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Conserved domains on  [gi|40555973|ref|NP_955058|]
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C-type lectin-like protein [Canarypox virus]

Protein Classification

PHA03097 family protein( domain architecture ID 11476136)

PHA03097 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 1-134 1.10e-52

C-type lectin-like protein; Provisional


:

Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 163.50  E-value: 1.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40555973    1 MKYIIAFIILAAFIQCTLS------IKCRSDYREFNGKCWQIKKDSRSRRSEAQtRCIQAGGYLArhLDDKDKKYLDVFT 74
Cdd:PHA03097  19 GSIIIALIALVIILSCKLSpgdrsgLNCRSGWVGYNNKCYTFSENITNKHLAIE-RCADMDGILT--LIDDQKEVLFVSR 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40555973   75 HQQGVKLWIGLSYKAAWDDGSEVLEGVVHGPKIDKCIYIKSKEYHSTNCNDEMGYVCMQR 134
Cdd:PHA03097  96 YKGGQDLWIGIEKKKGDDDDREVLDKVVKPPKSGKCAYLKDKTIISSNCNATKGWICFDR 155
 
Name Accession Description Interval E-value
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 1-134 1.10e-52

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 163.50  E-value: 1.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40555973    1 MKYIIAFIILAAFIQCTLS------IKCRSDYREFNGKCWQIKKDSRSRRSEAQtRCIQAGGYLArhLDDKDKKYLDVFT 74
Cdd:PHA03097  19 GSIIIALIALVIILSCKLSpgdrsgLNCRSGWVGYNNKCYTFSENITNKHLAIE-RCADMDGILT--LIDDQKEVLFVSR 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40555973   75 HQQGVKLWIGLSYKAAWDDGSEVLEGVVHGPKIDKCIYIKSKEYHSTNCNDEMGYVCMQR 134
Cdd:PHA03097  96 YKGGQDLWIGIEKKKGDDDDREVLDKVVKPPKSGKCAYLKDKTIISSNCNATKGWICFDR 155
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 22-131 1.37e-09

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: 52.22  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40555973     22 CRSDYREFNGKCWQIKKDSRSRrSEAQTRCIQAGGYLArHLDDKDK-----KYLDVFTHQQGVklWIGLSYKAA-----W 91
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTW-EDAQAFCQSLGGHLA-SIHSEAEndfvaSLLKNSGSSDYY--WIGLSDPDSngswqW 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 40555973     92 DDGSEVL------EGVVHGPKiDKCIYIKSKE--YHSTNCNDEMGYVC 131
Cdd:smart00034  77 SDGSGPVsysnwaPGEPNNSS-GDCVVLSTSGgkWNDVSCTSKLPFVC 123
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 46-133 1.22e-07

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 46.70  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40555973    46 EAQTRCIQAGGYLARHLDDKDKKYLDVFTHQQGVKLWIGLSYKAA-----WDDGSEVL------EGVVHGPKIDkC--IY 112
Cdd:pfam00059   6 EAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNegtwkWVDGSPVNytnwapEPNNNGENED-CveLS 84

                          90       100
                  ....*....|....*....|.
gi 40555973   113 IKSKEYHSTNCNDEMGYVCMQ 133
Cdd:pfam00059  85 SSSGKWNDENCNSKNPFVCEK 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 32-131 1.38e-07

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: 46.84  E-value: 1.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40555973  32 KCWQIKKDSRSRrSEAQTRCIQAGGYLARHLDDKDKKYL-DVFTHQQGVKLWIGLSYKAA-----WDDGSEVL------E 99
Cdd:cd00037   1 SCYKFSTEKLTW-EEAQEYCRSLGGHLASIHSEEENDFLaSLLKKSSSSDVWIGLNDLSSegtwkWSDGSPLVdytnwaP 79

