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Conserved domains on  [gi|17531345|ref|NP_494427|]
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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

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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 ...
 301-408 3.38e-27

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: 104.42  E-value: 3.38e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345 301 CNSTV-LMTPGIITSPNYPQNYDNNVYCSYKLSTLGSYNILLEFTSFSTEE----NVDLVTVYDGESTNGLKIGTYSGSR 375
Cdd:cd00041   1 CGGTLtASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGST 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 17531345 376 EPFHLISKGNNFFLAFSTDSRNVFKGFSASFVA 408
Cdd:cd00041  81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 21-145 2.04e-24

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: 97.29  E-value: 2.04e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345     21 CTDGFTLVNGKCLMMFKDESNHDDAESFCRLFRGTLFDVKNAIDNRAVASFIGSQV--ETVWMGLFCF-NNNLCLWDDNS 97
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGssDYYWIGLSDPdSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 17531345     98 GSTaAYDNFSGGYPEVTIGSCVYYATQGtlaGKWISADCTDRRSFVCE 145
Cdd:smart00034  81 GPV-SYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 165-275 3.57e-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: 82.65  E-value: 3.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345    165 FHRDLYSFTTAQTICEEECGNLVSIHSANENRYVMTIAS-HTTQANVLIGGMWPM-DHVNTWVDGT-MWDYSNIDSGYDP 241
Cdd:smart00034  15 FSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnSGSSDYYWIGLSDPDsNGSWQWSDGSgPVSYSNWAPGEPN 94

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 17531345    242 --TNHCIAMANNAtseynlGQWFGVDCKDYYSFVCK 275
Cdd:smart00034  95 nsSGDCVVLSTSG------GKWNDVSCTSKLPFVCE 124
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 301-408 3.38e-27

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: 104.42  E-value: 3.38e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345 301 CNSTV-LMTPGIITSPNYPQNYDNNVYCSYKLSTLGSYNILLEFTSFSTEE----NVDLVTVYDGESTNGLKIGTYSGSR 375
Cdd:cd00041   1 CGGTLtASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGST 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 17531345 376 EPFHLISKGNNFFLAFSTDSRNVFKGFSASFVA 408
Cdd:cd00041  81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 310-406 1.67e-25

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: 99.39  E-value: 1.67e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345    310 GIITSPNYPQNYDNNVYCSYKLSTLGSYNILLEFTSFSTEENV----DLVTVYDGESTNGLKIGTYSGSREPFHLI-SKG 384
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGRFCGSEAPPPVIsSSS 80

                           90       100
                   ....*....|....*....|..
gi 17531345    385 NNFFLAFSTDSRNVFKGFSASF 406
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 21-145 2.04e-24

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: 97.29  E-value: 2.04e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345     21 CTDGFTLVNGKCLMMFKDESNHDDAESFCRLFRGTLFDVKNAIDNRAVASFIGSQV--ETVWMGLFCF-NNNLCLWDDNS 97
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGssDYYWIGLSDPdSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 17531345     98 GSTaAYDNFSGGYPEVTIGSCVYYATQGtlaGKWISADCTDRRSFVCE 145
Cdd:smart00034  81 GPV-SYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 165-275 3.57e-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: 82.65  E-value: 3.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345    165 FHRDLYSFTTAQTICEEECGNLVSIHSANENRYVMTIAS-HTTQANVLIGGMWPM-DHVNTWVDGT-MWDYSNIDSGYDP 241
Cdd:smart00034  15 FSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnSGSSDYYWIGLSDPDsNGSWQWSDGSgPVSYSNWAPGEPN 94

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 17531345    242 --TNHCIAMANNAtseynlGQWFGVDCKDYYSFVCK 275
Cdd:smart00034  95 nsSGDCVVLSTSG------GKWNDVSCTSKLPFVCE 124
CUB pfam00431
CUB domain;
301-406 5.21e-18

