NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17509297|ref|NP_493166|]
View 

C-type LECtin [Caenorhabditis elegans]

Protein Classification

C-type lectin and CUB domain-containing protein( domain architecture ID 10637005)

C-type lectin and CUB (for complement C1r/C1s, Uegf, Bmp1) domain-containing protein; C-type lectin domain binds carbohydrate in a calcium-dependent manner, whereas CUB domain is found almost exclusively in extracellular and plasma membrane-associated proteins, many of which are developmentally regulated

Gene Ontology:  GO:0005509|GO:0030246
PubMed:  8510165|28876846

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 313-415 9.80e-29

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


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 108.65  E-value: 9.80e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297 313 RLMSDGIITSPNFPQNYFNNANCAYQISTLGSMRIALTFTFFNTQP-----YDLVTIYDGETSSSPVLGKYGGNQSSLTF 387
Cdd:cd00041   6 TASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncsYDYLEIYDGPSTSSPLLGRFCGSTLPPPI 85

                        90       100
                ....*....|....*....|....*...
gi 17509297 388 TSSRNNMLVTFITDGKDTSNGFSARFSS 415
Cdd:cd00041  86 ISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 166-284 1.17e-21

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: 89.97  E-value: 1.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297    166 YNGYCYTFSSTTNsinTFISAQGTCAQDCGYLASIHSPLEIRYINTFAPHA----YFYIGAIW-KNDGSLYWLDNSPW-D 239
Cdd:smart00034   8 YGGKCYKFSTEKK---TWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSgssdYYWIGLSDpDSNGSWQWSDGSGPvS 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 17509297    240 YNNIDPVQTN-RVDYCLTMSTTNfgsspaGFWFSTNCNNPGYYICK 284
Cdd:smart00034  85 YSNWAPGEPNnSSGDCVVLSTSG------GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 26-153 1.74e-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: 86.50  E-value: 1.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297     26 CTDGFTLINSKCLKLFPSLVSHTVAESSCNSYGATLVTVKNVKDDEAIAAIAGSSTP--LIWLGLYCFDSDpAQCLWDDV 103
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdYYWIGLSDPDSN-GSWQWSDG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 17509297    104 SGSaSNYNNFSAGFPLVVLGQCVYYSTQGalaGKWLSEECESQHvAYICE 153
Cdd:smart00034  80 SGP-VSYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKL-PFVCE 124
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 313-415 9.80e-29

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


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 108.65  E-value: 9.80e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297 313 RLMSDGIITSPNFPQNYFNNANCAYQISTLGSMRIALTFTFFNTQP-----YDLVTIYDGETSSSPVLGKYGGNQSSLTF 387
Cdd:cd00041   6 TASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncsYDYLEIYDGPSTSSPLLGRFCGSTLPPPI 85

                        90       100
                ....*....|....*....|....*...
gi 17509297 388 TSSRNNMLVTFITDGKDTSNGFSARFSS 415
Cdd:cd00041  86 ISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 318-413 4.21e-27

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 104.01  E-value: 4.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297    318 GIITSPNFPQNYFNNANCAYQISTLGSMRIALTFTFFNTQP-----YDLVTIYDGETSSSPVLGKY-GGNQSSLTFTSSR 391
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESsdnceYDYVEIYDGPSASSPLLGRFcGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 17509297    392 NNMLVTFITDGKDTSNGFSARF 413
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
316-413 4.03e-23

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 93.13  E-value: 4.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297   316 SDGIITSPNFPQNYFNNANCAYQISTLGSMRIALTFTFFNTQ-----PYDLVTIYDGETSSSPVLGKYGGNQSSLTFTSS 390
Cdd:pfam00431   8 SSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdecGYDYVEIRDGPSASSPLLGRFCGSGIPEDIVSS 87

