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Conserved domains on  [gi|21357479|ref|NP_652640|]
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lectin-29Ca [Drosophila melanogaster]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10034483)

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 cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 131-231 3.73e-13

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


:

Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 63.79  E-value: 3.73e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357479 131 KMPWDSAYDTCRQMGGHLANILDEKE---LNEIFSEETKKKYWVDINSRANDGaSWISTLSGRDVPFLKWKPN-LATNIH 206
Cdd:cd00037   9 KLTWEEAQEYCRSLGGHLASIHSEEEndfLASLLKKSSSSDVWIGLNDLSSEG-TWKWSDGSPLVDYTNWAPGePNPGGS 87

                        90       100
                ....*....|....*....|....*...
gi 21357479 207 NHCVYINSNEMYF---ENCANDNYFACQ 231
Cdd:cd00037  88 EDCVVLSSSSDGKwndVSCSSKLPFICE 115
 
Name Accession Description Interval E-value
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 131-231 3.73e-13

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 63.79  E-value: 3.73e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357479 131 KMPWDSAYDTCRQMGGHLANILDEKE---LNEIFSEETKKKYWVDINSRANDGaSWISTLSGRDVPFLKWKPN-LATNIH 206
Cdd:cd00037   9 KLTWEEAQEYCRSLGGHLASIHSEEEndfLASLLKKSSSSDVWIGLNDLSSEG-TWKWSDGSPLVDYTNWAPGePNPGGS 87

                        90       100
                ....*....|....*....|....*...
gi 21357479 207 NHCVYINSNEMYF---ENCANDNYFACQ 231
Cdd:cd00037  88 EDCVVLSSSSDGKwndVSCSSKLPFICE 115
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 123-231 1.72e-11

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: 59.54  E-value: 1.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357479    123 HFYLEKQKKMPWDSAYDTCRQMGGHLANILDEKE---LNEIFSEETK-KKYWVDINSRANDGASWISTLSGrDVPFLKWK 198
Cdd:smart00034  11 KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAEndfVASLLKNSGSsDYYWIGLSDPDSNGSWQWSDGSG-PVSYSNWA 89

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 21357479    199 PNLATNIHNHCVYINSNE--MYFENCANDNYFACQ 231
Cdd:smart00034  90 PGEPNNSSGDCVVLSTSGgkWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 131-231 6.69e-08

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 49.40  E-value: 6.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357479   131 KMPWDSAYDTCRQMGGHLANILDEKELNEIFSEETK--KKYWVDINSRANDGA-SWIstlSGRDVPFLKWKPNLATNI-H 206
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKsnKYFWIGLTDRKNEGTwKWV---DGSPVNYTNWAPEPNNNGeN 77

                          90       100
                  ....*....|....*....|....*..
gi 21357479   207 NHCVYIN--SNEMYFENCANDNYFACQ 231
Cdd:pfam00059  78 EDCVELSssSGKWNDENCNSKNPFVCE 104
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 104-230 6.67e-07

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 47.55  E-value: 6.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357479  104 NVKMSNKIKMSVFKKIGSRHFYLEKQKKMPW--------DSAYDTCRQMGGHLANILDEKELNEIFSEETKKKYWVDINS 175
Cdd:PHA03097  29 VIILSCKLSPGDRSGLNCRSGWVGYNNKCYTfsenitnkHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGIEK 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 21357479  176 RANDGASwiSTLSGRDVPFLKwkpnlatniHNHCVYINSNEMYFENCANDNYFAC 230
Cdd:PHA03097 109 KKGDDDD--REVLDKVVKPPK---------SGKCAYLKDKTIISSNCNATKGWIC 152
 
Name Accession Description Interval E-value
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 131-231 3.73e-13

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 63.79  E-value: 3.73e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357479 131 KMPWDSAYDTCRQMGGHLANILDEKE---LNEIFSEETKKKYWVDINSRANDGaSWISTLSGRDVPFLKWKPN-LATNIH 206
Cdd:cd00037   9 KLTWEEAQEYCRSLGGHLASIHSEEEndfLASLLKKSSSSDVWIGLNDLSSEG-TWKWSDGSPLVDYTNWAPGePNPGGS 87

                        90       100
                ....*....|....*....|....*...
gi 21357479 207 NHCVYINSNEMYF---ENCANDNYFACQ 231
Cdd:cd00037  88 EDCVVLSSSSDGKwndVSCSSKLPFICE 115
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 123-231 1.72e-11

