSlrKYFWTGLRDVDSCGEYNW 571
Cdd:smart00034    1 CPS--GWISYGGKCYKFSTEKKTWedaQAFCQslgghlASIHSEAENDFVASLLKNSGSS--DYYWIGLSDPDSNGSWQW 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 144446030    572 ATVGGrrrAVTFSNWNFLEP-ASPGGCVAMSTGKsvGKWEVKDCRSfKALSICK 624
Cdd:smart00034   77 SDGSG---PVSYSNWAPGEPnNSSGDCVVLSTSG--GKWNDVSCTS-KLPFVCE 124
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
163-209 1.69e-16

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 74.65  E-value: 1.69e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 144446030  163 NSYGRPCEFPFLIDGTWHHDCILDEDHSG-PWCATTLNYEYDRKWGIC 209
Cdd:cd00062     1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGkLWCSTTPNYDRDGKWGYC 48
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
237-342 1.78e-16

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 76.75  E-value: 1.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   237 ALSWKEAYVSCQNQGADLLSINSAAELTYL-KEKEGIAKIFWIGLNQLYSARGWEWSDHKPLNFLNWDPDRPSAPtiGGS 315
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLsSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNG--ENE 78
                           90       100
                   ....*....|....*....|....*..
gi 144446030   316 SCARMDAESGLWQSFSCEAQLPYVCRK 342
Cdd:pfam00059   79 DCVELSSSSGKWNDENCNSKNPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1398-1511 8.97e-16

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 75.33  E-value: 8.97e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   1398 FMPYEDGIYSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGFP--LWVGLSSHDgSESSFEWSDGS-TF 1474
Cdd:smart00034    5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPD-SNGSWQWSDGSgPV 83
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 144446030   1475 DYIPWKG---QTSPGNCVLLDPK-GTWKHEKCNSvKDGAIC 1511
Cdd:smart00034   84 SYSNWAPgepNNSSGDCVVLSTSgGKWNDVSCTS-KLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
655-792 9.57e-16

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 74.96  E-value: 9.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  655 SCYKVFHaerivRKRNWEEAERFCQALGAHLSSFSHVDEIkEFLHFLTDQFSGQHWlWIGLNKRSPDlqGSWQWSDRTPV 734
Cdd:cd00037     1 SCYKFST-----EKLTWEEAQEYCRSLGGHLASIHSEEEN-DFLASLLKKSSSSDV-WIGLNDLSSE--GTWKWSDGSPL 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 144446030  735 STIIMPNEFQQDYD-IRDCAavkVFHRPWRRGWHFYDdrefiylrpfaCDTKLEWVCQI 792
Cdd:cd00037    72 VDYTNWAPGEPNPGgSEDCV---VLSSSSDGKWNDVS-----------CSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
379-487 7.47e-15

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 72.13  E-value: 7.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   379 SNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNedIKEEVWIGLKNINIPTLFQWSDGTEVTLTYWDENEPNvpYNK 458
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKK--SNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNN--NGE 76
                           90       100
                   ....*....|....*....|....*....
gi 144446030   459 TPNCVSYLGELGQWKVQSCEEKLKYVCKR 487
Cdd:pfam00059   77 NEDCVELSSSSGKWNDENCNSKNPFVCEK 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1545-1661 1.62e-14

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 71.50  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1545 HCYKSDQALHSFSEAKKLCskHDHSATIVSIKDEDENKFVSRLMRENNNItmRVWLGLSQHSVDQSWSWLDGSE-VTFVK 1623
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYC--RSLGGHLASIHSEEENDFLASLLKKSSSS--DVWIGLNDLSSEGTWKWSDGSPlVDYTN 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 144446030 1624 W--ENKSKSGVGRC-SMLIASNETWKKVECEHGFGrVVCKV 1661
Cdd:cd00037    77 WapGEPNPGGSEDCvVLSSSSDGKWNDVSCSSKLP-FICEK 116
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
961-1091 3.38e-14

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 70.73  E-value: 3.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  961 KCFlKIKPVSLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPDMEAT-LWIGLRWTAYEKINKWTDN-RELTYSNFHP 1038
Cdd:cd00037     1 SCY-KFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSEGTWKWSDGsPLVDYTNWAP 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 144446030 1039 LlvsgrlrIPENFFEEesryHCALIlnlqKSPFTGTWNFTSCSERHFVsLCQK 1091
Cdd:cd00037    80 G-------EPNPGGSE----DCVVL----SSSSDGKWNDVSCSSKLPF-ICEK 116
fn2 pfam00040
Fibronectin type II domain;
169-209 1.25e-13

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 66.44  E-value: 1.25e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 144446030   169 CEFPFLIDGTWHHDCILDEDHSG-PWCATTLNYEYDRKWGIC 209
Cdd:pfam00040    1 CVFPFKYKGKWYHTCTTDGRRSGrLWCATTANYDGDGKWGYC 42
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
970-1091 5.95e-13

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 66.73  E-value: 5.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   970 SLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPDMEATLWIGLRWTAYEKINKWTDNRELTYSNFHPLLVSGRlripe 1049
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNG----- 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 144446030  1050 nffeeeSRYHCALIlnlqkSPFTGTWNFTSCSERHFVsLCQK 1091
Cdd:pfam00059   76 ------ENEDCVEL-----SSSSGKWNDENCNSKNPF-VCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1239-1359 2.38e-12

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 65.70  E-value: 2.38e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   1239 CPSPvlntpWIPFQNCCYNFIITKNrhmatTQDEVHTKCQKLNpkSHILSIRDEKENNFVLEQL-LYFNYMASWVMLGIT 1317
Cdd:smart00034    1 CPSG-----WISYGGKCYKFSTEKK-----TWEDAQAFCQSLG--GHLASIHSEAENDFVASLLkNSGSSDYYWIGLSDP 68
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 144446030   1318 YRNKSLMWFDKTPL-SYTHWRAGRPTIKNEKFLAGLSTDGFWD 1359
Cdd:smart00034   69 DSNGSWQWSDGSGPvSYSNWAPGEPNNSSGDCVVLSTSGGKWN 111
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
514-625 1.15e-11

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 63.41  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  514 CYKIYEDEVPFG---TNCN------LTITSRFEQEYLNDLMKKYDKSlrkYFWTGLRDVDSCGEYNWATvggRRRAVTFS 584
Cdd:cd00037     2 CYKFSTEKLTWEeaqEYCRslgghlASIHSEEENDFLASLLKKSSSS---DVWIGLNDLSSEGTWKWSD---GSPLVDYT 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 144446030  585 NWNFLEPASPGG--CVAMSTGKSvGKWEVKDCrSFKALSICKK 625
Cdd:cd00037    76 NWAPGEPNPGGSedCVVLSSSSD-GKWNDVSC-SSKLPFICEK 116
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1255-1359 5.52e-10

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 58.40  E-value: 5.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1255 CYNFIITKnrhmaTTQDEVHTKCQKLNpkSHILSIRDEKENNFVLEQLLYFNYMASWVMLGITYRNKSLMWFDKTP-LSY 1333
Cdd:cd00037     2 CYKFSTEK-----LTWEEAQEYCRSLG--GHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDY 74
                          90       100
                  ....*....|....*....|....*...
gi 144446030 1334 THWRAGRPTIKNEKFLAGL--STDGFWD 1359
Cdd:cd00037    75 TNWAPGEPNPGGSEDCVVLssSSDGKWN 102
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
1554-1660 5.06e-09

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 55.56  E-value: 5.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  1554 HSFSEAKKLCSKHdhSATIVSIKDEDENKFVSRLMRENNNitmRVWLGLSQHSVDQSWSWLDGSEVTFVKWENKSKSGVG 1633
Cdd:pfam00059    2 KTWDEAREACRKL--GGHLVSINSAEELDFLSSTLKKSNK---YFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGE 76
                           90       100       110
                   ....*....|....*....|....*....|.
gi 144446030  1634 R--CSMLIASNETWKKVECE--HGFgrvVCK 1660
Cdd:pfam00059   77 NedCVELSSSSGKWNDENCNskNPF---VCE 104
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
821-932 2.06e-08

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 54.16  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  821 SEYWFVADlHLNYEEAVLYCASNHSFLATITSFVGLKAIKNKIANisGDGQKWWIRISEWPIDDHF---------TYSRY 891
Cdd:cd00037     1 SCYKFSTE-KLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKK--SSSSDVWIGLNDLSSEGTWkwsdgsplvDYTNW 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 144446030  892 PWHRFPVTFGEECLYMSAKT---WlidlgKPTDCSTKLPFICEK 932
Cdd:cd00037    78 APGEPNPGGSEDCVVLSSSSdgkW-----NDVSCSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
530-625 2.14e-07

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 50.94  E-value: 2.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   530 LTITSRFEQEYLNDLMKKYDKslrkYFWTGLRDVDSCGEYNWatVGGRRraVTFSNWNFLEPASPGG--CVAMStgKSVG 607
Cdd:pfam00059   19 VSINSAEELDFLSSTLKKSNK----YFWIGLTDRKNEGTWKW--VDGSP--VNYTNWAPEPNNNGENedCVELS--SSSG 88
                           90
                   ....*....|....*...
gi 144446030   608 KWEVKDCrSFKALSICKK 625
Cdd:pfam00059   89 KWNDENC-NSKNPFVCEK 105
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
831-932 1.53e-06

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 48.24  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   831 LNYEEAVLYCASNHSFLATITSFVGLKAIKNKIANisgDGQKWWIRIS--------EWPIDDHFTYSryPWHRFP--VTF 900
Cdd:pfam00059    2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKK---SNKYFWIGLTdrknegtwKWVDGSPVNYT--NWAPEPnnNGE 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 144446030   901 GEECLYMSAKTWLIDLgkpTDCSTKLPFICEK 932
Cdd:pfam00059   77 NEDCVELSSSSGKWND---ENCNSKNPFVCEK 105
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
38-112 2.62e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 47.89  E-value: 2.62e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 144446030     38 IVHGNTGKCI--KPVYGWIVADDCDETED-KLWKWVSQHRLFHLHSQKCLGLDITKSVNeLRMFSCDSSA-MLWWKCEH 112
Cdd:smart00458    1 IISGNTGKCLdvNGNKNPVGLFDCHGTGGnQLWKLTSDGAIRIKDTDLCLTANGNTGST-VTLYSCDGTNdNQYWEVNK 78
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
820-931 4.80e-06

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 47.59  E-value: 4.80e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    820 GSEYWFVADLhLNYEEAVLYCASNHSFLATITSFVGLKAIKNKIANISGDGQkWWI------RISEWPIDDHFTYSRYP- 892
Cdd:smart00034   10 GKCYKFSTEK-KTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDY-YWIglsdpdSNGSWQWSDGSGPVSYSn 87
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 144446030    893 WHR-FPVTFGEECLYMSAKTWLIDlgkPTDCSTKLPFICE 931
Cdd:smart00034   88 WAPgEPNNSSGDCVVLSTSGGKWN---DVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
668-791 5.96e-06

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 46.70  E-value: 5.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   668 KRNWEEAERFCQALGAHLSSFSHVDEIKEFLHFLTDQFSGqhwLWIGLNKRspDLQGSWQWSDRTPVSTIIMPNEFQQDY 747
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY---FWIGLTDR--KNEGTWKWVDGSPVNYTNWAPEPNNNG 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 144446030   748 DIRDCAAVkvfHRPWRRgWHFYDdrefiylrpfaCDTKLEWVCQ 791
Cdd:pfam00059   76 ENEDCVEL---SSSSGK-WNDEN-----------CNSKNPFVCE 104
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
367-486 1.88e-05