                          90       100
                  ....*....|....*....|...
gi 17509297   391 RNNMLVTFITDGKDTSNGFSARF 413
Cdd:pfam00431  88 SNQMTIKFVSDASVQKRGFKATY 110
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 166-284 1.17e-21

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: 89.97  E-value: 1.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297    166 YNGYCYTFSSTTNsinTFISAQGTCAQDCGYLASIHSPLEIRYINTFAPHA----YFYIGAIW-KNDGSLYWLDNSPW-D 239
Cdd:smart00034   8 YGGKCYKFSTEKK---TWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSgssdYYWIGLSDpDSNGSWQWSDGSGPvS 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 17509297    240 YNNIDPVQTN-RVDYCLTMSTTNfgsspaGFWFSTNCNNPGYYICK 284
Cdd:smart00034  85 YSNWAPGEPNnSSGDCVVLSTSG------GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 26-153 1.74e-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: 86.50  E-value: 1.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297     26 CTDGFTLINSKCLKLFPSLVSHTVAESSCNSYGATLVTVKNVKDDEAIAAIAGSSTP--LIWLGLYCFDSDpAQCLWDDV 103
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdYYWIGLSDPDSN-GSWQWSDG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 17509297    104 SGSaSNYNNFSAGFPLVVLGQCVYYSTQGalaGKWLSEECESQHvAYICE 153
Cdd:smart00034  80 SGP-VSYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKL-PFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 169-285 4.63e-15

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: 71.11  E-value: 4.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297 169 YCYTFSSTTNsinTFISAQGTCAQDCGYLASIHSPLEIRYINTFA---PHAYFYIGAIWKN-DGSLYWLDNSP-WDYNNI 243
Cdd:cd00037   1 SCYKFSTEKL---TWEEAQEYCRSLGGHLASIHSEEENDFLASLLkksSSSDVWIGLNDLSsEGTWKWSDGSPlVDYTNW 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17509297 244 DPVQ--TNRVDYCLTMSttnfgSSPAGFWFSTNCNNPGYYICKR 285
Cdd:cd00037  78 APGEpnPGGSEDCVVLS-----SSSDGKWNDVSCSSKLPFICEK 116
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 36-153 1.83e-13

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: 66.49  E-value: 1.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297  36 KCLKLFPSLVSHTVAESSCNSYGATLVTVKNVKDDEAIAAIAGSSTPL-IWLGLYCFDSDpAQCLWDDvSGSASNYNNFS 114
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSE-GTWKWSD-GSPLVDYTNWA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17509297 115 AGFPLVVLGQ-CVYYSTQGalAGKWLSEECESQHvAYICE 153
Cdd:cd00037  79 PGEPNPGGSEdCVVLSSSS--DGKWNDVSCSSKL-PFICE 115
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 186-285 5.83e-10

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 56.33  E-value: 5.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297   186 AQGTCAQDCGYLASIHSPLEIRYINTFAPHA--YFYIG-AIWKNDGSLYWLDNSPWDYNNIDPVQTNRVD--YCLTMSTT 260
Cdd:pfam00059   7 AREACRKLGGHLVSINSAEELDFLSSTLKKSnkYFWIGlTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGEneDCVELSSS 86

                          90       100
                  ....*....|....*....|....*
gi 17509297   261 NfgsspaGFWFSTNCNNPGYYICKR 285
Cdd:pfam00059  87 S------GKWNDENCNSKNPFVCEK 105
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 50-153 2.93e-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: 45.55  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297    50 AESSCNSYGATLVTVKNVKDDEAIAAIAGSSTPLIWLGLYcFDSDPAQCLWDDvsGSASNYNNFSAGFPLV-VLGQCVYY 128
Cdd:pfam00059   7 AREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLT-DRKNEGTWKWVD--GSPVNYTNWAPEPNNNgENEDCVEL 83