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 78.88  E-value: 5.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345   301 CNSTVLMTPGIITSPNYPQNYDNNVYCSYKLSTLGSYNILLEFTSFSTEENV----DLVTVYDGESTNGLKIGTYSGSRE 376
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDecgyDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 17531345   377 PFHLISKGNNFFLAFSTDSRNVFKGFSASF 406
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 165-276 7.13e-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: 76.12  E-value: 7.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345 165 FHRDLYSFTTAQTICEEECGNLVSIHSANENRYVMTIASHTTQANVLIGG-MWPMDHVNTWVDGT-MWDYSNIDSGYDPT 242
Cdd:cd00037   5 FSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLnDLSSEGTWKWSDGSpLVDYTNWAPGEPNP 84

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 17531345 243 N---HCIAMANNATseynlGQWFGVDCKDYYSFVCKR 276
Cdd:cd00037  85 GgseDCVVLSSSSD-----GKWNDVSCSSKLPFICEK 116
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 31-145 1.15e-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: 72.65  E-value: 1.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345  31 KCLMMFKDESNHDDAESFCRLFRGTLFDVKNAIDNRAVASFI-GSQVETVWMGLFCFN-NNLCLWDDNSgSTAAYDNFSG 108
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkKSSSSDVWIGLNDLSsEGTWKWSDGS-PLVDYTNWAP 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 17531345 109 GYPEVT-IGSCVYYATQGTlaGKWISADCTDRRSFVCE 145
Cdd:cd00037  80 GEPNPGgSEDCVVLSSSSD--GKWNDVSCSSKLPFICE 115
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 41-146 3.78e-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: 54.02  E-value: 3.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345    41 NHDDAESFCRLFRGTLFDVKNAIDNRAVASFIGSQVETVWMGLFCFNNNLCL-WDDNSGSTaaYDNFSGGYPEVT-IGSC 118
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWkWVDGSPVN--YTNWAPEPNNNGeNEDC 80

                          90       100
                  ....*....|....*....|....*...
gi 17531345   119 VYYATQgtlAGKWISADCTDRRSFVCET 146
Cdd:pfam00059  81 VELSSS---SGKWNDENCNSKNPFVCEK 105
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 170-276 1.80e-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: 43.24  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345   170 YSFTTAQTICEEECGNLVSIHSANENRYVMTIASHTTQaNVLIG-GMWPMDHVNTWVDGTMWDYSN---IDSGYDPTNHC 245
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNK-YFWIGlTDRKNEGTWKWVDGSPVNYTNwapEPNNNGENEDC 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 17531345   246 IAMannatsEYNLGQWFGVDCKDYYSFVCKR 276
Cdd:pfam00059  81 VEL------SSSSGKWNDENCNSKNPFVCEK 105
 
Name Accession Description Interval E-value
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 301-408 3.38e-27

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: 104.42  E-value: 3.38e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345 301 CNSTV-LMTPGIITSPNYPQNYDNNVYCSYKLSTLGSYNILLEFTSFSTEE----NVDLVTVYDGESTNGLKIGTYSGSR 375
Cdd:cd00041   1 CGGTLtASTSGTISSPNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLESspncSYDYLEIYDGPSTSSPLLGRFCGST 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 17531345 376 EPFHLISKGNNFFLAFSTDSRNVFKGFSASFVA 408
Cdd:cd00041  81 LPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 310-406 1.67e-25

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: 99.39  E-value: 1.67e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345    310 GIITSPNYPQNYDNNVYCSYKLSTLGSYNILLEFTSFSTEENV----DLVTVYDGESTNGLKIGTYSGSREPFHLI-SKG 384
Cdd:smart00042   1 GTITSPNYPQSYPNNLDCVWTIRAPPGYRIELQFTDFDLESSDnceyDYVEIYDGPSASSPLLGRFCGSEAPPPVIsSSS 80

                           90       100
                   ....*....|....*....|..
gi 17531345    385 NNFFLAFSTDSRNVFKGFSASF 406
Cdd:smart00042  81 NSLTLTFVSDSSVQKRGFSARY 102
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 21-145 2.04e-24

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: 97.29  E-value: 2.04e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345     21 CTDGFTLVNGKCLMMFKDESNHDDAESFCRLFRGTLFDVKNAIDNRAVASFIGSQV--ETVWMGLFCF-NNNLCLWDDNS 97
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGssDYYWIGLSDPdSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 17531345     98 GSTaAYDNFSGGYPEVTIGSCVYYATQGtlaGKWISADCTDRRSFVCE 145
Cdd:smart00034  81 GPV-SYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 165-275 3.57e-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: 82.65  E-value: 3.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345    165 FHRDLYSFTTAQTICEEECGNLVSIHSANENRYVMTIAS-HTTQANVLIGGMWPM-DHVNTWVDGT-MWDYSNIDSGYDP 241
Cdd:smart00034  15 FSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKnSGSSDYYWIGLSDPDsNGSWQWSDGSgPVSYSNWAPGEPN 94

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 17531345    242 --TNHCIAMANNAtseynlGQWFGVDCKDYYSFVCK 275
Cdd:smart00034  95 nsSGDCVVLSTSG------GKWNDVSCTSKLPFVCE 124
CUB pfam00431
CUB domain;
301-406 5.21e-18

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 78.88  E-value: 5.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345   301 CNSTVLMTPGIITSPNYPQNYDNNVYCSYKLSTLGSYNILLEFTSFSTEENV----DLVTVYDGESTNGLKIGTYSGSRE 376
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDecgyDYVEIRDGPSASSPLLGRFCGSGI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 17531345   377 PFHLISKGNNFFLAFSTDSRNVFKGFSASF 406
Cdd:pfam00431  81 PEDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 165-276 7.13e-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: 76.12  E-value: 7.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345 165 FHRDLYSFTTAQTICEEECGNLVSIHSANENRYVMTIASHTTQANVLIGG-MWPMDHVNTWVDGT-MWDYSNIDSGYDPT 242
Cdd:cd00037   5 FSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDVWIGLnDLSSEGTWKWSDGSpLVDYTNWAPGEPNP 84

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 17531345 243 N---HCIAMANNATseynlGQWFGVDCKDYYSFVCKR 276
Cdd:cd00037  85 GgseDCVVLSSSSD-----GKWNDVSCSSKLPFICEK 116
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 31-145 1.15e-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: 72.65  E-value: 1.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345  31 KCLMMFKDESNHDDAESFCRLFRGTLFDVKNAIDNRAVASFI-GSQVETVWMGLFCFN-NNLCLWDDNSgSTAAYDNFSG 108
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLkKSSSSDVWIGLNDLSsEGTWKWSDGS-PLVDYTNWAP 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 17531345 109 GYPEVT-IGSCVYYATQGTlaGKWISADCTDRRSFVCE 145
Cdd:cd00037  80 GEPNPGgSEDCVVLSSSSD--GKWNDVSCSSKLPFICE 115
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 44-144 1.32e-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: 55.07  E-value: 1.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345  44 DAESFCRLFRGTLFDVKNAIDNRAVASFIGSQVETVWMGLFcFNNNLCLWDDNSGSTAAYdnfSGGYPEVTIGSCVYYat 123
Cdd:cd03602  14 EAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAAWIGLY-RDVDSWRWSDGSESSFRN---WNTFQPFGQGDCATM-- 87

                        90       100
                ....*....|....*....|.
gi 17531345 124 qgTLAGKWISADCTDRRSFVC 144
Cdd:cd03602  88 --YSSGRWYAALCSALKPFIC 106
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 41-146 3.78e-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: 54.02  E-value: 3.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345    41 NHDDAESFCRLFRGTLFDVKNAIDNRAVASFIGSQVETVWMGLFCFNNNLCL-WDDNSGSTaaYDNFSGGYPEVT-IGSC 118
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWkWVDGSPVN--YTNWAPEPNNNGeNEDC 80

                          90       100
                  ....*....|....*....|....*...
gi 17531345   119 VYYATQgtlAGKWISADCTDRRSFVCET 146
Cdd:pfam00059  81 VELSSS---SGKWNDENCNSKNPFVCEK 105
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 30-144 2.19e-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: 52.07  E-value: 2.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345  30 GKCLMMFKDESNHDDAESFCR-LFRGTLFDVKN-AIDNRAVASFIGSQVETVWMGLFCFNNNLC---LWDDnsGSTAAYD 104
Cdd:cd03598   1 GRCYRFVKSPRTFRDAQVICRrCYRGNLASIHSfAFNYRVQRLVSTLNQAQVWIGGIITGKGRCrrfSWVD--GSVWNYA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17531345 105 NFSGGYPEVTIGSCVYYATQGtlaGKWISADCTDRRSFVC 144
Cdd:cd03598  79 YWAPGQPGNRRGHCVELCTRG---GHWRRAHCKLRRPFIC 115
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 172-274 2.73e-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: 51.68  E-value: 2.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345 172 FTTAQTICEEeC--GNLVSIHSANENRYVMTIASHTTQANVLIGGM---WPMDHVNTWVDGTMWDYSNIDSGyDPTN--- 243
Cdd:cd03598  13 FRDAQVICRR-CyrGNLASIHSFAFNYRVQRLVSTLNQAQVWIGGIitgKGRCRRFSWVDGSVWNYAYWAPG-QPGNrrg 90

                        90       100       110
                ....*....|....*....|....*....|.
gi 17531345 244 HCIAMANNAtseynlGQWFGVDCKDYYSFVC 274
Cdd:cd03598  91 HCVELCTRG------GHWRRAHCKLRRPFIC 115
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 21-145 5.09e-07

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: 48.52  E-value: 5.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345  21 CTDGFTLVNGKCLMMFKDESNHDDAESFCRLFR--GTLFDVKNAIDNRAVASFI-GSQVET--VWMGLFCFNNNLClWDD 95
Cdd:cd03594   1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYGpgAHLASIHSPAEAAAIASLIsSYQKAYqpVWIGLHDPQQSRG-WEW 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17531345  96 NSGSTAAYDNFSGGYPEVTIGSCVYYaTQGTLAGKWISADCTDRRSFVCE 145
Cdd:cd03594  80 SDGSKLDYRSWDRNPPYARGGYCAEL-SRSTGFLKWNDANCEERNPFICK 128
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 165-276 1.39e-05

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: 44.22  E-value: 1.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345 165 FHRDLYSFTTAQTICEEECGNLVSIHSANENRYVMTIASHttQANVLIG-------GMWpmdhvnTWVDGT-------MW 230
Cdd:cd03590  15 FSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSG--NRSYWIGlsdeeteGEW------KWVDGTplnssktFW 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 17531345 231 DYSNIDSGYDPTNHCiamannATSEYNLGQWFGVDCKDYYSFVCKR 276
Cdd:cd03590  87 HPGEPNNWGGGGEDC------AELVYDSGGWNDVPCNLEYRWICEK 126
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 184-275 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 17531345 184 GNLVSIHSANENRYVMTIASHTTQANvLIGGMWP--MDHVNT----WVDGTMWDYSNIDSGyDPTNH-----CIAMANNA 252
Cdd:cd03589  39 AHLVSIHSQEENDFVYDLFESSRGPD-TPYGLWIglHDRTSEgpfeWTDGSPVDFTKWAGG-QPDNYggnedCVQMWRRG 116

                        90       100
                ....*....|....*....|...
gi 17531345 253 TSeynLGQWFGVDCKDYYSFVCK 275
Cdd:cd03589 117 DA---GQSWNDMPCDAVFPYICK 136
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 170-276 1.80e-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: 43.24  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345   170 YSFTTAQTICEEECGNLVSIHSANENRYVMTIASHTTQaNVLIG-GMWPMDHVNTWVDGTMWDYSN---IDSGYDPTNHC 245
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNK-YFWIGlTDRKNEGTWKWVDGSPVNYTNwapEPNNNGENEDC 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 17531345   246 IAMannatsEYNLGQWFGVDCKDYYSFVCKR 276
Cdd:pfam00059  81 VEL------SSSSGKWNDENCNSKNPFVCEK 105
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 169-274 7.35e-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: 41.59  E-value: 7.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345 169 LYSFTTAQTICEEECGNLVSIHSANENRYVMTIASHTTQAnVLIGGMWPMDHVnTWVDGTMWDYSNIDSGYDPTN-HCIA 247
Cdd:cd03602   9 SKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSA-AWIGLYRDVDSW-RWSDGSESSFRNWNTFQPFGQgDCAT 86