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


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 50.08  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   367 PNNGFCYLLVNESNSWDKAHAKCKAFS-SDLISIHSLADVEVVVTKLhNEDIKEEVWIGLKNINIPTLFQWSDGTEVTLT 445
Cdd:TIGR00864  326 EENGHCFQIVPEEAAWLDAQEQCLARAgAALAIVDNDALQNFLARKV-THSLDRGVWIGFSDVNGAEKGPAHQGEAFEAE 404
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 144446030   446 YWDENEPNVPYNKTPN-CVSyLGELGQWKVQSCEEKLKYVCK 486
Cdd:TIGR00864  405 ECEEGLAGEPHPARAEhCVR-LDPRGQCNSDLCNAPHAYVCE 445
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
1269-1347 4.51e-05

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 44.01  E-value: 4.51e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 144446030  1269 TQDEVHTKCQKLNpkSHILSIRDEKENNFVLEQLLYFNYmASWVMLGITYRNKSLMWFDKTPLSYTHWrAGRPTIKNEK 1347
Cdd:pfam00059    3 TWDEAREACRKLG--GHLVSINSAEELDFLSSTLKKSNK-YFWIGLTDRKNEGTWKWVDGSPVNYTNW-APEPNNNGEN 77
PHA02911 PHA02911
C-type lectin-like protein; Provisional
333-489 1.43e-04

C-type lectin-like protein; Provisional


Pssm-ID: 177496 [Multi-domain]  Cd Length: 213  Bit Score: 45.18  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  333 EAQLPYVCRKPLnnTVELTDVWTYSDTRCDAGWLPNNGFCYLLVNESNSWDKAHAK--CKAFSSDLIsihsladvevvvt 410
Cdd:PHA02911   77 EPSIATTCPDNL--TIHCPEVPSPSEPICSRDWINHMGICLLSLGEEVGFRMEIAKrfCEKKDADLI------------- 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  411 KLHNEDIKeevwiGLKNIniptlfqWSdGTEVTlTYW-DENEPNVPYNKTPNCV----SYLGELGQWKVQSCEEKLKYVC 485
Cdd:PHA02911  142 GKIDEEKK-----ALENI-------WT-GNDHS-RFWiDNRAAASTFDPVNECAigtqNHIPEVPEVLKSPCDERHSFIC 207

                  ....
gi 144446030  486 KRKG 489
Cdd:PHA02911  208 IKKD 211
PHA02642 PHA02642
C-type lectin-like protein; Provisional
643-732 2.33e-04

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 44.34  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  643 CPEGWQSFPaslscYKVFHAERivRKRNWEEAERFCQALGAHLSSFshvdEIKEFLHFLTdQFSGQHWLWIGLNKRSPDl 722
Cdd:PHA02642   88 CPKGWIGFG-----YKCFYFSE--DSKNWTFGNTFCTSLGATLVKV----ETEEELNFLK-RYKDSSDHWIGLNRESSN- 154
                          90
                  ....*....|
gi 144446030  723 qGSWQWSDRT 732
Cdd:PHA02642  155 -HPWKWADNS 163
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
1406-1514 1.06e-03

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


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 44.30  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  1406 YSVIQKKVTWYEALNMC-SQSGGHLASVHNQNGQLFLEDIVKRD-GFPLWVGLSSHDGSE-SSFEWSDGSTFD-----YI 1477
Cdd:TIGR00864  332 FQIVPEEAAWLDAQEQClARAGAALAIVDNDALQNFLARKVTHSlDRGVWIGFSDVNGAEkGPAHQGEAFEAEeceegLA 411
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 144446030  1478 PWKGQTSPGNCVLLDPKGTWKHEKCNSVKDGAICYKP 1514
Cdd:TIGR00864  412 GEPHPARAEHCVRLDPRGQCNSDLCNAPHAYVCELNP 448
PHA02642 PHA02642
C-type lectin-like protein; Provisional
229-298 2.51e-03

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 41.25  E-value: 2.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  229 CYQFnTQTALSWKEAYVSCQNQGADLLSINSAAELTYLKEKEGIAKiFWIGLNQLYSARGWEWSDHKPLN 298
Cdd:PHA02642   99 CFYF-SEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSD-HWIGLNRESSNHPWKWADNSNYN 166
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_LY75 cd23411
ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and ...
32-145 2.72e-56

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


Pssm-ID: 467789  Cd Length: 116  Bit Score: 190.72  E-value: 2.72e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   32 ANDPFTIVHGNTGKCIKPVYGWIVADDCDE-TEDKLWKWVSQHRLFHLHSQKCLGLDITKSVNELRMFSCDS-SAMLWWK 109
Cdd:cd23411     1 GNDIFTIQHENSGKCLKVENSQISAVDCKQsSESLQWKWVSEHRLFNLGSKQCLGLDITKPSNTLKMFECDSkSVMLWWR 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 144446030  110 CEHHSLYGAARYRLALKDGHGTAISNASDVWKKGGS 145
Cdd:cd23411    81 CEGGSLYGASQYRLAVKNGSVTASIDSNDTWKKGGS 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
361-486 1.50e-28

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 111.92  E-value: 1.50e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    361 CDAGWLPNNGFCYLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEDIKEEVWIGLKNINIPTLFQWSDGT 440
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWIGLSDPDSNGSWQWSDGS 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 144446030    441 E-VTLTYWDENEPNvpyNKTPNCVSYLGELGQWKVQSCEEKLKYVCK 486
Cdd:smart00034   81 GpVSYSNWAPGEPN---NSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
216-340 4.53e-27

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 107.69  E-value: 4.53e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    216 CEDNWEKNEqfGSCYQFNTqTALSWKEAYVSCQNQGADLLSINSAAELTYLKE---KEGIAKIFWIGLNQLYSARGWEWS 292
Cdd:smart00034    1 CPSGWISYG--GKCYKFST-EKKTWEDAQAFCQSLGGHLASIHSEAENDFVASllkNSGSSDYYWIGLSDPDSNGSWQWS 77
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*....
gi 144446030    293 DHKPL-NFLNWDPDRPSAptiGGSSCARMDAESGLWQSFSCEAQLPYVC 340
Cdd:smart00034   78 DGSGPvSYSNWAPGEPNN---SSGDCVVLSTSGGKWNDVSCTSKLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
228-342 5.09e-24

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 98.46  E-value: 5.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  228 SCYQFNTQTaLSWKEAYVSCQNQGADLLSINSAAELTYLKE--KEGIAKIFWIGLNQLYSARGWEWSDHKP-LNFLNWDP 304
Cdd:cd00037     1 SCYKFSTEK-LTWEEAQEYCRSLGGHLASIHSEEENDFLASllKKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAP 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 144446030  305 DRPSAPtiGGSSCARMDA-ESGLWQSFSCEAQLPYVCRK 342
Cdd:cd00037    80 GEPNPG--GSEDCVVLSSsSDGKWNDVSCSSKLPFICEK 116
beta-trefoil_Ricin_PLA2R1 cd23410
ricin B-type lectin domain, beta-trefoil fold, found in secretory phospholipase A2 receptor ...
34-145 3.83e-22

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


Pssm-ID: 467788  Cd Length: 118  Bit Score: 93.27  E-value: 3.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   34 DPFTIVHGNTGKCIKPVYGWIVADDCDE-TEDKLWKWVSQHRLFHLHSQKCLGLDITKSVNELRMFSCDSS-AMLWWKCE 111
Cdd:cd23410     2 GMFILESESLKKCISADKSGLFLENCDQpSDSMLWKWVSRHRLFNLGSSMCLGLNLSYPQQPLGLFECDSTlRTLWWRCN 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 144446030  112 HHSLYGAARYRLALKDGHGTAISNASDVWKKGGS 145
Cdd:cd23410    82 GKMLIGADQYKLTAVGSKVVASRQSSHKWKPYGS 115
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
371-487 4.30e-22

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 93.07  E-value: 4.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  371 FCYLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEDiKEEVWIGLKNINIPTLFQWSDGTE-VTLTYWDE 449
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSS-SSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAP 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 144446030  450 NEPNvpYNKTPNCVS-YLGELGQWKVQSCEEKLKYVCKR 487
Cdd:cd00037    80 GEPN--PGGSEDCVVlSSSSDGKWNDVSCSSKLPFICEK 116
beta-trefoil_Ricin_MRC-like cd23385
ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...
34-142 1.05e-21

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


Pssm-ID: 467784 [Multi-domain]  Cd Length: 119  Bit Score: 92.28  E-value: 1.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   34 DPFTIVHGNTGKCI--KPVYGWIVADDCDET-EDKLWKWVSQHRLFHLHSQKCLGLDITKSVNELRMFSCDSS-AMLWWK 109
Cdd:cd23385     1 DSFLIYNEDLGKCLaaRSSSSKVSLSTCNPNsPNQQWKWTSGHRLFNVGTGKCLGVSSSSPSSPLRLFECDSEdELQKWK 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 144446030  110 CEHHSLYGAARYRLALKDGHG------TAISNASDVWKK 142
Cdd:cd23385    81 CSKDGLLLLKGLGLLLLYDKSgknvvvSKGSGLSSRWKI 119
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1539-1660 6.66e-20

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 87.27  E-value: 6.66e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   1539 WIQYKGHCYKSDQALHSFSEAKKLCSKhdHSATIVSIKDEDENKFVSRLMRENNNITMrVWLGLSQHSVDQSWSWLDGSE 1618
Cdd:smart00034    5 WISYGGKCYKFSTEKKTWEDAQAFCQS--LGGHLASIHSEAENDFVASLLKNSGSSDY-YWIGLSDPDSNGSWQWSDGSG 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 144446030   1619 -VTFVKW-ENKSKSGVGRCSMLIASNETWKKVECEHGFgRVVCK 1660
Cdd:smart00034   82 pVSYSNWaPGEPNNSSGDCVVLSTSGGKWNDVSCTSKL-PFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
951-1090 1.79e-19

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 85.73  E-value: 1.79e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    951 CSEQWIPFQNKCFlKIKPVSLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPD--MEATLWIGLRWTAYEKINKWTDN 1028
Cdd:smart00034    1 CPSGWISYGGKCY-KFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNsgSSDYYWIGLSDPDSNGSWQWSDG 79
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 144446030   1029 RELT-YSNFHPllvsgrlripenFFEEESRYHCALIlnlqkSPFTGTWNFTSCSERHFvSLCQ 1090
Cdd:smart00034   80 SGPVsYSNWAP------------GEPNNSSGDCVVL-----STSGGKWNDVSCTSKLP-FVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
643-791 3.06e-19

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 85.34  E-value: 3.06e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    643 CPEGWQSFpaSLSCYKVFHaerivRKRNWEEAERFCQALGAHLSSFSHVDEIKeFLHFLTDQFSGQHWLWIGLNKRSPDl 722
Cdd:smart00034    1 CPSGWISY--GGKCYKFST-----EKKTWEDAQAFCQSLGGHLASIHSEAEND-FVASLLKNSGSSDYYWIGLSDPDSN- 71
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 144446030    723 qGSWQWSDRTPVSTIIMPNEFQQDYDIRDCAAVKVFhrpwRRGWHFYDdrefiylrpfaCDTKLEWVCQ 791
Cdd:smart00034   72 -GSWQWSDGSGPVSYSNWAPGEPNNSSGDCVVLSTS----GGKWNDVS-----------CTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1115-1222 1.21e-18

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 83.05  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1115 YKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLSVQALLHNSS-LWIGLFSQDDELNFGWSDG-KRLHFSRWAE--- 1189
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSEGTWKWSDGsPLVDYTNWAPgep 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 144446030 1190 TNGQLEDCVVLDT--DGFWKTVDCNDNQPgAICYY 1222
Cdd:cd00037    83 NPGGSEDCVVLSSssDGKWNDVSCSSKLP-FICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1108-1220 3.05e-18