                          90       100
                  ....*....|....*....|....*
gi 17509297   129 STQgalAGKWLSEECESQHvAYICE 153
Cdd:pfam00059  84 SSS---SGKWNDENCNSKN-PFVCE 104
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 166-283 8.82e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 36.77  E-value: 8.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297  166 YNGYCYTFSSTTNSINtfiSAQGTCAQDCGYLASIHSPLEIRYINTFAPHAYFYIG----AIWKNDGSLYWldnspwdyn 241
Cdd:PHA03097  53 YNNKCYTFSENITNKH---LAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGiekkKGDDDDREVLD--------- 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 17509297  242 niDPVQTNRVDYCLTMSTTNFGSSpagfwfstNCNNPGYYIC 283
Cdd:PHA03097 121 --KVVKPPKSGKCAYLKDKTIISS--------NCNATKGWIC 152
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 313-415 9.80e-29

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


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 108.65  E-value: 9.80e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297 313 RLMSDGIITSPNFPQNYFNNANCAYQISTLGSMRIALTFTFFNTQP-----YDLVTIYDGETSSSPVLGKYGGNQSSLTF 387
Cdd:cd00041   6 TASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncsYDYLEIYDGPSTSSPLLGRFCGSTLPPPI 85

                        90       100
                ....*....|....*....|....*...
gi 17509297 388 TSSRNNMLVTFITDGKDTSNGFSARFSS 415
Cdd:cd00041  86 ISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 318-413 4.21e-27

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 104.01  E-value: 4.21e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297    318 GIITSPNFPQNYFNNANCAYQISTLGSMRIALTFTFFNTQP-----YDLVTIYDGETSSSPVLGKY-GGNQSSLTFTSSR 391
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESsdnceYDYVEIYDGPSASSPLLGRFcGSEAPPPVISSSS 80

                           90       100
                   ....*....|....*....|..
gi 17509297    392 NNMLVTFITDGKDTSNGFSARF 413
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
316-413 4.03e-23

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 93.13  E-value: 4.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297   316 SDGIITSPNFPQNYFNNANCAYQISTLGSMRIALTFTFFNTQ-----PYDLVTIYDGETSSSPVLGKYGGNQSSLTFTSS 390
Cdd:pfam00431   8 SSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdecGYDYVEIRDGPSASSPLLGRFCGSGIPEDIVSS 87

                          90       100
                  ....*....|....*....|...
gi 17509297   391 RNNMLVTFITDGKDTSNGFSARF 413
Cdd:pfam00431  88 SNQMTIKFVSDASVQKRGFKATY 110
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 166-284 1.17e-21

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: 89.97  E-value: 1.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297    166 YNGYCYTFSSTTNsinTFISAQGTCAQDCGYLASIHSPLEIRYINTFAPHA----YFYIGAIW-KNDGSLYWLDNSPW-D 239
Cdd:smart00034   8 YGGKCYKFSTEKK---TWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSgssdYYWIGLSDpDSNGSWQWSDGSGPvS 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 17509297    240 YNNIDPVQTN-RVDYCLTMSTTNfgsspaGFWFSTNCNNPGYYICK 284
Cdd:smart00034  85 YSNWAPGEPNnSSGDCVVLSTSG------GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 26-153 1.74e-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: 86.50  E-value: 1.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297     26 CTDGFTLINSKCLKLFPSLVSHTVAESSCNSYGATLVTVKNVKDDEAIAAIAGSSTP--LIWLGLYCFDSDpAQCLWDDV 103
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSsdYYWIGLSDPDSN-GSWQWSDG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 17509297    104 SGSaSNYNNFSAGFPLVVLGQCVYYSTQGalaGKWLSEECESQHvAYICE 153
Cdd:smart00034  80 SGP-VSYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKL-PFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 169-285 4.63e-15

