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Conserved domains on  [gi|78707260|ref|NP_001027437|]
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narrow, isoform A [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 ...
 42-176 1.97e-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: 53.01  E-value: 1.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707260  42 ELNYFLAYQYCRSLGLQLASFETKEKAESMTTYLKNagYGNYDFWTSGNRLGT-GMFLWMSTGLPFNatfdfFENSADAi 120
Cdd:cd00037   9 KLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKK--SSSSDVWIGLNDLSSeGTWKWSDGSPLVD-----YTNWAPG- 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 78707260 121 qaglldpvdhnsntspqrtarDSSSGAEKGCVILK-QPTLKWMPEDCSAVKDFICEQ 176
Cdd:cd00037  81 ---------------------EPNPGGSEDCVVLSsSSDGKWNDVSCSSKLPFICEK 116
 
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 ...
 42-176 1.97e-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: 53.01  E-value: 1.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707260  42 ELNYFLAYQYCRSLGLQLASFETKEKAESMTTYLKNagYGNYDFWTSGNRLGT-GMFLWMSTGLPFNatfdfFENSADAi 120
Cdd:cd00037   9 KLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKK--SSSSDVWIGLNDLSSeGTWKWSDGSPLVD-----YTNWAPG- 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 78707260 121 qaglldpvdhnsntspqrtarDSSSGAEKGCVILK-QPTLKWMPEDCSAVKDFICEQ 176
Cdd:cd00037  81 ---------------------EPNPGGSEDCVVLSsSSDGKWNDVSCSSKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 38-175 9.61e-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: 51.45  E-value: 9.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707260     38 PYSPELNYFLAYQYCRSLGLQLASFETKEKAESMTTYLKNAGyGNYDFWTSGNRLGT-GMFLWmSTGLPFNaTFDFFens 116
Cdd:smart00034  15 FSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSG-SSDYYWIGLSDPDSnGSWQW-SDGSGPV-SYSNW--- 88

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 78707260    117 adaiqaglldpvdhnsntspqrtARDSSSGAEKGCVILKQPTLKWMPEDCSAVKDFICE 175
Cdd:smart00034  89 -----------------------APGEPNNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 43-176 1.87e-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: 42.08  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707260    43 LNYFLAYQYCRSLGLQLASFETKEKAESMTTYLKNAgygNYDFWTSGNRLGTGM-FLWmSTGLPFNATFdffensadaiq 121
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKS---NKYFWIGLTDRKNEGtWKW-VDGSPVNYTN----------- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 78707260   122 aglLDPVDHNSNTSPQrtardsssgaekgCVILKQPTLKWMPEDCSAVKDFICEQ 176
Cdd:pfam00059  67 ---WAPEPNNNGENED-------------CVELSSSSGKWNDENCNSKNPFVCEK 105
 
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 ...
 42-176 1.97e-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: 53.01  E-value: 1.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707260  42 ELNYFLAYQYCRSLGLQLASFETKEKAESMTTYLKNagYGNYDFWTSGNRLGT-GMFLWMSTGLPFNatfdfFENSADAi 120
Cdd:cd00037   9 KLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKK--SSSSDVWIGLNDLSSeGTWKWSDGSPLVD-----YTNWAPG- 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 78707260 121 qaglldpvdhnsntspqrtarDSSSGAEKGCVILK-QPTLKWMPEDCSAVKDFICEQ 176
Cdd:cd00037  81 ---------------------EPNPGGSEDCVVLSsSSDGKWNDVSCSSKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 38-175 9.61e-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: 51.45  E-value: 9.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707260     38 PYSPELNYFLAYQYCRSLGLQLASFETKEKAESMTTYLKNAGyGNYDFWTSGNRLGT-GMFLWmSTGLPFNaTFDFFens 116
Cdd:smart00034  15 FSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSG-SSDYYWIGLSDPDSnGSWQW-SDGSGPV-SYSNW--- 88

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 78707260    117 adaiqaglldpvdhnsntspqrtARDSSSGAEKGCVILKQPTLKWMPEDCSAVKDFICE 175
Cdd:smart00034  89 -----------------------APGEPNNSSGDCVVLSTSGGKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 43-176 1.87e-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: 42.08  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707260    43 LNYFLAYQYCRSLGLQLASFETKEKAESMTTYLKNAgygNYDFWTSGNRLGTGM-FLWmSTGLPFNATFdffensadaiq 121
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKS---NKYFWIGLTDRKNEGtWKW-VDGSPVNYTN----------- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 78707260   122 aglLDPVDHNSNTSPQrtardsssgaekgCVILKQPTLKWMPEDCSAVKDFICEQ 176
Cdd:pfam00059  67 ---WAPEPNNNGENED-------------CVELSSSSGKWNDENCNSKNPFVCEK 105
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 42-175 4.06e-03

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.


Pssm-ID: 153071  Cd Length: 119  Bit Score: 35.59  E-value: 4.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78707260  42 ELNYFLAYQYCRSLGLQLASFETKEkAESMTTYLKNAGYGNYDFWTSGNRL--GTGMFLWmstglpfnatfdffensADa 119
Cdd:cd03601   9 TMNYAKAGAFCRSRGMRLASLAMRD-SEMRDAILAFTLVKGHGYWVGADNLqdGEYDFLW-----------------ND- 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 78707260 120 iqaGLLDPVDHNsNTSPQRTARDSSSgaeKGCVILKQPTLKWMPEDCSAVKDFICE 175
Cdd:cd03601  70 ---GVSLPTDSD-LWAPNEPSNPQSR---QLCVQLWSKYNLLDDEYCGRAKRVICE 118
 
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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