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 82.26  E-value: 3.05e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   1108 VKYLNNLYKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLS--VQALLHNSSLWIGLFSQDDELNFGWSDGKRL-HF 1184
Cdd:smart00034    6 ISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVAslLKNSGSSDYYWIGLSDPDSNGSWQWSDGSGPvSY 85
                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 144446030   1185 SRWA--ETNGQLEDCVVLDTD-GFWKTVDCNDNQPgAIC 1220
Cdd:smart00034   86 SNWApgEPNNSSGDCVVLSTSgGKWNDVSCTSKLP-FVC 123
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
162-209 5.92e-18

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


Pssm-ID: 128373  Cd Length: 49  Bit Score: 78.88  E-value: 5.92e-18
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 144446030    162 GNSYGRPCEFPFLIDGTWHHDCILDEDHSG-PWCATTLNYEYDRKWGIC 209
Cdd:smart00059    1 GNSDGEPCVFPFIYNGKKYHDCTSEGRSDGmLWCSTTPNYDRDGKWGFC 49
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
216-342 7.29e-18

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


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 81.20  E-value: 7.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  216 CEDNWEKNEqfGSCYQFNTQTaLSWKEAYVSCQNQGADLLSINSAAELTYLKEKEGIAKIFWIGLNQLYSARGWEWSDHK 295
Cdd:cd03590     1 CPTNWKSFQ--SSCYFFSTEK-KSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWKWVDGT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 144446030  296 PLN--FLNWDPDRPSAPTIGGSSCARMDAESGLWQSFSCEAQLPYVCRK 342
Cdd:cd03590    78 PLNssKTFWHPGEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1406-1513 1.10e-17

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 80.36  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1406 YSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDG-FPLWVGLsSHDGSESSFEWSDGST-FDYIPWK--- 1480
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSsSDVWIGL-NDLSSEGTWKWSDGSPlVDYTNWApge 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 144446030 1481 -GQTSPGNCVLL--DPKGTWKHEKCNSvKDGAICYK 1513
Cdd:cd00037    82 pNPGGSEDCVVLssSSDGKWNDVSCSS-KLPFICEK 116
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
227-341 1.54e-17

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


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 80.49  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  227 GSCYQFNTQtALSWKEAYVSCQN--QGADLLSINSAAELT--------YLKEKEGIakifWIGLNQLYSARGWEWSDHKP 296
Cdd:cd03594    10 GNCYGYFRQ-PLSWSDAELFCQKygPGAHLASIHSPAEAAaiaslissYQKAYQPV----WIGLHDPQQSRGWEWSDGSK 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 144446030  297 LNFLNWDPDRPSAptiGGSSCARMDAESG--LWQSFSCEAQLPYVCR 341
Cdd:cd03594    85 LDYRSWDRNPPYA---RGGYCAELSRSTGflKWNDANCEERNPFICK 128
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
1121-1222 1.83e-17

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 79.44  E-value: 1.83e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  1121 TLTWHSAKRECLKSNMQLVSITDPYQQAFLSVQALLHNSSLWIGLFSQDDELNFGWSDGKRLHFSRWAE---TNGQLEDC 1197
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPepnNNGENEDC 80
                           90       100
                   ....*....|....*....|....*.
gi 144446030  1198 VVLD-TDGFWKTVDCNdNQPGAICYY 1222
Cdd:pfam00059   81 VELSsSSGKWNDENCN-SKNPFVCEK 105
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
1412-1513 6.18e-17

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 77.90  E-value: 6.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  1412 KVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGFPLWVGLSSHDgSESSFEWSDGSTFDYIPWKGQTSP----GN 1487
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRK-NEGTWKWVDGSPVNYTNWAPEPNNngenED 79
                           90       100
                   ....*....|....*....|....*..
gi 144446030  1488 CVLLDPK-GTWKHEKCNSVKdGAICYK 1513
Cdd:pfam00059   80 CVELSSSsGKWNDENCNSKN-PFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
501-624 7.63e-17

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 78.41  E-value: 7.63e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    501 CPPdeGWKRHGETCYKIYEDEVPF---GTNCN------LTITSRFEQEYLNDLMKKYDKSlrKYFWTGLRDVDSCGEYNW 571
Cdd:smart00034    1 CPS--GWISYGGKCYKFSTEKKTWedaQAFCQslgghlASIHSEAENDFVASLLKNSGSS--DYYWIGLSDPDSNGSWQW 76
                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 144446030    572 ATVGGrrrAVTFSNWNFLEP-ASPGGCVAMSTGKsvGKWEVKDCRSfKALSICK 624
Cdd:smart00034   77 SDGSG---PVSYSNWAPGEPnNSSGDCVVLSTSG--GKWNDVSCTS-KLPFVCE 124
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
163-209 1.69e-16

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


Pssm-ID: 238019  Cd Length: 48  Bit Score: 74.65  E-value: 1.69e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 144446030  163 NSYGRPCEFPFLIDGTWHHDCILDEDHSG-PWCATTLNYEYDRKWGIC 209
Cdd:cd00062     1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGkLWCSTTPNYDRDGKWGYC 48
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
237-342 1.78e-16

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 76.75  E-value: 1.78e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   237 ALSWKEAYVSCQNQGADLLSINSAAELTYL-KEKEGIAKIFWIGLNQLYSARGWEWSDHKPLNFLNWDPDRPSAPtiGGS 315
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLsSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNG--ENE 78
                           90       100
                   ....*....|....*....|....*..
gi 144446030   316 SCARMDAESGLWQSFSCEAQLPYVCRK 342
Cdd:pfam00059   79 DCVELSSSSGKWNDENCNSKNPFVCEK 105
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
361-486 3.37e-16

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


Pssm-ID: 153059  Cd Length: 137  Bit Score: 77.01  E-value: 3.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  361 CDAGWLPNNGFCYLLVNESNSWDKAHAKCKAFSS-----DLISIHSLADvEVVVTKLHN----EDIKEEVWIGLKNINIP 431
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFSIpgliaHLVSIHSQEE-NDFVYDLFEssrgPDTPYGLWIGLHDRTSE 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 144446030  432 TLFQWSDGTEVTLTYWDENEPNvPYNKTPNCV---SYLGELGQWKVQSCEEKLKYVCK 486
Cdd:cd03589    80 GPFEWTDGSPVDFTKWAGGQPD-NYGGNEDCVqmwRRGDAGQSWNDMPCDAVFPYICK 136
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
361-486 5.94e-16

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


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 75.87  E-value: 5.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  361 CDAGWLPNNGFCYLLVNESNSWDKAHAKCKAF--SSDLISIHSLADVEVV---VTKLHNEDikEEVWIGLKNINIPTLFQ 435
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIaslISSYQKAY--QPVWIGLHDPQQSRGWE 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 144446030  436 WSDGTEVTLTYWDENEpnvPYNKTPNCVSYLGELG--QWKVQSCEEKLKYVCK 486
Cdd:cd03594    79 WSDGSKLDYRSWDRNP---PYARGGYCAELSRSTGflKWNDANCEERNPFICK 128
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1398-1511 8.97e-16

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 75.33  E-value: 8.97e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   1398 FMPYEDGIYSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGFP--LWVGLSSHDgSESSFEWSDGS-TF 1474
Cdd:smart00034    5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPD-SNGSWQWSDGSgPV 83
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|.
gi 144446030   1475 DYIPWKG---QTSPGNCVLLDPK-GTWKHEKCNSvKDGAIC 1511
Cdd:smart00034   84 SYSNWAPgepNNSSGDCVVLSTSgGKWNDVSCTS-KLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
655-792 9.57e-16

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 74.96  E-value: 9.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  655 SCYKVFHaerivRKRNWEEAERFCQALGAHLSSFSHVDEIkEFLHFLTDQFSGQHWlWIGLNKRSPDlqGSWQWSDRTPV 734
Cdd:cd00037     1 SCYKFST-----EKLTWEEAQEYCRSLGGHLASIHSEEEN-DFLASLLKKSSSSDV-WIGLNDLSSE--GTWKWSDGSPL 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 144446030  735 STIIMPNEFQQDYD-IRDCAavkVFHRPWRRGWHFYDdrefiylrpfaCDTKLEWVCQI 792
Cdd:cd00037    72 VDYTNWAPGEPNPGgSEDCV---VLSSSSDGKWNDVS-----------CSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
379-487 7.47e-15

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 72.13  E-value: 7.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   379 SNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNedIKEEVWIGLKNINIPTLFQWSDGTEVTLTYWDENEPNvpYNK 458
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKK--SNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNN--NGE 76
                           90       100
                   ....*....|....*....|....*....
gi 144446030   459 TPNCVSYLGELGQWKVQSCEEKLKYVCKR 487
Cdd:pfam00059   77 NEDCVELSSSSGKWNDENCNSKNPFVCEK 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1545-1661 1.62e-14

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 71.50  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1545 HCYKSDQALHSFSEAKKLCskHDHSATIVSIKDEDENKFVSRLMRENNNItmRVWLGLSQHSVDQSWSWLDGSE-VTFVK 1623
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYC--RSLGGHLASIHSEEENDFLASLLKKSSSS--DVWIGLNDLSSEGTWKWSDGSPlVDYTN 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 144446030 1624 W--ENKSKSGVGRC-SMLIASNETWKKVECEHGFGrVVCKV 1661
Cdd:cd00037    77 WapGEPNPGGSEDCvVLSSSSDGKWNDVSCSSKLP-FICEK 116
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
361-487 2.24e-14

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


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 71.18  E-value: 2.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  361 CDAGWLPNNGFCYLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLhneDIKEEVWIGLKNINIPTLFQWSDGT 440
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKIL---SGNRSYWIGLSDEETEGEWKWVDGT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 144446030  441 --EVTLTYWDENEPNVPYNKTPNCVSYLGELGQWKVQSCEEKLKYVCKR 487
Cdd:cd03590    78 plNSSKTFWHPGEPNNWGGGGEDCAELVYDSGGWNDVPCNLEYRWICEK 126
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
961-1091 3.38e-14

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 70.73  E-value: 3.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  961 KCFlKIKPVSLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPDMEAT-LWIGLRWTAYEKINKWTDN-RELTYSNFHP 1038
Cdd:cd00037     1 SCY-KFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSEGTWKWSDGsPLVDYTNWAP 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 144446030 1039 LlvsgrlrIPENFFEEesryHCALIlnlqKSPFTGTWNFTSCSERHFVsLCQK 1091
Cdd:cd00037    80 G-------EPNPGGSE----DCVVL----SSSSDGKWNDVSCSSKLPF-ICEK 116
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
216-342 6.64e-14

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 69.67  E-value: 6.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  216 CEDNWEKNEqfGSCYQFNTQTaLSWKEAYVSCQNQGADLLSINSAAELTYLKEKEGiAKIFWIGLNQLYSARGWEWSDHK 295
Cdd:cd03593     1 CPKDWICYG--NKCYYFSMEK-KTWNESKEACSSKNSSLLKIDDEEELEFLQSQIG-SSSYWIGLSREKSEKPWKWIDGS 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 144446030  296 PLNflNWDPDRPSAPTiggSSCA-----RMDAEsglwqsfSCEAQLPYVCRK 342
Cdd:cd03593    77 PLN--NLFNIRGSTKS---GNCAylsstGIYSE-------DCSTKKRWICEK 116
fn2 pfam00040
Fibronectin type II domain;
169-209 1.25e-13

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 66.44  E-value: 1.25e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 144446030   169 CEFPFLIDGTWHHDCILDEDHSG-PWCATTLNYEYDRKWGIC 209
Cdd:pfam00040    1 CVFPFKYKGKWYHTCTTDGRRSGrLWCATTANYDGDGKWGYC 42
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
970-1091 5.95e-13

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 66.73  E-value: 5.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   970 SLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPDMEATLWIGLRWTAYEKINKWTDNRELTYSNFHPLLVSGRlripe 1049
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNG----- 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 144446030  1050 nffeeeSRYHCALIlnlqkSPFTGTWNFTSCSERHFVsLCQK 1091
Cdd:pfam00059   76 ------ENEDCVEL-----SSSSGKWNDENCNSKNPF-VCEK 105
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
216-342 7.71e-13