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: 71.11  E-value: 4.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297 169 YCYTFSSTTNsinTFISAQGTCAQDCGYLASIHSPLEIRYINTFA---PHAYFYIGAIWKN-DGSLYWLDNSP-WDYNNI 243
Cdd:cd00037   1 SCYKFSTEKL---TWEEAQEYCRSLGGHLASIHSEEENDFLASLLkksSSSDVWIGLNDLSsEGTWKWSDGSPlVDYTNW 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 17509297 244 DPVQ--TNRVDYCLTMSttnfgSSPAGFWFSTNCNNPGYYICKR 285
Cdd:cd00037  78 APGEpnPGGSEDCVVLS-----SSSDGKWNDVSCSSKLPFICEK 116
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 36-153 1.83e-13

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: 66.49  E-value: 1.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297  36 KCLKLFPSLVSHTVAESSCNSYGATLVTVKNVKDDEAIAAIAGSSTPL-IWLGLYCFDSDpAQCLWDDvSGSASNYNNFS 114
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSdVWIGLNDLSSE-GTWKWSD-GSPLVDYTNWA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17509297 115 AGFPLVVLGQ-CVYYSTQGalAGKWLSEECESQHvAYICE 153
Cdd:cd00037  79 PGEPNPGGSEdCVVLSSSS--DGKWNDVSCSSKL-PFICE 115
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 186-285 5.83e-10

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 56.33  E-value: 5.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297   186 AQGTCAQDCGYLASIHSPLEIRYINTFAPHA--YFYIG-AIWKNDGSLYWLDNSPWDYNNIDPVQTNRVD--YCLTMSTT 260
Cdd:pfam00059   7 AREACRKLGGHLVSINSAEELDFLSSTLKKSnkYFWIGlTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGEneDCVELSSS 86

                          90       100
                  ....*....|....*....|....*
gi 17509297   261 NfgsspaGFWFSTNCNNPGYYICKR 285
Cdd:pfam00059  87 S------GKWNDENCNSKNPFVCEK 105
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 26-153 5.63e-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: 51.22  E-value: 5.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297  26 CTDGFTLINSKCLKLFPSLVSHTVAESSCNSY--GATLVTVKNVKDDEAIA----AIAGSSTPlIWLGLYcfdsDPAQCL 99
Cdd:cd03594   1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIAslisSYQKAYQP-VWIGLH----DPQQSR 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17509297 100 -WDDVSGSASNYNNFSAGFPLVVLGQCVYYSTQGALAgKWLSEECESQHvAYICE 153
Cdd:cd03594  76 gWEWSDGSKLDYRSWDRNPPYARGGYCAELSRSTGFL-KWNDANCEERN-PFICK 128
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 162-285 3.12e-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: 48.87  E-value: 3.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297 162 CDFNYNGY---CYTFSSTTNSINtfiSAQGTCAQDCGYLASIHSPLEIRYINTFAPHAYFYIGAIWKNDGSLY-WLDNSP 237
Cdd:cd03593   1 CPKDWICYgnkCYYFSMEKKTWN---ESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWkWIDGSP 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 17509297 238 WDyNNIDPVQTNRVDYCLTMSTTNFgsspagfwFSTNCNNPGYYICKR 285
Cdd:cd03593  78 LN-NLFNIRGSTKSGNCAYLSSTGI--------YSEDCSTKKRWICEK 116
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 26-153 4.57e-07

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: 48.54  E-value: 4.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297  26 CTDGfTLINSKCLKLFPSLVSHTVAESSCNSYGATLVTVKNVKDDEAIAAIAGSSTPL---IWLGLycfdSD-PAQCLWD 101
Cdd:cd03596   1 CLKG-TKIHKKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGnweVWLGI----NDmVAEGKWV 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17509297 102 DVSGSASNYNNFSAGFPLVVLG----QCVYYStqGALAGKWLSEECESQhVAYICE 153
Cdd:cd03596  76 DVNGSPISYFNWEREITAQPDGgkreNCVALS--SSAQGKWFDEDCRRE-KPYVCE 128
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 50-153 2.93e-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: 45.55  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297    50 AESSCNSYGATLVTVKNVKDDEAIAAIAGSSTPLIWLGLYcFDSDPAQCLWDDvsGSASNYNNFSAGFPLV-VLGQCVYY 128
Cdd:pfam00059   7 AREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLT-DRKNEGTWKWVD--GSPVNYTNWAPEPNNNgENEDCVEL 83