                        90       100       110
                ....*....|....*....|....*....|....*
gi 40555973 100 GVVHGPKIDKCIYIKSK---EYHSTNCNDEMGYVC 131
Cdd:cd00037  80 GEPNPGGSEDCVVLSSSsdgKWNDVSCSSKLPFIC 114
 
Name Accession Description Interval E-value
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 1-134 1.10e-52

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 163.50  E-value: 1.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40555973    1 MKYIIAFIILAAFIQCTLS------IKCRSDYREFNGKCWQIKKDSRSRRSEAQtRCIQAGGYLArhLDDKDKKYLDVFT 74
Cdd:PHA03097  19 GSIIIALIALVIILSCKLSpgdrsgLNCRSGWVGYNNKCYTFSENITNKHLAIE-RCADMDGILT--LIDDQKEVLFVSR 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40555973   75 HQQGVKLWIGLSYKAAWDDGSEVLEGVVHGPKIDKCIYIKSKEYHSTNCNDEMGYVCMQR 134
Cdd:PHA03097  96 YKGGQDLWIGIEKKKGDDDDREVLDKVVKPPKSGKCAYLKDKTIISSNCNATKGWICFDR 155
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 22-131 1.37e-09

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: 52.22  E-value: 1.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40555973     22 CRSDYREFNGKCWQIKKDSRSRrSEAQTRCIQAGGYLArHLDDKDK-----KYLDVFTHQQGVklWIGLSYKAA-----W 91
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTW-EDAQAFCQSLGGHLA-SIHSEAEndfvaSLLKNSGSSDYY--WIGLSDPDSngswqW 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 40555973     92 DDGSEVL------EGVVHGPKiDKCIYIKSKE--YHSTNCNDEMGYVC 131
Cdd:smart00034  77 SDGSGPVsysnwaPGEPNNSS-GDCVVLSTSGgkWNDVSCTSKLPFVC 123
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 46-133 1.22e-07

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 46.70  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40555973    46 EAQTRCIQAGGYLARHLDDKDKKYLDVFTHQQGVKLWIGLSYKAA-----WDDGSEVL------EGVVHGPKIDkC--IY 112
Cdd:pfam00059   6 EAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNegtwkWVDGSPVNytnwapEPNNNGENED-CveLS 84

                          90       100
                  ....*....|....*....|.
gi 40555973   113 IKSKEYHSTNCNDEMGYVCMQ 133
Cdd:pfam00059  85 SSSGKWNDENCNSKNPFVCEK 105
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 32-131 1.38e-07

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: 46.84  E-value: 1.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40555973  32 KCWQIKKDSRSRrSEAQTRCIQAGGYLARHLDDKDKKYL-DVFTHQQGVKLWIGLSYKAA-----WDDGSEVL------E 99
Cdd:cd00037   1 SCYKFSTEKLTW-EEAQEYCRSLGGHLASIHSEEENDFLaSLLKKSSSSDVWIGLNDLSSegtwkWSDGSPLVdytnwaP 79

                        90       100       110
                ....*....|....*....|....*....|....*
gi 40555973 100 GVVHGPKIDKCIYIKSK---EYHSTNCNDEMGYVC 131
Cdd:cd00037  80 GEPNPGGSEDCVVLSSSsdgKWNDVSCSSKLPFIC 114
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 22-133 7.95e-05

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: 39.24  E-value: 7.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40555973  22 CRSDYREFNGKCWQIKKDSRSRrSEAQTRCIQAGGYLARhLDDKD-----KKYLDVFTHqqgvklWIGLSYKA-----AW 91
Cdd:cd03593   1 CPKDWICYGNKCYYFSMEKKTW-NESKEACSSKNSSLLK-IDDEEeleflQSQIGSSSY------WIGLSREKsekpwKW 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 40555973  92 DDGSEV--LEGVVHGPKIDKCIYIKSKEYHSTNCNDEMGYVCMQ 133
Cdd:cd03593  73 IDGSPLnnLFNIRGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
 
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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