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 66.83  E-value: 7.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  216 CEDNWEKNEqfGSCYQFNTQTAlSWKEAYVSCQNQGADLLSINSAAELTYLKEKEGIAKifWIGLNQLYSARGWEWSDHK 295
Cdd:cd03588     1 CEEGWDKFQ--GHCYRHFPDRE-TWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ--WIGLNDRTIEGDFRWSDGH 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 144446030  296 PLNFLNWDPDRPSAPTIGGSSCARMDA-ESGLWQSFSCEAQLPYVCRK 342
Cdd:cd03588    76 PLQFENWRPNQPDNFFATGEDCVVMIWhEEGEWNDVPCNYHLPFTCKK 123
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
1539-1660 9.75e-13

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


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 66.63  E-value: 9.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1539 WIQYKGHCYKSDQALHSFSEAKKLCSKHDHSATIVSIKDEDENKFVSRLMRENNNITMRVWLGLSQHSVDQSWSWLDGSE 1618
Cdd:cd03594     5 WLPYKGNCYGYFRQPLSWSDAELFCQKYGPGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSRGWEWSDGSK 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 144446030 1619 VTFVKWE-NKSKSGVGRCSMLIASNE--TWKKVECE--HGFgrvVCK 1660
Cdd:cd03594    85 LDYRSWDrNPPYARGGYCAELSRSTGflKWNDANCEerNPF---ICK 128
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
361-487 2.22e-12

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 65.68  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  361 CDAGWLPNNGFCYLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEDikeevWIGLKNINIPTLFQWSDGT 440
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ-----WIGLNDRTIEGDFRWSDGH 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 144446030  441 EVTLTYWDENEPNVPYNKTPNCVSYLG-ELGQWKVQSCEEKLKYVCKR 487
Cdd:cd03588    76 PLQFENWRPNQPDNFFATGEDCVVMIWhEEGEWNDVPCNYHLPFTCKK 123
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
1239-1359 2.38e-12

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 65.70  E-value: 2.38e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   1239 CPSPvlntpWIPFQNCCYNFIITKNrhmatTQDEVHTKCQKLNpkSHILSIRDEKENNFVLEQL-LYFNYMASWVMLGIT 1317
Cdd:smart00034    1 CPSG-----WISYGGKCYKFSTEKK-----TWEDAQAFCQSLG--GHLASIHSEAENDFVASLLkNSGSSDYYWIGLSDP 68
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 144446030   1318 YRNKSLMWFDKTPL-SYTHWRAGRPTIKNEKFLAGLSTDGFWD 1359
Cdd:smart00034   69 DSNGSWQWSDGSGPvSYSNWAPGEPNNSSGDCVVLSTSGGKWN 111
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
227-341 4.13e-12

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


Pssm-ID: 153059  Cd Length: 137  Bit Score: 65.07  E-value: 4.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  227 GSCYQFnTQTALSWKEAYVSCQNQG-----ADLLSINSAAELTYLKE------KEGIAKIFWIGLNQLYSARGWEWSDHK 295
Cdd:cd03589    10 GYCYRF-FGDRLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDlfessrGPDTPYGLWIGLHDRTSEGPFEWTDGS 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 144446030  296 PLNFLNWDPDRPSApTIGGSSCARM---DAESGLWQSFSCEAQLPYVCR 341
Cdd:cd03589    89 PVDFTKWAGGQPDN-YGGNEDCVQMwrrGDAGQSWNDMPCDAVFPYICK 136
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
514-625 1.15e-11

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 63.41  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  514 CYKIYEDEVPFG---TNCN------LTITSRFEQEYLNDLMKKYDKSlrkYFWTGLRDVDSCGEYNWATvggRRRAVTFS 584
Cdd:cd00037     2 CYKFSTEKLTWEeaqEYCRslgghlASIHSEEENDFLASLLKKSSSS---DVWIGLNDLSSEGTWKWSD---GSPLVDYT 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 144446030  585 NWNFLEPASPGG--CVAMSTGKSvGKWEVKDCrSFKALSICKK 625
Cdd:cd00037    76 NWAPGEPNPGGSedCVVLSSSSD-GKWNDVSC-SSKLPFICEK 116
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
1115-1221 9.24e-11

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


Pssm-ID: 153072  Cd Length: 108  Bit Score: 60.47  E-value: 9.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1115 YKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLSVQALLHNSSLWIGLFsqDDELNFGWSDGKRLHFSRWA-ETNGQ 1193
Cdd:cd03602     3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLY--RDVDSWRWSDGSESSFRNWNtFQPFG 80
                          90       100
                  ....*....|....*....|....*...
gi 144446030 1194 LEDCVVLDTDGFWKTVDCNDNQPgAICY 1221
Cdd:cd03602    81 QGDCATMYSSGRWYAALCSALKP-FICY 107
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
643-732 1.34e-10

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


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 60.85  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  643 CPEGWQSFPASlsCYKVFHAERivrkrNWEEAERFCQAL--GAHLSSFSHVDEIKEFLHFLTDQFSGQHWLWIGLNKrsP 720
Cdd:cd03594     1 CPKGWLPYKGN--CYGYFRQPL-----SWSDAELFCQKYgpGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHD--P 71
                          90
                  ....*....|..
gi 144446030  721 DLQGSWQWSDRT 732
Cdd:cd03594    72 QQSRGWEWSDGS 83
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
643-734 1.56e-10

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 60.28  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  643 CPEGWQSFPASlsCYKVFHAerivrKRNWEEAERFCQALGAHLSSFSHVDEiKEFLHFLtdqfsGQHWLWIGLNKRSpdL 722
Cdd:cd03588     1 CEEGWDKFQGH--CYRHFPD-----RETWEDAERRCREQQGHLSSIVTPEE-QEFVNNN-----AQDYQWIGLNDRT--I 65
                          90
                  ....*....|..
gi 144446030  723 QGSWQWSDRTPV 734
Cdd:cd03588    66 EGDFRWSDGHPL 77
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
1539-1661 1.72e-10

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


Pssm-ID: 153059  Cd Length: 137  Bit Score: 60.45  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1539 WIQYKGHCYKSDQALHSFSEAKKLCSKHD---HSATIVSIKDEDENKFVSRLMRENN--NITMRVWLGLSQHSVDQSWSW 1613
Cdd:cd03589     5 WTAFGGYCYRFFGDRLTWEEAELRCRSFSipgLIAHLVSIHSQEENDFVYDLFESSRgpDTPYGLWIGLHDRTSEGPFEW 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 144446030 1614 LDGSEVTFVKW------ENKSKSGVGRCSMLIASNETWKKVECEHGFgRVVCKV 1661
Cdd:cd03589    85 TDGSPVDFTKWaggqpdNYGGNEDCVQMWRRGDAGQSWNDMPCDAVF-PYICKM 137
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
1109-1216 2.72e-10

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 59.51  E-value: 2.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1109 KYLNNLYKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLSVQAllhNSSLWIGLFSQDDELNFGWSDGKRLHFSRWA 1188
Cdd:cd03588     7 KFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNA---QDYQWIGLNDRTIEGDFRWSDGHPLQFENWR 83
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 144446030 1189 ETN-----GQLEDCVVL--DTDGFWKTVDCNDNQP 1216
Cdd:cd03588    84 PNQpdnffATGEDCVVMiwHEEGEWNDVPCNYHLP 118
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
1113-1219 2.94e-10

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


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 59.36  E-value: 2.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1113 NLYKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLsVQALLHNSSLWIGLFSQDDELNFGWSDGKRLHFSRWAETN- 1191
Cdd:cd03603     1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWL-LSNFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEp 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 144446030 1192 ----GQLEDCV----VLDTDGFWKTVDCNDNQPGAI 1219
Cdd:cd03603    80 hnngGGNEDYAainhFPGISGKWNDLANSYNTLGYV 115
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
643-791 4.11e-10

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


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 59.24  E-value: 4.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  643 CPEGWQSFpaSLSCYkVFHAErivrKRNWEEAERFCQALGAHLSSFSHVDEikefLHFLTDQFSGQHWLWIGLNKrsPDL 722
Cdd:cd03590     1 CPTNWKSF--QSSCY-FFSTE----KKSWEESRQFCEDMGAHLVIINSQEE----QEFISKILSGNRSYWIGLSD--EET 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 144446030  723 QGSWQWSDRTPVSTIIM------PNEFQQDYDirDCAAVkvfhRPWRRGWhfYDDrefiylrpfACDTKLEWVCQ 791
Cdd:cd03590    68 EGEWKWVDGTPLNSSKTfwhpgePNNWGGGGE--DCAEL----VYDSGGW--NDV---------PCNLEYRWICE 125
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
1255-1359 5.52e-10

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 58.40  E-value: 5.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1255 CYNFIITKnrhmaTTQDEVHTKCQKLNpkSHILSIRDEKENNFVLEQLLYFNYMASWVMLGITYRNKSLMWFDKTP-LSY 1333
Cdd:cd00037     2 CYKFSTEK-----LTWEEAQEYCRSLG--GHLASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDY 74
                          90       100
                  ....*....|....*....|....*...
gi 144446030 1334 THWRAGRPTIKNEKFLAGL--STDGFWD 1359
Cdd:cd00037    75 TNWAPGEPNPGGSEDCVVLssSSDGKWN 102
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
230-327 2.44e-09

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


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 56.66  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  230 YQFnTQTALSWKEAYVSCQNQGADLLSINSAAELTYLKEKEGIAKIFWIGLNQLYSARGWEWSDHKPLNFLNWDPDRPSA 309
Cdd:cd03603     3 YKF-VDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHN 81
                          90       100
                  ....*....|....*....|.
gi 144446030  310 PTIGGSSCARMDA---ESGLW 327
Cdd:cd03603    82 NGGGNEDYAAINHfpgISGKW 102
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
361-487 2.57e-09

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 56.57  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  361 CDAGWLPNNGFCYLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEDikeeVWIGLKNINIPTLFQWSDGT 440
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSS----YWIGLSREKSEKPWKWIDGS 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 144446030  441 evTLTYWDENEPNVPYNktpNCVSylgeLGQWKVQS--CEEKLKYVCKR 487
Cdd:cd03593    77 --PLNNLFNIRGSTKSG---NCAY----LSSTGIYSedCSTKKRWICEK 116
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
1409-1513 2.62e-09

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


Pssm-ID: 153072  Cd Length: 108  Bit Score: 56.23  E-value: 2.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1409 IQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGFPLWVGLSshdGSESSFEWSDGSTFDYIPWKGQTSPGN- 1487
Cdd:cd03602     6 VNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLY---RDVDSWRWSDGSESSFRNWNTFQPFGQg 82
                          90       100
                  ....*....|....*....|....*..
gi 144446030 1488 -CVLLDPKGTWKHEKCNSVKDgAICYK 1513
Cdd:cd03602    83 dCATMYSSGRWYAALCSALKP-FICYD 108
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
1538-1651 3.33e-09

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


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 56.54  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1538 RWIQYKGHCYKSDQALHSFSEAKKLCSkhDHSATIVSIKDEDENKFVSRLMRENNNitmrVWLGLSQHSVDQSWSWLDGS 1617
Cdd:cd03590     4 NWKSFQSSCYFFSTEKKSWEESRQFCE--DMGAHLVIINSQEEQEFISKILSGNRS----YWIGLSDEETEGEWKWVDGT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 144446030 1618 --EVTFVKWE----NKSKSGVGRCSMLIASNETWKKVECE 1651
Cdd:cd03590    78 plNSSKTFWHpgepNNWGGGGEDCAELVYDSGGWNDVPCN 117
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
235-340 3.83e-09