                          90       100
                  ....*....|....*....|....*
gi 17509297   129 STQgalAGKWLSEECESQHvAYICE 153
Cdd:pfam00059  84 SSS---SGKWNDENCNSKN-PFVCE 104
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 168-283 1.37e-05

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: 43.98  E-value: 1.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297 168 GYCYTFSSTTNsinTFISAQGTCaQDC--GYLASIHSPL---EIRYINTFAPHAYFYIGAIWKNDG---SLYWLDNSPWD 239
Cdd:cd03598   1 GRCYRFVKSPR---TFRDAQVIC-RRCyrGNLASIHSFAfnyRVQRLVSTLNQAQVWIGGIITGKGrcrRFSWVDGSVWN 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 17509297 240 YNNIDPVQ-TNRVDYCLTMSTTNfgsspaGFWFSTNCNNPGYYIC 283
Cdd:cd03598  77 YAYWAPGQpGNRRGHCVELCTRG------GHWRRAHCKLRRPFIC 115
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 166-284 1.65e-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: 44.27  E-value: 1.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297 166 YNGYCY-------TFSSTTNSINTFisaqgTCAQDCGYLASIHSPLEIRYIntfapHAYF-------YIGAIW------K 225
Cdd:cd03589   8 FGGYCYrffgdrlTWEEAELRCRSF-----SIPGLIAHLVSIHSQEENDFV-----YDLFessrgpdTPYGLWiglhdrT 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17509297 226 NDGSLYWLDNSPWDYNNIDPVQTNrvDY-----CLTMSTTNfgsSPAGFWFSTNCNNPGYYICK 284
Cdd:cd03589  78 SEGPFEWTDGSPVDFTKWAGGQPD--NYggnedCVQMWRRG---DAGQSWNDMPCDAVFPYICK 136
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 171-282 4.85e-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: 42.41  E-value: 4.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297 171 YTFSSTTNsinTFISAQGTCAQDCGYLASIHSPLEIRYI-NTFAPHAYFYIGAiWK--NDGSLYWLDNSPWDYNNIDPVQ 247
Cdd:cd03603   3 YKFVDGGM---TWEAAQTLAESLGGHLVTINSAEENDWLlSNFGGYGASWIGA-SDaaTEGTWKWSDGEESTYTNWGSGE 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 17509297 248 TNRV-----DYcltmSTTNFGSSPAGFW--FSTNCNNPGYYI 282
Cdd:cd03603  79 PHNNgggneDY----AAINHFPGISGKWndLANSYNTLGYVI 116
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 164-285 1.90e-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: 41.14  E-value: 1.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297 164 FNYNGYCYTFSSTTNSintFISAQGTCAQDCGYLASIHSPLEIRYINTFAPHAYFYigaiW------KNDGSLYWLDNSP 237
Cdd:cd03590   6 KSFQSSCYFFSTEKKS---WEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSY----WiglsdeETEGEWKWVDGTP 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17509297 238 -------WDYNNIDPVQTNRVDyCLTMSttnfgsSPAGFWFSTNCNNPGYYICKR 285
Cdd:cd03590  79 lnssktfWHPGEPNNWGGGGED-CAELV------YDSGGWNDVPCNLEYRWICEK 126
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 164-284 1.76e-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: 38.12  E-value: 1.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297 164 FNYNGYCYTFsstTNSINTFISAQGTCAQ--DCGYLASIHSPLEI----RYINTFAP-HAYFYIGAI-WKNDGSLYWLDN 235
Cdd:cd03594   6 LPYKGNCYGY---FRQPLSWSDAELFCQKygPGAHLASIHSPAEAaaiaSLISSYQKaYQPVWIGLHdPQQSRGWEWSDG 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17509297 236 SPWDYNNIDPVQT-NRVDYCLTMS-TTNFGSspagfWFSTNCNNPGYYICK 284
Cdd:cd03594  83 SKLDYRSWDRNPPyARGGYCAELSrSTGFLK-----WNDANCEERNPFICK 128
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 170-284 2.16e-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: 38.33  E-value: 2.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297 170 CYT---FSSTTNSINtFISAQGTCAQDCGYLASIHSPLEIRYINTF-----APHAYFYIGaIWKNDGSL----------Y 231
Cdd:cd03595  12 CYKiayFQDSRRRLN-FEEARQACREDGGELLSIESENEQKLIERFiqtlrASDGDFWIG-LRRSSQYNvtssacsslyY 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17509297 232 WLDNSPWDYNN--IDPVQTNrVDYCLTMSTTNfgSSPAGF-------WFSTNCNNPGYYICK 284
Cdd:cd03595  90 WLDGSISTFRNwyVDEPSCG-SEVCVVMYHQP--SAPAGQggpylfqWNDDNCNMKNNFICK 148
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 176-285 3.09e-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: 37.35  E-value: 3.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297 176 TTNSINTFISAQGTCAQDCGYLASIHSPLEIRYINTFAPH---AYFYIGaIWKNDGSLYWLD--NSPWDYNNIDPVQTN- 249
Cdd:cd03592   5 YSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKynlGYYWID-GNDINNEGTWVDtdKKELEYKNWAPGEPNn 83