                        90       100
                ....*....|....*....|....*..
gi 17531345 248 MANNatseynlGQWFGVDCKDYYSFVC 274
Cdd:cd03602  87 MYSS-------GRWYAALCSALKPFIC 106
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 165-276 1.40e-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: 41.21  E-value: 1.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345 165 FHRDLYSFTTAQTICEEECGNLVSIHSANENRYVMTIASHTTQANVLIGGmwpMDHVN--TWVD--GTMWDYSNIDSGyD 240
Cdd:cd03592   5 YSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYYWIDG---NDINNegTWVDtdKKELEYKNWAPG-E 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 17531345 241 PTN----HCIAMANNATseynlGQWFGVDCKDYYSFVCKR 276
Cdd:cd03592  81 PNNgrneNCLEIYIKDN-----GKWNDEPCSKKKSAICYT 115
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 172-274 1.88e-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: 40.74  E-value: 1.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345 172 FTTAQTICEEECGNLVSIHSANENRYVMTIASHTTQAnVLIGgmwpmdhVN--------TWVDGTMWDYSNIDSGyDPTN 243
Cdd:cd03591  13 FDDAQKLCSEAGGTLAMPRNAAENAAIASYVKKGNTY-AFIG-------ITdletegqfVYLDGGPLTYTNWKPG-EPNN 83

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 17531345 244 H-----CIAMANNatseynlGQWFGVDCKDYYSFVC 274
Cdd:cd03591  84 AgggedCVEMYTS-------GKWNDVACNLTRLFVC 112
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 184-275 6.43e-04

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: 39.66  E-value: 6.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345 184 GNLVSIHSANENRYV--MTIASHTTQANVLIG-GMWPMDHVNTWVDGTMWDYSNIDSG--YDPTNHCIAMannaTSEYNL 258
Cdd:cd03594  36 AHLASIHSPAEAAAIasLISSYQKAYQPVWIGlHDPQQSRGWEWSDGSKLDYRSWDRNppYARGGYCAEL----SRSTGF 111

                        90
                ....*....|....*..
gi 17531345 259 GQWFGVDCKDYYSFVCK 275
Cdd:cd03594 112 LKWNDANCEERNPFICK 128
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 171-261 1.49e-03

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: 38.17  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345 171 SFTTAQTICEEECGNLVSIHSANENRYVMTIAShtTQANVLIGGmWPMDHVNTWV--DGTMWDYSNIDSGyDPTNHCIAM 248
Cdd:cd03603  11 TWEAAQTLAESLGGHLVTINSAEENDWLLSNFG--GYGASWIGA-SDAATEGTWKwsDGEESTYTNWGSG-EPHNNGGGN 86

                        90
                ....*....|....*.
gi 17531345 249 ANNA---TSEYNLGQW 261
Cdd:cd03603  87 EDYAainHFPGISGKW 102
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 21-144 7.00e-03

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: 36.57  E-value: 7.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531345  21 CTDGFTLVNGKCLMMFKDESNHDDAESFCRLF-----RGTLFDVKNAIDNRAV-----ASFIGSQVETVWMGLF------ 84
Cdd:cd03589   1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFsipglIAHLVSIHSQEENDFVydlfeSSRGPDTPYGLWIGLHdrtseg 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17531345  85 CFnnnlcLWDDnsGSTAAYDNFSGGYPEVTIGS--CVYYATQGTLAGKWISADCTDRRSFVC 144
Cdd:cd03589  81 PF-----EWTD--GSPVDFTKWAGGQPDNYGGNedCVQMWRRGDAGQSWNDMPCDAVFPYIC 135
 
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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