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


Pssm-ID: 153072  Cd Length: 108  Bit Score: 55.84  E-value: 3.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  235 QTALSWKEAYVSCQNQGADLLSINSAAELTYLKE-KEGIAKIFWIGLnqLYSARGWEWSDHKPLNFLNWDPDRPSaptiG 313
Cdd:cd03602     7 NESKTWSEAQQYCRENYTDLATVQNQEDNALLSNlSRVSNSAAWIGL--YRDVDSWRWSDGSESSFRNWNTFQPF----G 80
                          90       100
                  ....*....|....*....|....*..
gi 144446030  314 GSSCARMDAeSGLWQSFSCEAQLPYVC 340
Cdd:cd03602    81 QGDCATMYS-SGRWYAALCSALKPFIC 106
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
1554-1660 5.06e-09

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 55.56  E-value: 5.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  1554 HSFSEAKKLCSKHdhSATIVSIKDEDENKFVSRLMRENNNitmRVWLGLSQHSVDQSWSWLDGSEVTFVKWENKSKSGVG 1633
Cdd:pfam00059    2 KTWDEAREACRKL--GGHLVSINSAEELDFLSSTLKKSNK---YFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGE 76
                           90       100       110
                   ....*....|....*....|....*....|.
gi 144446030  1634 R--CSMLIASNETWKKVECE--HGFgrvVCK 1660
Cdd:pfam00059   77 NedCVELSSSSGKWNDENCNskNPF---VCE 104
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
821-932 2.06e-08

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 54.16  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  821 SEYWFVADlHLNYEEAVLYCASNHSFLATITSFVGLKAIKNKIANisGDGQKWWIRISEWPIDDHF---------TYSRY 891
Cdd:cd00037     1 SCYKFSTE-KLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKK--SSSSDVWIGLNDLSSEGTWkwsdgsplvDYTNW 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 144446030  892 PWHRFPVTFGEECLYMSAKT---WlidlgKPTDCSTKLPFICEK 932
Cdd:cd00037    78 APGEPNPGGSEDCVVLSSSSdgkW-----NDVSCSSKLPFICEK 116
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
1413-1481 2.23e-08

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


Pssm-ID: 153059  Cd Length: 137  Bit Score: 54.67  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1413 VTWYEALNMC---SQSG--GHLASVHNQNGQLFLEDIVK---RDGFP--LWVGLssHD-GSESSFEWSDGSTFDYIPWKG 1481
Cdd:cd03589    20 LTWEEAELRCrsfSIPGliAHLVSIHSQEENDFVYDLFEssrGPDTPygLWIGL--HDrTSEGPFEWTDGSPVDFTKWAG 97
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
1400-1506 2.81e-08

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


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 53.91  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1400 PYEDGIYSVIQKKVTWYEALNMC--SQSGGHLASVHNQNGQLFLEDIVK---RDGFPLWVGLssHDGSES-SFEWSDGST 1473
Cdd:cd03594     7 PYKGNCYGYFRQPLSWSDAELFCqkYGPGAHLASIHSPAEAAAIASLISsyqKAYQPVWIGL--HDPQQSrGWEWSDGSK 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 144446030 1474 FDYIPWKGQTS---PGNCVLLDPKG---TWKHEKCNSVK 1506
Cdd:cd03594    85 LDYRSWDRNPPyarGGYCAELSRSTgflKWNDANCEERN 123
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
643-791 3.02e-08

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 53.49  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  643 CPEGWQSFpaSLSCYKVFHaerivRKRNWEEAERFCQALGAHLSSFSHVDEikefLHFLTDQfSGQHWLWIGLNKRSPDl 722
Cdd:cd03593     1 CPKDWICY--GNKCYYFSM-----EKKTWNESKEACSSKNSSLLKIDDEEE----LEFLQSQ-IGSSSYWIGLSREKSE- 67
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 144446030  723 qGSWQWSDRTPVSTIIMPNEFQQDydiRDCAAVKvfhrpwrrGWHFYDDRefiylrpfaCDTKLEWVCQ 791
Cdd:cd03593    68 -KPWKWIDGSPLNNLFNIRGSTKS---GNCAYLS--------STGIYSED---------CSTKKRWICE 115
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
1538-1618 3.97e-08

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 53.10  E-value: 3.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1538 RWIQYKGHCYKSDQALHSFSEAKKLCSkhDHSATIVSIKDEDENKFVSRLMRENNnitmrVWLGLSQHSVDQSWSWLDGS 1617
Cdd:cd03593     4 DWICYGNKCYYFSMEKKTWNESKEACS--SKNSSLLKIDDEEELEFLQSQIGSSS-----YWIGLSREKSEKPWKWIDGS 76

                  .
gi 144446030 1618 E 1618
Cdd:cd03593    77 P 77
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
227-340 6.45e-08

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 52.45  E-value: 6.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  227 GSCYQFNtQTALSWKEAYVSCQN-QGADLLSINSAA---ELTYLKEKEGIAKiFWIGLNQLYSARGWE--WSDHKPLNFL 300
Cdd:cd03598     1 GRCYRFV-KSPRTFRDAQVICRRcYRGNLASIHSFAfnyRVQRLVSTLNQAQ-VWIGGIITGKGRCRRfsWVDGSVWNYA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 144446030  301 NWDPDRPSaptIGGSSCARMDAESGLWQSFSCEAQLPYVC 340
Cdd:cd03598    79 YWAPGQPG---NRRGHCVELCTRGGHWRRAHCKLRRPFIC 115
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
1399-1506 6.64e-08

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 52.72  E-value: 6.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1399 MPYEDGIYSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGFplWVGLsSHDGSESSFEWSDGSTF-DYI 1477
Cdd:cd03593     6 ICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSY--WIGL-SREKSEKPWKWIDGSPLnNLF 82
                          90       100
                  ....*....|....*....|....*....
gi 144446030 1478 PWKGQTSPGNCVLLDPKGTwKHEKCNSVK 1506
Cdd:cd03593    83 NIRGSTKSGNCAYLSSTGI-YSEDCSTKK 110
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
1113-1220 7.73e-08

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


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 52.69  E-value: 7.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1113 NLYKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLSvQALLHNSSLWIGLFSQDDELNFGWSDGKRLH--FSRWAET 1190
Cdd:cd03590    11 SCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIS-KILSGNRSYWIGLSDEETEGEWKWVDGTPLNssKTFWHPG 89
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 144446030 1191 -----NGQLEDCVVLDTD-GFWKTVDCNDNQPgAIC 1220
Cdd:cd03590    90 epnnwGGGGEDCAELVYDsGGWNDVPCNLEYR-WIC 124
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
1115-1220 9.01e-08

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


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 51.91  E-value: 9.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1115 YKIIPKTLTWHSAKRECLKSNMQLVSITDPYQQAFLSVQALLHNSSLWIGLFSQDDELNFGWSDGKRLHFSRW--AETNG 1192
Cdd:cd03591     4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYTNWkpGEPNN 83
                          90       100       110
                  ....*....|....*....|....*....|
gi 144446030 1193 QL--EDCVVLDTDGFWKTVDCNDNQPgAIC 1220
Cdd:cd03591    84 AGggEDCVEMYTSGKWNDVACNLTRL-FVC 112
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
372-485 1.01e-07

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 52.07  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  372 CYLLVNESNSWDKAHAKC-KAFSSDLISIHSLaDVEVVVTKLHNEDIKEEVWIG--LKNINIPTLFQWSDGTEVTLTYWd 448
Cdd:cd03598     3 CYRFVKSPRTFRDAQVICrRCYRGNLASIHSF-AFNYRVQRLVSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWNYAYW- 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 144446030  449 enEPNVPYNKTPNCVSYLGELGQWKVQSCEEKLKYVC 485
Cdd:cd03598    81 --APGQPGNRRGHCVELCTRGGHWRRAHCKLRRPFIC 115
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
373-485 1.06e-07

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


Pssm-ID: 153072  Cd Length: 108  Bit Score: 51.61  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  373 YLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLhnEDIKEEVWIGLKNINIPtlFQWSDGTEVTLTYWDenep 452
Cdd:cd03602     3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLS--RVSNSAAWIGLYRDVDS--WRWSDGSESSFRNWN---- 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 144446030  453 NVPYNKTPNCVsYLGELGQWKVQSCEEKLKYVC 485
Cdd:cd03602    75 TFQPFGQGDCA-TMYSSGRWYAALCSALKPFIC 106
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
951-1091 1.54e-07

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


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 51.92  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  951 CSEQWIPFQNKCFLkIKPVSLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPDMEATlWIGLRWTAYEKINKWTDNRE 1030
Cdd:cd03590     1 CPTNWKSFQSSCYF-FSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSY-WIGLSDEETEGEWKWVDGTP 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 144446030 1031 L--TYSNFHPllvsgrlRIPEN-FFEEEsryHCALIlnlqkSPFTGTWNFTSCSERHFvSLCQK 1091
Cdd:cd03590    79 LnsSKTFWHP-------GEPNNwGGGGE---DCAEL-----VYDSGGWNDVPCNLEYR-WICEK 126
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
530-625 2.14e-07

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 50.94  E-value: 2.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   530 LTITSRFEQEYLNDLMKKYDKslrkYFWTGLRDVDSCGEYNWatVGGRRraVTFSNWNFLEPASPGG--CVAMStgKSVG 607
Cdd:pfam00059   19 VSINSAEELDFLSSTLKKSNK----YFWIGLTDRKNEGTWKW--VDGSP--VNYTNWAPEPNNNGENedCVELS--SSSG 88
                           90
                   ....*....|....*...
gi 144446030   608 KWEVKDCrSFKALSICKK 625
Cdd:pfam00059   89 KWNDENC-NSKNPFVCEK 105
beta-trefoil_Ricin_MRC1 cd23407
ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 1 (MRC1) ...
36-142 2.78e-07

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


Pssm-ID: 467785  Cd Length: 123  Bit Score: 50.83  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   36 FTIVHGNTGKCIKPV-YGWIVADDCD-ETEDKLWKWVSQHRLFHLHSQKCLGLDITKSVNELRMFSCDS-SAMLWWKCEH 112
Cdd:cd23407     3 FLIYNEDHNRCVQARsSSSVTTATCNpNAESQKFRWVSGSQILSVAFKLCLGVPSKKDWVTVTLFPCNEkSELQKWECKN 82
                          90       100       110
                  ....*....|....*....|....*....|....
gi 144446030  113 HSLYGAARYRLAL---KDGHGTA-ISNASDVWKK 142
Cdd:cd23407    83 DTLLALKGEDLYFnygNRQEKNVmLYKGSGLWSR 116
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
951-1038 2.93e-07

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 50.79  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  951 CSEQWIPFQNKCFLKIKpVSLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPdmEATLWIGLRWTAYEKINKWTDNRE 1030
Cdd:cd03593     1 CPKDWICYGNKCYYFSM-EKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIG--SSSYWIGLSREKSEKPWKWIDGSP 77

                  ....*...
gi 144446030 1031 LTySNFHP 1038
Cdd:cd03593    78 LN-NLFNI 84
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
951-1084 3.13e-07

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


Pssm-ID: 153059  Cd Length: 137  Bit Score: 51.20  E-value: 3.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  951 CSEQWIPFQNKCFlKIKPVSLTFSQASDTCHSYG-----GTLPSVLSQIEQDFITSLL-----PDMEATLWIGLRWTAYE 1020
Cdd:cd03589     1 CPTFWTAFGGYCY-RFFGDRLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFessrgPDTPYGLWIGLHDRTSE 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 144446030 1021 KINKWTDNRELTYSNFHPllvsgrlRIPENFFEEESryhCALILNLQKSpfTGTWNFTSCSERH 1084
Cdd:cd03589    80 GPFEWTDGSPVDFTKWAG-------GQPDNYGGNED---CVQMWRRGDA--GQSWNDMPCDAVF 131
beta-trefoil_Ricin_PTPRB-like cd23409
ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein ...
34-126 4.99e-07