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 17509297 250 -RVDYCLTMSTTnfgssPAGFWFSTNCNNPGYYICKR 285
Cdd:cd03592  84 gRNENCLEIYIK-----DNGKWNDEPCSKKKSAICYT 115
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 37-153 4.55e-03

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: 37.41  E-value: 4.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297  37 CLKLFPSLVSHTVAESSCNSYGATLVTVKNVKDDEAIAAIAGSSTP-------LIWLGLycfDSDPAQCLWDD------- 102
Cdd:cd03600   6 CYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGrhgrgslRLWIGL---QREPRQCSDPSlplrgfs 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17509297 103 --VSGSASNYNNFSAGFPLVVLGQ-CVYYSTQGALAG--KWLSEECESQHVAYICE 153
Cdd:cd03600  83 wvTGDQDTDFSNWLQEPAGTCTSPrCVALSAAGSTPDnlKWKDGPCSARADGYLCK 138
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 36-152 8.47e-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: 35.89  E-value: 8.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297  36 KCLKLFPSLVSHTVAESSCNS-YGATLVTVKNVKDDEAIAAIAGSSTP-LIWLG--LYCfDSDPAQCLWDDvsGSASNYN 111
Cdd:cd03598   2 RCYRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLVSTLNQaQVWIGgiITG-KGRCRRFSWVD--GSVWNYA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17509297 112 NFSAGFPLVVLGQCVYYSTQGalaGKWLSEECeSQHVAYIC 152
Cdd:cd03598  79 YWAPGQPGNRRGHCVELCTRG---GHWRRAHC-KLRRPFIC 115
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 166-283 8.82e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 36.77  E-value: 8.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509297  166 YNGYCYTFSSTTNSINtfiSAQGTCAQDCGYLASIHSPLEIRYINTFAPHAYFYIG----AIWKNDGSLYWldnspwdyn 241
Cdd:PHA03097  53 YNNKCYTFSENITNKH---LAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGiekkKGDDDDREVLD--------- 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 17509297  242 niDPVQTNRVDYCLTMSTTNFGSSpagfwfstNCNNPGYYIC 283
Cdd:PHA03097 121 --KVVKPPKSGKCAYLKDKTIISS--------NCNATKGWIC 152
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH