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Conserved domains on  [gi|72000946|ref|NP_507255|]
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C-type lectin domain-containing protein [Caenorhabditis elegans]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10636995)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein may bind carbohydrate in a calcium-dependent manner

CATH:  3.10.100.10
Gene Ontology:  GO:0030246|GO:0120153
PubMed:  16336259|10508765
SCOP:  4002453

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 97-225 8.08e-18

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


:

Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 78.41  E-value: 8.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946     97 CHIGFELIGGKCLQLLTGVGTRANGNHNCWLHGGSkLFSIRNEQENSAILDFASKN-NIGNIWTGLLCHGhTISTCIWDI 175
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGH-LASIHSEAENDFVASLLKNSgSSDYYWIGLSDPD-SNGSWQWSD 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 72000946    176 VSGSaESYDNFASGYPNVSTASCGYFITTGkeaGQWKTGLCNQQNSILCE 225
Cdd:smart00034  79 GSGP-VSYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 239-348 2.86e-14

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: 68.78  E-value: 2.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946    239 FNNHCYTRFDDAYTVAEAHEFCKPMCAEVVSINSGDESRYVQSIY----NVKEHIILGVAVLNDNNIYWLDGSSTV-FIN 313
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsgSSDYYWIGLSDPDSNGSWQWSDGSGPVsYSN 87

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 72000946    314 IG----NNDNGTCAIMDVSfgMGYWTTIECSQKAWILCK 348
Cdd:smart00034  88 WApgepNNSSGDCVVLSTS--GGKWNDVSCTSKLPFVCE 124
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 97-225 8.08e-18

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 78.41  E-value: 8.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946     97 CHIGFELIGGKCLQLLTGVGTRANGNHNCWLHGGSkLFSIRNEQENSAILDFASKN-NIGNIWTGLLCHGhTISTCIWDI 175
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGH-LASIHSEAENDFVASLLKNSgSSDYYWIGLSDPD-SNGSWQWSD 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 72000946    176 VSGSaESYDNFASGYPNVSTASCGYFITTGkeaGQWKTGLCNQQNSILCE 225
Cdd:smart00034  79 GSGP-VSYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 239-348 2.86e-14

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: 68.78  E-value: 2.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946    239 FNNHCYTRFDDAYTVAEAHEFCKPMCAEVVSINSGDESRYVQSIY----NVKEHIILGVAVLNDNNIYWLDGSSTV-FIN 313
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsgSSDYYWIGLSDPDSNGSWQWSDGSGPVsYSN 87

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 72000946    314 IG----NNDNGTCAIMDVSfgMGYWTTIECSQKAWILCK 348
Cdd:smart00034  88 WApgepNNSSGDCVVLSTS--GGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 107-225 1.78e-11

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 60.71  E-value: 1.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946 107 KCLQLLTGVGTRANGNHNCWLHGGSkLFSIRNEQENSAILDFASKNNIGNIWTGLLCHGHTiSTCIWdiVSGSAE-SYDN 185
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGH-LASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSE-GTWKW--SDGSPLvDYTN 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 72000946 186 FASGYPNVSTAS-CGYFITTGkeAGQWKTGLCNQQNSILCE 225
Cdd:cd00037  77 WAPGEPNPGGSEdCVVLSSSS--DGKWNDVSCSSKLPFICE 115
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 242-349 1.10e-09

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: 55.32  E-value: 1.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946 242 HCYTRFDDAYTVAEAHEFCKPMCAEVVSINSGDESRYVQSIYNVKEHII--LGVAVLNDNNIY-WLDGSSTV-FIN---- 313
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDvwIGLNDLSSEGTWkWSDGSPLVdYTNwapg 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 72000946 314 -IGNNDNGTCAIMDVSfGMGYWTTIECSQKAWILCKR 349
Cdd:cd00037  81 ePNPGGSEDCVVLSSS-SDGKWNDVSCSSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 250-349 1.77e-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: 45.93  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946   250 AYTVAEAHEFCKPMCAEVVSINSGDESRYVQSI---YNVKEHIILGvAVLNDNNIYWLDGSSTVFIN-----IGNNDNGT 321
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTlkkSNKYFWIGLT-DRKNEGTWKWVDGSPVNYTNwapepNNNGENED 79

                          90       100
                  ....*....|....*....|....*...
gi 72000946   322 CAIMdvSFGMGYWTTIECSQKAWILCKR 349
Cdd:pfam00059  80 CVEL--SSSSGKWNDENCNSKNPFVCEK 105
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 130-225 4.84e-03

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 36.30  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946   130 GSKLFSIRNEQENSAILDFAsKNNIGNIWTGLLCHGHTiSTCIWdiVSGSAESYDNFASGYPNVST-ASCGYFittGKEA 208
Cdd:pfam00059  15 GGHLVSINSAEELDFLSSTL-KKSNKYFWIGLTDRKNE-GTWKW--VDGSPVNYTNWAPEPNNNGEnEDCVEL---SSSS 87

                          90
                  ....*....|....*..
gi 72000946   209 GQWKTGLCNQQNSILCE 225
Cdd:pfam00059  88 GKWNDENCNSKNPFVCE 104
 
Name Accession Description Interval E-value
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 97-225 8.08e-18

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


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 78.41  E-value: 8.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946     97 CHIGFELIGGKCLQLLTGVGTRANGNHNCWLHGGSkLFSIRNEQENSAILDFASKN-NIGNIWTGLLCHGhTISTCIWDI 175
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGH-LASIHSEAENDFVASLLKNSgSSDYYWIGLSDPD-SNGSWQWSD 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 72000946    176 VSGSaESYDNFASGYPNVSTASCGYFITTGkeaGQWKTGLCNQQNSILCE 225
Cdd:smart00034  79 GSGP-VSYSNWAPGEPNNSSGDCVVLSTSG---GKWNDVSCTSKLPFVCE 124
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 239-348 2.86e-14

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: 68.78  E-value: 2.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946    239 FNNHCYTRFDDAYTVAEAHEFCKPMCAEVVSINSGDESRYVQSIY----NVKEHIILGVAVLNDNNIYWLDGSSTV-FIN 313
Cdd:smart00034   8 YGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsgSSDYYWIGLSDPDSNGSWQWSDGSGPVsYSN 87

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 72000946    314 IG----NNDNGTCAIMDVSfgMGYWTTIECSQKAWILCK 348
Cdd:smart00034  88 WApgepNNSSGDCVVLSTS--GGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 107-225 1.78e-11

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 60.71  E-value: 1.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946 107 KCLQLLTGVGTRANGNHNCWLHGGSkLFSIRNEQENSAILDFASKNNIGNIWTGLLCHGHTiSTCIWdiVSGSAE-SYDN 185
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGH-LASIHSEEENDFLASLLKKSSSSDVWIGLNDLSSE-GTWKW--SDGSPLvDYTN 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 72000946 186 FASGYPNVSTAS-CGYFITTGkeAGQWKTGLCNQQNSILCE 225
Cdd:cd00037  77 WAPGEPNPGGSEdCVVLSSSS--DGKWNDVSCSSKLPFICE 115
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 242-349 1.10e-09

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: 55.32  E-value: 1.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946 242 HCYTRFDDAYTVAEAHEFCKPMCAEVVSINSGDESRYVQSIYNVKEHII--LGVAVLNDNNIY-WLDGSSTV-FIN---- 313
Cdd:cd00037   1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDvwIGLNDLSSEGTWkWSDGSPLVdYTNwapg 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 72000946 314 -IGNNDNGTCAIMDVSfGMGYWTTIECSQKAWILCKR 349
Cdd:cd00037  81 ePNPGGSEDCVVLSSS-SDGKWNDVSCSSKLPFICEK 116
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 239-348 4.90e-08

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


Pssm-ID: 153059  Cd Length: 137  Bit Score: 51.20  E-value: 4.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946 239 FNNHCYTRFDDAYTVAEAHEFCK----PMC-AEVVSINSGDESRYVQSIYN--VKEHIILGVAV-LND----NNIYWLDG 306
Cdd:cd03589   8 FGGYCYRFFGDRLTWEEAELRCRsfsiPGLiAHLVSIHSQEENDFVYDLFEssRGPDTPYGLWIgLHDrtseGPFEWTDG 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 72000946 307 SSTVFIN--IGNNDNGT----CAIMDVSFGMGY-WTTIECSQKAWILCK 348
Cdd:cd03589  88 SPVDFTKwaGGQPDNYGgnedCVQMWRRGDAGQsWNDMPCDAVFPYICK 136
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 250-349 1.77e-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: 45.93  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946   250 AYTVAEAHEFCKPMCAEVVSINSGDESRYVQSI---YNVKEHIILGvAVLNDNNIYWLDGSSTVFIN-----IGNNDNGT 321
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTlkkSNKYFWIGLT-DRKNEGTWKWVDGSPVNYTNwapepNNNGENED 79

                          90       100
                  ....*....|....*....|....*...
gi 72000946   322 CAIMdvSFGMGYWTTIECSQKAWILCKR 349
Cdd:pfam00059  80 CVEL--SSSSGKWNDENCNSKNPFVCEK 105
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 239-349 8.32e-05

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 41.79  E-value: 8.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946 239 FNNHCYTRFDDAYTVAEAHEFCKPMCAEVVSINSGDESRYVQSIYNVKEHIILGVAVLnDNNIYWLDGSSTVFINIGNN- 317
Cdd:cd03588   8 FQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTI-EGDFRWSDGHPLQFENWRPNq 86

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 72000946 318 -DN-----GTCAIMdVSFGMGYWTTIECSQKAWILCKR 349
Cdd:cd03588  87 pDNffatgEDCVVM-IWHEEGEWNDVPCNYHLPFTCKK 123
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 237-349 6.08e-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: 39.21  E-value: 6.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946 237 KNFNNHCYTRFDDAYTVAEAHEFCKPMCAEVVSINSGDESRYVQSIYNVKEHIILGVAVLNDNNIY-WLDGS----STVF 311
Cdd:cd03590   6 KSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWkWVDGTplnsSKTF 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 72000946 312 INIG--NNDNGT---CAIMDVSfgMGYWTTIECSQKAWILCKR 349
Cdd:cd03590  86 WHPGepNNWGGGgedCAELVYD--SGGWNDVPCNLEYRWICEK 126
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 235-349 9.00e-04

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 38.47  E-value: 9.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946 235 CEKN---FNNHCYTRFDDAYTVAEAHEFCKPMCAEVVSINSGDESRYVQSIYNVKEHIIlGVAVLNDNNIY-WLDGS--S 308
Cdd:cd03593   1 CPKDwicYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWI-GLSREKSEKPWkWIDGSplN 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 72000946 309 TVFINIGNNDNGTCAimdvSFGMGYWTTIECSQKAWILCKR 349
Cdd:cd03593  80 NLFNIRGSTKSGNCA----YLSSTGIYSEDCSTKKRWICEK 116
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 130-225 1.55e-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: 37.74  E-value: 1.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946 130 GSKLFSIRNEQENSAILDFASKNNIGNIWTGllchGHTIS-TCIWDIVSGSAESYDNFASGYPNVS-TASC--GYFITTG 205
Cdd:cd03592  23 GTDLVAIQNAEENALLNGFALKYNLGYYWID----GNDINnEGTWVDTDKKELEYKNWAPGEPNNGrNENCleIYIKDNG 98

                        90       100
                ....*....|....*....|
gi 72000946 206 KeagqWKTGLCNQQNSILCE 225
Cdd:cd03592  99 K----WNDEPCSKKKSAICY 114
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 130-225 4.84e-03

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 36.30  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72000946   130 GSKLFSIRNEQENSAILDFAsKNNIGNIWTGLLCHGHTiSTCIWdiVSGSAESYDNFASGYPNVST-ASCGYFittGKEA 208
Cdd:pfam00059  15 GGHLVSINSAEELDFLSSTL-KKSNKYFWIGLTDRKNE-GTWKW--VDGSPVNYTNWAPEPNNNGEnEDCVEL---SSSS 87

                          90
                  ....*....|....*..
gi 72000946   209 GQWKTGLCNQQNSILCE 225
Cdd:pfam00059  88 GKWNDENCNSKNPFVCE 104
 
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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