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


Pssm-ID: 467787  Cd Length: 117  Bit Score: 50.13  E-value: 4.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   34 DPFTIVHGNTGKCIKPVYGWIVADdCDETE-DKLWKWVSQHRLFHLHSQKCLGLDITKSVNELR--MFSCdSSAMLWWKC 110
Cdd:cd23409     2 EGFLILHVQKQQCLFGNKTVSVGK-CNATSpNQQWQWTEDGKLLHVKSGQCLGISNSSAFHSRRaiLLDC-SQAPRWTCH 79
                          90
                  ....*....|....*.
gi 144446030  111 EHHSLYGAARYRLALK 126
Cdd:cd23409    80 ENEGLLEVANSSLFLT 95
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
1120-1221 1.17e-06

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


Pssm-ID: 153062  Cd Length: 115  Bit Score: 48.91  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1120 KTLTWHSAKRECLKSNMQLVSITDPYQQAFLSVQALLHNSSL-WIGLFSQDDELNFGWSDGKRLHFSRWAET---NGQLE 1195
Cdd:cd03592     8 EKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYyWIDGNDINNEGTWVDTDKKELEYKNWAPGepnNGRNE 87
                          90       100
                  ....*....|....*....|....*...
gi 144446030 1196 DCVV--LDTDGFWKTVDCNdNQPGAICY 1221
Cdd:cd03592    88 NCLEiyIKDNGKWNDEPCS-KKKSAICY 114
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
951-1091 1.46e-06

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 49.11  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  951 CSEQWIPFQNKCFlKIKPVSLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPDMEatlWIGLRWTAYEKINKWTDNRE 1030
Cdd:cd03588     1 CEEGWDKFQGHCY-RHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ---WIGLNDRTIEGDFRWSDGHP 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 144446030 1031 LTYSNFHPllvsgrlRIPENFFeeESRYHCALILNLQKspftGTWNFTSCSeRHFVSLCQK 1091
Cdd:cd03588    77 LQFENWRP-------NQPDNFF--ATGEDCVVMIWHEE----GEWNDVPCN-YHLPFTCKK 123
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
831-932 1.53e-06

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 48.24  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   831 LNYEEAVLYCASNHSFLATITSFVGLKAIKNKIANisgDGQKWWIRIS--------EWPIDDHFTYSryPWHRFP--VTF 900
Cdd:pfam00059    2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKK---SNKYFWIGLTdrknegtwKWVDGSPVNYT--NWAPEPnnNGE 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 144446030   901 GEECLYMSAKTWLIDLgkpTDCSTKLPFICEK 932
Cdd:pfam00059   77 NEDCVELSSSSGKWND---ENCNSKNPFVCEK 105
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
234-340 1.57e-06

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


Pssm-ID: 153062  Cd Length: 115  Bit Score: 48.53  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  234 TQTALSWKEAYVSCQNQGADLLSINSAAELTYLKEKegIAKI----FWIGLNQLYSARGWEWSDHKPLNFLNWDPDRPSA 309
Cdd:cd03592     6 STEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGF--ALKYnlgyYWIDGNDINNEGTWVDTDKKELEYKNWAPGEPNN 83
                          90       100       110
                  ....*....|....*....|....*....|..
gi 144446030  310 PtiGGSSCARM-DAESGLWQSFSCEAQLPYVC 340
Cdd:cd03592    84 G--RNENCLEIyIKDNGKWNDEPCSKKKSAIC 113
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
1110-1216 2.21e-06

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


Pssm-ID: 153059  Cd Length: 137  Bit Score: 48.89  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1110 YLNNLYKIIPKTLTWHSAKRECLKSNM-----QLVSITDPYQQAFL-----SVQALLHNSSLWIGLFSQDDELNFGWSDG 1179
Cdd:cd03589     8 FGGYCYRFFGDRLTWEEAELRCRSFSIpgliaHLVSIHSQEENDFVydlfeSSRGPDTPYGLWIGLHDRTSEGPFEWTDG 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 144446030 1180 KRLHFSRWAETN----GQLEDCVVL----DTDGFWKTVDCNDNQP 1216
Cdd:cd03589    88 SPVDFTKWAGGQpdnyGGNEDCVQMwrrgDAGQSWNDMPCDAVFP 132
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
38-112 2.62e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 47.89  E-value: 2.62e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 144446030     38 IVHGNTGKCI--KPVYGWIVADDCDETED-KLWKWVSQHRLFHLHSQKCLGLDITKSVNeLRMFSCDSSA-MLWWKCEH 112
Cdd:smart00458    1 IISGNTGKCLdvNGNKNPVGLFDCHGTGGnQLWKLTSDGAIRIKDTDLCLTANGNTGST-VTLYSCDGTNdNQYWEVNK 78
beta-trefoil_Ricin_MRC2 cd23408
ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 2 (MRC2) ...
34-111 3.82e-06

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


Pssm-ID: 467786  Cd Length: 124  Bit Score: 47.86  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   34 DPFTIVHGNTGKCIKpVYGWIV--ADDCDET-EDKLWKWVSQHRLFHLHSQKCLGL---DITKSVNELRMFSCDSSAMLW 107
Cdd:cd23408     1 DVFLIYSDGAQGCLE-VRDSVVrlSPACNTSsPAQQWKWVSRNRLFNLGSMQCLGVsgpNGSGTSATLGTYECDRESVNM 79

                  ....*
gi 144446030  108 -WKCE 111
Cdd:cd23408    80 rWHCR 84
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
1539-1624 3.91e-06

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 47.57  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1539 WIQYKGHCYKSDQALHSFSEAKKLCskHDHSATIVSIKDEDENKFVSRLMRENNnitmrvWLGLSQHSVDQSWSWLDGSE 1618
Cdd:cd03588     5 WDKFQGHCYRHFPDRETWEDAERRC--REQQGHLSSIVTPEEQEFVNNNAQDYQ------WIGLNDRTIEGDFRWSDGHP 76

                  ....*.
gi 144446030 1619 VTFVKW 1624
Cdd:cd03588    77 LQFENW 82
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
820-931 4.80e-06

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 47.59  E-value: 4.80e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030    820 GSEYWFVADLhLNYEEAVLYCASNHSFLATITSFVGLKAIKNKIANISGDGQkWWI------RISEWPIDDHFTYSRYP- 892
Cdd:smart00034   10 GKCYKFSTEK-KTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDY-YWIglsdpdSNGSWQWSDGSGPVSYSn 87
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|
gi 144446030    893 WHR-FPVTFGEECLYMSAKTWLIDlgkPTDCSTKLPFICE 931
Cdd:smart00034   88 WAPgEPNNSSGDCVVLSTSGGKWN---DVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
668-791 5.96e-06

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 46.70  E-value: 5.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   668 KRNWEEAERFCQALGAHLSSFSHVDEIKEFLHFLTDQFSGqhwLWIGLNKRspDLQGSWQWSDRTPVSTIIMPNEFQQDY 747
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKY---FWIGLTDR--KNEGTWKWVDGSPVNYTNWAPEPNNNG 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 144446030   748 DIRDCAAVkvfHRPWRRgWHFYDdrefiylrpfaCDTKLEWVCQ 791
Cdd:pfam00059   76 ENEDCVEL---SSSSGK-WNDEN-----------CNSKNPFVCE 104
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
1405-1504 6.02e-06

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


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 46.91  E-value: 6.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1405 IYSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGFPLWVGLSShDGSESSFEWSDGSTFDYIPWK---- 1480
Cdd:cd03591     3 IFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITD-LETEGQFVYLDGGPLTYTNWKpgep 81
                          90       100
                  ....*....|....*....|....*
gi 144446030 1481 -GQTSPGNCVLLDPKGTWKHEKCNS 1504
Cdd:cd03591    82 nNAGGGEDCVEMYTSGKWNDVACNL 106
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
963-1036 7.84e-06

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


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 46.65  E-value: 7.84e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 144446030  963 FLKIKPVSLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPDMEATlWIGLRWTAYEKINKWTDNRELTYSNF 1036
Cdd:cd03603     2 FYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGAS-WIGASDAATEGTWKWSDGEESTYTNW 74
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
373-472 8.15e-06

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


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 46.65  E-value: 8.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  373 YLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEdikEEVWIGLKNINIPTLFQWSDGTEVTLTYWDENEP 452
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGY---GASWIGASDAATEGTWKWSDGEESTYTNWGSGEP 79
                          90       100
                  ....*....|....*....|....*
gi 144446030  453 nvPYNKTPNCV-----SYLGELGQW 472
Cdd:cd03603    80 --HNNGGGNEDyaainHFPGISGKW 102
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
1414-1513 9.15e-06

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


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 46.53  E-value: 9.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1414 TWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGFpLWVGLSSHDGsESSFEWSDGSTFDYIPW---KGQ----TSPG 1486
Cdd:cd03590    21 SWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS-YWIGLSDEET-EGEWKWVDGTPLNSSKTfwhPGEpnnwGGGG 98
                          90       100
                  ....*....|....*....|....*....
gi 144446030 1487 -NCV-LLDPKGTWKHEKCNSVKDgAICYK 1513
Cdd:cd03590    99 eDCAeLVYDSGGWNDVPCNLEYR-WICEK 126
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
1113-1222 9.69e-06

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


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 46.60  E-value: 9.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1113 NLYKIIPKTLTWHSAKREC--LKSNMQLVSITDPYQQAFLS--VQALLH-NSSLWIGLFSQDDELNFGWSDGKRLHFSRW 1187
Cdd:cd03594    11 NCYGYFRQPLSWSDAELFCqkYGPGAHLASIHSPAEAAAIAslISSYQKaYQPVWIGLHDPQQSRGWEWSDGSKLDYRSW 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 144446030 1188 --AETNGQLEDCVVL-DTDGF--WKTVDCNDNQPgAICYY 1222
Cdd:cd03594    91 drNPPYARGGYCAELsRSTGFlkWNDANCEERNP-FICKY 129
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
1547-1650 1.13e-05

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


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 46.14  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1547 YKSDQALHSFSEAKKLCSkhDHSATIVSIKDEDENKFVSRLMRENNNitmRVWLGLSQHSVDQSWSWLDGSEVTFVKWEN 1626
Cdd:cd03591     4 FVTNGEEKNFDDAQKLCS--EAGGTLAMPRNAAENAAIASYVKKGNT---YAFIGITDLETEGQFVYLDGGPLTYTNWKP 78
                          90       100
                  ....*....|....*....|....*..
gi 144446030 1627 KSKSGVGR---CsMLIASNETWKKVEC 1650
Cdd:cd03591    79 GEPNNAGGgedC-VEMYTSGKWNDVAC 104
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
1406-1487 1.44e-05

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


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 45.88  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1406 YSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGFpLWVGLSSHDgSESSFEWSDGSTFDYIPWkGQTSP 1485
Cdd:cd03603     3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGA-SWIGASDAA-TEGTWKWSDGEESTYTNW-GSGEP 79

                  ..
gi 144446030 1486 GN 1487
Cdd:cd03603    80 HN 81
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
367-486 1.88e-05

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


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 50.08  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030   367 PNNGFCYLLVNESNSWDKAHAKCKAFS-SDLISIHSLADVEVVVTKLhNEDIKEEVWIGLKNINIPTLFQWSDGTEVTLT 445
Cdd:TIGR00864  326 EENGHCFQIVPEEAAWLDAQEQCLARAgAALAIVDNDALQNFLARKV-THSLDRGVWIGFSDVNGAEKGPAHQGEAFEAE 404
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 144446030   446 YWDENEPNVPYNKTPN-CVSyLGELGQWKVQSCEEKLKYVCK 486
Cdd:TIGR00864  405 ECEEGLAGEPHPARAEhCVR-LDPRGQCNSDLCNAPHAYVCE 445
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
242-340 2.29e-05