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: 59.54  E-value: 1.72e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357479    123 HFYLEKQKKMPWDSAYDTCRQMGGHLANILDEKE---LNEIFSEETK-KKYWVDINSRANDGASWISTLSGrDVPFLKWK 198
Cdd:smart00034  11 KCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAEndfVASLLKNSGSsDYYWIGLSDPDSNGSWQWSDGSG-PVSYSNWA 89

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 21357479    199 PNLATNIHNHCVYINSNE--MYFENCANDNYFACQ 231
Cdd:smart00034  90 PGEPNNSSGDCVVLSTSGgkWNDVSCTSKLPFVCE 124
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 124-231 6.50e-08

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


Pssm-ID: 153063  Cd Length: 116  Bit Score: 49.64  E-value: 6.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357479 124 FYLEKQKKmPWDSAYDTCRQMGGHLANILDEKELNEIFSEETKKKYWVDInSRANDGASWISTLSGrdvPFLKWKPNLAT 203
Cdd:cd03593  13 YYFSMEKK-TWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGL-SREKSEKPWKWIDGS---PLNNLFNIRGS 87

                        90       100
                ....*....|....*....|....*...
gi 21357479 204 NIHNHCVYINSNEMYFENCANDNYFACQ 231
Cdd:cd03593  88 TKSGNCAYLSSTGIYSEDCSTKKRWICE 115
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 131-231 6.69e-08

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 49.40  E-value: 6.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357479   131 KMPWDSAYDTCRQMGGHLANILDEKELNEIFSEETK--KKYWVDINSRANDGA-SWIstlSGRDVPFLKWKPNLATNI-H 206
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKsnKYFWIGLTDRKNEGTwKWV---DGSPVNYTNWAPEPNNNGeN 77

                          90       100
                  ....*....|....*....|....*..
gi 21357479   207 NHCVYIN--SNEMYFENCANDNYFACQ 231
Cdd:pfam00059  78 EDCVELSssSGKWNDENCNSKNPFVCE 104
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 104-230 6.67e-07

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 47.55  E-value: 6.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357479  104 NVKMSNKIKMSVFKKIGSRHFYLEKQKKMPW--------DSAYDTCRQMGGHLANILDEKELNEIFSEETKKKYWVDINS 175
Cdd:PHA03097  29 VIILSCKLSPGDRSGLNCRSGWVGYNNKCYTfsenitnkHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGIEK 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 21357479  176 RANDGASwiSTLSGRDVPFLKwkpnlatniHNHCVYINSNEMYFENCANDNYFAC 230
Cdd:PHA03097 109 KKGDDDD--REVLDKVVKPPK---------SGKCAYLKDKTIISSNCNATKGWIC 152
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 130-231 1.42e-05

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: 43.13  E-value: 1.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357479 130 KKMPWDSAYDTCRQMGGHLANILDEKELNEIFSEETKKK---YWVDINSRANDGaSWISTlSGRDVPFLKWKPNLATNIH 206
Cdd:cd03592   8 EKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNlgyYWIDGNDINNEG-TWVDT-DKKELEYKNWAPGEPNNGR 85

                        90       100
                ....*....|....*....|....*....
gi 21357479 207 N-HCV--YINSNEMYF-ENCANDNYFACQ 231
Cdd:cd03592  86 NeNCLeiYIKDNGKWNdEPCSKKKSAICY 114
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 122-230 6.83e-04

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


Pssm-ID: 153072  Cd Length: 108  Bit Score: 38.12  E-value: 6.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357479 122 RHFYLEKQKKMpWDSAYDTCRQMGGHLANILDEKELNEI--FSEETKKKYWVDInSRANDGASWIstlSGRDVPFLKWKP 199
Cdd:cd03602   1 RTFYLVNESKT-WSEAQQYCRENYTDLATVQNQEDNALLsnLSRVSNSAAWIGL-YRDVDSWRWS---DGSESSFRNWNT 75

                        90       100       110
                ....*....|....*....|....*....|..
gi 21357479 200 NLATNiHNHCVYINSN-EMYFENCANDNYFAC 230
Cdd:cd03602  76 FQPFG-QGDCATMYSSgRWYAALCSALKPFIC 106
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 123-186 8.30e-04

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


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 38.17  E-value: 8.30e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21357479 123 HFYLEKQKKMPWDSAYDTCRQMGGHLANILDEKE---LNEIFSE----------ETKKKYWVDINSRANDGASWIST 186
Cdd:cd03603   1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEEndwLLSNFGGygaswigasdAATEGTWKWSDGEESTYTNWGSG 77
 
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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