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


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 45.36  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  242 EAYVSCQNQGADLLSINSAAELTYLKE--KEGIAKIFwIGLNQLYSARGWEWSDHKPLNFLNWDPDRPSAPTiGGSSCAR 319
Cdd:cd03591    15 DAQKLCSEAGGTLAMPRNAAENAAIASyvKKGNTYAF-IGITDLETEGQFVYLDGGPLTYTNWKPGEPNNAG-GGEDCVE 92
                          90       100
                  ....*....|....*....|.
gi 144446030  320 MdAESGLWQSFSCEAQLPYVC 340
Cdd:cd03591    93 M-YTSGKWNDVACNLTRLFVC 112
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
1555-1625 2.41e-05

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


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 45.11  E-value: 2.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 144446030 1555 SFSEAKKLCskHDHSATIVSIKDEDENKFVSRLMRENNNitmrVWLGLSQHSVDQSWSWLDGSEVTFVKWE 1625
Cdd:cd03603    11 TWEAAQTLA--ESLGGHLVTINSAEENDWLLSNFGGYGA----SWIGASDAATEGTWKWSDGEESTYTNWG 75
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
381-486 3.13e-05

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


Pssm-ID: 153065  Cd Length: 149  Bit Score: 45.65  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  381 SWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEDIKE-EVWIGLK--------NINIPTLFQWSDGTEVTLTYWDENE 451
Cdd:cd03595    26 NFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDgDFWIGLRrssqynvtSSACSSLYYWLDGSISTFRNWYVDE 105
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 144446030  452 PN-------VPYNKtPNCVSYLGE--LGQWKVQSCEEKLKYVCK 486
Cdd:cd03595   106 PScgsevcvVMYHQ-PSAPAGQGGpyLFQWNDDNCNMKNNFICK 148
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
1239-1341 3.23e-05

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


Pssm-ID: 153059  Cd Length: 137  Bit Score: 45.43  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1239 CPspvlnTPWIPFQNCCYNFIITKnrhmaTTQDEVHTKCQKLN---PKSHILSIRDEKENNFVLEqllYFNYMAS----- 1310
Cdd:cd03589     1 CP-----TFWTAFGGYCYRFFGDR-----LTWEEAELRCRSFSipgLIAHLVSIHSQEENDFVYD---LFESSRGpdtpy 67
                          90       100       110
                  ....*....|....*....|....*....|...
gi 144446030 1311 --WVMLGITYRNKSLMWFDKTPLSYTHWRAGRP 1341
Cdd:cd03589    68 glWIGLHDRTSEGPFEWTDGSPVDFTKWAGGQP 100
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
531-623 3.26e-05

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


Pssm-ID: 153066  Cd Length: 129  Bit Score: 45.07  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  531 TITSRFEQEYLNDLMKKYDKSLRKyFWTGLRDVDSCGEynWATVGGRRraVTFSNWNFLEPASPGG-----CVAMStGKS 605
Cdd:cd03596    37 TPRDSDENDALRDYVKASVPGNWE-VWLGINDMVAEGK--WVDVNGSP--ISYFNWEREITAQPDGgkrenCVALS-SSA 110
                          90
                  ....*....|....*...
gi 144446030  606 VGKWEVKDCRSFKAlSIC 623
Cdd:cd03596   111 QGKWFDEDCRREKP-YVC 127
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
229-340 4.10e-05

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


Pssm-ID: 153066  Cd Length: 129  Bit Score: 45.07  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  229 CYQFNTQTAlSWKEAYVSCQNQGADLLSINSAAELT----YLKEKEGIAKIFWIGLNQLYSARGWEWSDHKPLNFLNWDP 304
Cdd:cd03596    11 CYLVSEETK-HYHEASEDCIARGGTLATPRDSDENDalrdYVKASVPGNWEVWLGINDMVAEGKWVDVNGSPISYFNWER 89
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 144446030  305 DRPSAPTiGGS--SCARMDAES-GLWQSFSCEAQLPYVC 340
Cdd:cd03596    90 EITAQPD-GGKreNCVALSSSAqGKWFDEDCRREKPYVC 127
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
643-734 4.11e-05

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


Pssm-ID: 153059  Cd Length: 137  Bit Score: 45.04  E-value: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  643 CPEGWQSFPASlsCYKVFHAERivrkrNWEEAERFCQALG-----AHLSSFSHVDEIKeflhFLTDQF------SGQHWL 711
Cdd:cd03589     1 CPTFWTAFGGY--CYRFFGDRL-----TWEEAELRCRSFSipgliAHLVSIHSQEEND----FVYDLFessrgpDTPYGL 69
                          90       100
                  ....*....|....*....|...
gi 144446030  712 WIGLNKRSPDlqGSWQWSDRTPV 734
Cdd:cd03589    70 WIGLHDRTSE--GPFEWTDGSPV 90
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
1555-1652 4.12e-05

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


Pssm-ID: 153072  Cd Length: 108  Bit Score: 44.29  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1555 SFSEAKKLCSKHdHSaTIVSIKDEDENKFVSRLMRENNNItmrVWLGLSQHSvdQSWSWLDGSEVTFVKWENKSKSGVGR 1634
Cdd:cd03602    11 TWSEAQQYCREN-YT-DLATVQNQEDNALLSNLSRVSNSA---AWIGLYRDV--DSWRWSDGSESSFRNWNTFQPFGQGD 83
                          90
                  ....*....|....*...
gi 144446030 1635 CSMlIASNETWKKVECEH 1652
Cdd:cd03602    84 CAT-MYSSGRWYAALCSA 100
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
1269-1347 4.51e-05

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 44.01  E-value: 4.51e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 144446030  1269 TQDEVHTKCQKLNpkSHILSIRDEKENNFVLEQLLYFNYmASWVMLGITYRNKSLMWFDKTPLSYTHWrAGRPTIKNEK 1347
Cdd:pfam00059    3 TWDEAREACRKLG--GHLVSINSAEELDFLSSTLKKSNK-YFWIGLTDRKNEGTWKWVDGSPVNYTNW-APEPNNNGEN 77
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
228-341 5.61e-05

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


Pssm-ID: 153065  Cd Length: 149  Bit Score: 44.88  E-value: 5.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  228 SCYQF----NTQTALSWKEAYVSCQNQGADLLSINSAAEL----TYLKEKEGIAKIFWIGL--NQLYSARG------WEW 291
Cdd:cd03595    11 PCYKIayfqDSRRRLNFEEARQACREDGGELLSIESENEQklieRFIQTLRASDGDFWIGLrrSSQYNVTSsacsslYYW 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 144446030  292 SDHKPLNFLNWDPDRPSAptiGGSSCARM----DAESGL-------WQSFSCEAQLPYVCR 341
Cdd:cd03595    91 LDGSISTFRNWYVDEPSC---GSEVCVVMyhqpSAPAGQggpylfqWNDDNCNMKNNFICK 148
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
951-1084 8.15e-05

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


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 43.90  E-value: 8.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  951 CSEQWIPFQNKCFlKIKPVSLTFSQASDTCHSY--GGTLPSVLSQIEQDFITSLLPDM---EATLWIGLRWTAYEKINKW 1025
Cdd:cd03594     1 CPKGWLPYKGNCY-GYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIASLISSYqkaYQPVWIGLHDPQQSRGWEW 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 144446030 1026 TDNRELTYSNFH--PLLVSGRlripenffeeesryHCALILnlQKSPFTgTWNFTSCSERH 1084
Cdd:cd03594    80 SDGSKLDYRSWDrnPPYARGG--------------YCAELS--RSTGFL-KWNDANCEERN 123
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
1402-1511 1.13e-04

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


Pssm-ID: 153070  Cd Length: 141  Bit Score: 43.96  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1402 EDGIYSVIQKKVTWYEALNMCSQSGGHLASVHNQN-----GQLFLEDIVKRDGFP--LWVGLSSHDGSESS-------FE 1467
Cdd:cd03600     3 SDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEeadvvSLLLAAGPGRHGRGSlrLWIGLQREPRQCSDpslplrgFS 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 144446030 1468 W-SDGSTFDYIPWKGQTSPG----NCVLLDPKGT------WKHEKCNSVKDGAIC 1511
Cdd:cd03600    83 WvTGDQDTDFSNWLQEPAGTctspRCVALSAAGStpdnlkWKDGPCSARADGYLC 137
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
530-596 1.35e-04

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


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 43.18  E-value: 1.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 144446030  530 LTITSRFEQEYLNDLMKKYdkslrKYFWTGLRDVDSCGEYNWATvgGRRraVTFSNWNFLEPASPGG 596
Cdd:cd03603    27 VTINSAEENDWLLSNFGGY-----GASWIGASDAATEGTWKWSD--GEE--STYTNWGSGEPHNNGG 84
PHA02911 PHA02911
C-type lectin-like protein; Provisional
333-489 1.43e-04

C-type lectin-like protein; Provisional


Pssm-ID: 177496 [Multi-domain]  Cd Length: 213  Bit Score: 45.18  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  333 EAQLPYVCRKPLnnTVELTDVWTYSDTRCDAGWLPNNGFCYLLVNESNSWDKAHAK--CKAFSSDLIsihsladvevvvt 410
Cdd:PHA02911   77 EPSIATTCPDNL--TIHCPEVPSPSEPICSRDWINHMGICLLSLGEEVGFRMEIAKrfCEKKDADLI------------- 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  411 KLHNEDIKeevwiGLKNIniptlfqWSdGTEVTlTYW-DENEPNVPYNKTPNCV----SYLGELGQWKVQSCEEKLKYVC 485
Cdd:PHA02911  142 GKIDEEKK-----ALENI-------WT-GNDHS-RFWiDNRAAASTFDPVNECAigtqNHIPEVPEVLKSPCDERHSFIC 207

                  ....
gi 144446030  486 KRKG 489
Cdd:PHA02911  208 IKKD 211
CLECT_DGCR2_like cd03599
C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein ...
643-767 1.47e-04

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.


Pssm-ID: 153069  Cd Length: 153  Bit Score: 43.75  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  643 CPEGWQSFPASLSCYKVFhaeriVRKRNWEEAERFCQALGAHLSSFSHVDEIKEFLHFLTDQ------FSGQHWLWIG-- 714
Cdd:cd03599     1 CPSGWHHYEGTASCYKVY-----LSGENYWDAVQTCQKVNGSLATFTTDQELQFILAQEWDFdervfgRKDQCKFWVGyq 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 144446030  715 --LNKRSPDLQGSWQWSDRTPVSTIIMP----NEFQQDYDIRDCAAVKVFHRPWRR-----GWH 767
Cdd:cd03599    76 yvITNRNHSLEGRWEVAYKGSMEVFLPPepifATGMSTNDNVFCAQLQCFQIPSLRerglhSWH 139
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
822-930 1.77e-04

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


Pssm-ID: 153072  Cd Length: 108  Bit Score: 42.36  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  822 EYWFVaDLHLNYEEAVLYCASNHSFLATITSFVGLKAIKNkiaNISGDGQKWWIRISE------WPIDDHFTYSryPWHR 895
Cdd:cd03602     2 TFYLV-NESKTWSEAQQYCRENYTDLATVQNQEDNALLSN---LSRVSNSAAWIGLYRdvdswrWSDGSESSFR--NWNT 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 144446030  896 FPVTFGEECLYM-SAKTWlidlgKPTDCSTKLPFIC 930
Cdd:cd03602    76 FQPFGQGDCATMySSGRW-----YAALCSALKPFIC 106
PHA02642 PHA02642
C-type lectin-like protein; Provisional
643-732 2.33e-04

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 44.34  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  643 CPEGWQSFPaslscYKVFHAERivRKRNWEEAERFCQALGAHLSSFshvdEIKEFLHFLTdQFSGQHWLWIGLNKRSPDl 722
Cdd:PHA02642   88 CPKGWIGFG-----YKCFYFSE--DSKNWTFGNTFCTSLGATLVKV----ETEEELNFLK-RYKDSSDHWIGLNRESSN- 154
                          90
                  ....*....|
gi 144446030  723 qGSWQWSDRT 732
Cdd:PHA02642  155 -HPWKWADNS 163
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
373-485 2.72e-04

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


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 42.28  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  373 YLLVNESNSWDKAHAKCKAFSSDLISIHSLAD----VEVVVTKLhnedikEEVWIGLKNINIPTLFQWSDGTEVTLTYWD 448
Cdd:cd03591     4 FVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAEnaaiASYVKKGN------TYAFIGITDLETEGQFVYLDGGPLTYTNWK 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 144446030  449 ENEPNVPYNKTpNCVSYLGElGQWKVQSCEEKLKYVC 485
Cdd:cd03591    78 PGEPNNAGGGE-DCVEMYTS-GKWNDVACNLTRLFVC 112
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
373-487 3.28e-04

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


Pssm-ID: 153062  Cd Length: 115  Bit Score: 41.98  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  373 YLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKL--HNEDIkeeVWIGLKNINIPTLFQWSDGTEVTLTYWDEN 450
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFAlkYNLGY---YWIDGNDINNEGTWVDTDKKELEYKNWAPG 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 144446030  451 EPNVPYNKtpNCV-SYLGELGQWKVQSCEEKLKYVCKR 487
Cdd:cd03592    80 EPNNGRNE--NCLeIYIKDNGKWNDEPCSKKKSAICYT 115
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
1406-1497 3.31e-04

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 42.05  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1406 YSVIQKKVTWYEALNMCSQ-SGGHLASVHNQNGQLFLEDIVKRDGFP-LWVGLSSHDGSESS-FEWSDGSTFDYIPW-KG 1481
Cdd:cd03598     4 YRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTLNQAqVWIGGIITGKGRCRrFSWVDGSVWNYAYWaPG 83
                          90
                  ....*....|....*...
gi 144446030 1482 QTSP--GNCVLLDPKGTW 1497
Cdd:cd03598    84 QPGNrrGHCVELCTRGGH 101
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
501-625 4.64e-04

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


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 41.91  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  501 CPPDegWKRHGETCYKIYEDEVPFG---TNCN------LTITSRFEQEYLNDLMKKydkslRKYFWTGLRDVDSCGEYNW 571
Cdd:cd03590     1 CPTN--WKSFQSSCYFFSTEKKSWEesrQFCEdmgahlVIINSQEEQEFISKILSG-----NRSYWIGLSDEETEGEWKW 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 144446030  572 atVGGRRRAVTFSNWNFLEPASPGG----CVAMSTgkSVGKWEVKDCrSFKALSICKK 625
Cdd:cd03590    74 --VDGTPLNSSKTFWHPGEPNNWGGggedCAELVY--DSGGWNDVPC-NLEYRWICEK 126
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
1253-1358 6.65e-04

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 41.28  E-value: 6.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1253 NCCYNFIITKNRHmattqDEVHTKCQKLnPKSHILSIRDEKENNFVLEQLLYFNYMASWVMlGITY---RNKSLMWFDKT 1329
Cdd:cd03598     1 GRCYRFVKSPRTF-----RDAQVICRRC-YRGNLASIHSFAFNYRVQRLVSTLNQAQVWIG-GIITgkgRCRRFSWVDGS 73
                          90       100
                  ....*....|....*....|....*....
gi 144446030 1330 PLSYTHWRAGRPTIKNEKFLAGLSTDGFW 1358
Cdd:cd03598    74 VWNYAYWAPGQPGNRRGHCVELCTRGGHW 102
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
1406-1503 8.28e-04

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 41.02  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1406 YSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFLEDIVKRDGfplWVGLSSHdGSESSFEWSDGSTFDYIPWK-GQ-- 1482
Cdd:cd03588    13 YRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ---WIGLNDR-TIEGDFRWSDGHPLQFENWRpNQpd 88
                          90       100
                  ....*....|....*....|....*.
gi 144446030 1483 ---TSPGNCVLL--DPKGTWKHEKCN 1503
Cdd:cd03588    89 nffATGEDCVVMiwHEEGEWNDVPCN 114
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
655-733 1.04e-03

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


Pssm-ID: 153065  Cd Length: 149  Bit Score: 41.41  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  655 SCYKVFHAERIVRKRNWEEAERFCQALGAHLSSFSHVDEIKEFLHFLTDQFSGQHWLWIGLNKRS------PDLQGSWQW 728
Cdd:cd03595    11 PCYKIAYFQDSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIQTLRASDGDFWIGLRRSSqynvtsSACSSLYYW 90

                  ....*
gi 144446030  729 SDRTP 733
Cdd:cd03595    91 LDGSI 95
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
1406-1514 1.06e-03

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


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 44.30  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  1406 YSVIQKKVTWYEALNMC-SQSGGHLASVHNQNGQLFLEDIVKRD-GFPLWVGLSSHDGSE-SSFEWSDGSTFD-----YI 1477
Cdd:TIGR00864  332 FQIVPEEAAWLDAQEQClARAGAALAIVDNDALQNFLARKVTHSlDRGVWIGFSDVNGAEkGPAHQGEAFEAEeceegLA 411
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 144446030  1478 PWKGQTSPGNCVLLDPKGTWKHEKCNSVKDGAICYKP 1514
Cdd:TIGR00864  412 GEPHPARAEHCVRLDPRGQCNSDLCNAPHAYVCELNP 448
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
542-623 1.54e-03

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


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 39.97  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  542 NDLMKKYDKSLRKYFWTGLRDVDSCGEYNWATvGGRrraVTFSNWNFLEPASPGG---CVAMSTGksvGKWEVKDCRSfK 618
Cdd:cd03591    36 NAAIASYVKKGNTYAFIGITDLETEGQFVYLD-GGP---LTYTNWKPGEPNNAGGgedCVEMYTS---GKWNDVACNL-T 107

                  ....*
gi 144446030  619 ALSIC 623
Cdd:cd03591   108 RLFVC 112
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
361-453 1.64e-03

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


Pssm-ID: 153067  Cd Length: 129  Bit Score: 40.26  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  361 CDAGWLPNNGFCYLLVNESNSWDKAHAKCKAFSSDLISIHSLADVEVVVTKLHNEDIKEEV---WIGLKNINIpTLFQWS 437
Cdd:cd03597     1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMTKQKltpWVGLRKINV-SYWCWE 79
                          90
                  ....*....|....*...
gi 144446030  438 DGTEVTLT--YWDENEPN 453
Cdd:cd03597    80 DMSPFTNTtlQWLPGEPS 97
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
372-485 1.82e-03

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


Pssm-ID: 153066  Cd Length: 129  Bit Score: 40.06  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  372 CYLLVNESNSWDKAHAKCKAFSSDLIS------IHSLADVevVVTKLHNEdikEEVWIGLKNINIPTLFQWSDGTEVTLT 445
Cdd:cd03596    11 CYLVSEETKHYHEASEDCIARGGTLATprdsdeNDALRDY--VKASVPGN---WEVWLGINDMVAEGKWVDVNGSPISYF 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 144446030  446 YWDENEPNVPYN-KTPNCVSYLGEL-GQWKVQSCEEKLKYVC 485
Cdd:cd03596    86 NWEREITAQPDGgKRENCVALSSSAqGKWFDEDCRREKPYVC 127
PHA02642 PHA02642
C-type lectin-like protein; Provisional
229-298 2.51e-03

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 41.25  E-value: 2.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  229 CYQFnTQTALSWKEAYVSCQNQGADLLSINSAAELTYLKEKEGIAKiFWIGLNQLYSARGWEWSDHKPLN 298
Cdd:PHA02642   99 CFYF-SEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSD-HWIGLNRESSNHPWKWADNSNYN 166
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
1546-1624 3.55e-03

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


Pssm-ID: 153065  Cd Length: 149  Bit Score: 39.87  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1546 CYK----SDQALH-SFSEAKKLCSKHDhsATIVSIKDEDENKFVSRLMRENNNITMRVWLGLSQHSVDQSWS-------- 1612
Cdd:cd03595    12 CYKiayfQDSRRRlNFEEARQACREDG--GELLSIESENEQKLIERFIQTLRASDGDFWIGLRRSSQYNVTSsacsslyy 89
                          90
                  ....*....|..
gi 144446030 1613 WLDGSEVTFVKW 1624
Cdd:cd03595    90 WLDGSISTFRNW 101
Xlink pfam00193
Extracellular link domain;
658-693 4.28e-03

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 37.94  E-value: 4.28e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 144446030   658 KVFHAERIVRKR-NWEEAERFCQALGAHLSSFSHVDE 693
Cdd:pfam00193    1 GVFHLESPGRYKlTFQEAQAACAALGATLATPEQLYA 37
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
970-1090 4.81e-03

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


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 38.43  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  970 SLTFSQASDTCHSYGGTLPSVLSQIEQDFITSLLPDMEATLWIGLRWTAYEKINKWTDNRELTYSNFHPllvsGRlriPE 1049
Cdd:cd03591    10 EKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKP----GE---PN 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 144446030 1050 NFFEEESryhCALILNlqkspfTGTWNFTSCS-ERHFVslCQ 1090
Cdd:cd03591    83 NAGGGED---CVEMYT------SGKWNDVACNlTRLFV--CE 113
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
1248-1332 5.08e-03

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 38.47  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1248 WIPFQNCCYNFIITKNrhmatTQDEVHTKCQKLNpkSHILSIRDEKENNFVLEQLLYFNYmasWVMLGITYRNKSLMWFD 1327
Cdd:cd03593     5 WICYGNKCYYFSMEKK-----TWNESKEACSSKN--SSLLKIDDEEELEFLQSQIGSSSY---WIGLSREKSEKPWKWID 74

                  ....*
gi 144446030 1328 KTPLS 1332
Cdd:cd03593    75 GSPLN 79
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
1406-1513 5.53e-03

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


Pssm-ID: 153062  Cd Length: 115  Bit Score: 38.51  E-value: 5.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1406 YSVIQKKVTWYEALNMCSQSGGHLASVHNQNGQLFL-EDIVKRDGFPLWVGLSSHDGsESSFEWSDGSTFDYIPW-KGQT 1483
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLnGFALKYNLGYYWIDGNDINN-EGTWVDTDKKELEYKNWaPGEP 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 144446030 1484 SPG---NCV--LLDPKGTWKHEKCNSvKDGAICYK 1513
Cdd:cd03592    82 NNGrneNCLeiYIKDNGKWNDEPCSK-KKSAICYT 115
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
501-624 6.91e-03

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


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 38.51  E-value: 6.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030  501 CPPdeGWKRHGETCYKIYEDEVP----------FGTNCNL-TITSRFEQEYLNDLMKKYDKSlRKYFWTGLRDVDSCGEY 569
Cdd:cd03594     1 CPK--GWLPYKGNCYGYFRQPLSwsdaelfcqkYGPGAHLaSIHSPAEAAAIASLISSYQKA-YQPVWIGLHDPQQSRGW 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 144446030  570 NWATvggrRRAVTFSNWNFLEPASPGG-CVAMSTGKSVGKWEVKDCRSFKALsICK 624
Cdd:cd03594    78 EWSD----GSKLDYRSWDRNPPYARGGyCAELSRSTGFLKWNDANCEERNPF-ICK 128
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
1544-1650 9.11e-03

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


Pssm-ID: 153068  Cd Length: 117  Bit Score: 37.82  E-value: 9.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 144446030 1544 GHCYKSDQALHSFSEAKKLCSKHdHSATIVSIKDEDENKFVSRLMRENNNItmRVWLGLSQHSVDQSW--SWLDGSEVTF 1621
Cdd:cd03598     1 GRCYRFVKSPRTFRDAQVICRRC-YRGNLASIHSFAFNYRVQRLVSTLNQA--QVWIGGIITGKGRCRrfSWVDGSVWNY 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 144446030 1622 VKWE-NKSKSGVGRCSMLIASNETWKKVEC 1650
Cdd:cd03598    78 AYWApGQPGNRRGHCVELCTRGGHWRRAHC 107
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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