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Conserved domains on  [gi|2057079772|ref|NP_001382260|]
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putative C-type lectin domain family 20 member A precursor [Homo sapiens]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10132587)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein similar to Homo sapiens putative C-type lectin domain family 20 member A

Gene Ontology:  GO:0030246
PubMed:  16336259

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 22-132 1.21e-37

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: 131.73  E-value: 1.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772  22 RDLVLVKEALSWYDAQQHCRLHYTDLADLQPSGLWKLYSLMT---STPAWIGLFFDasTSGLRWSSGSTFTALEWGQkLP 98
Cdd:cd03602     1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSrvsNSAAWIGLYRD--VDSWRWSDGSESSFRNWNT-FQ 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2057079772  99 EFGVGFCATLYTWlklPSIGAASCTAQKPFLCYC 132
Cdd:cd03602    78 PFGQGDCATMYSS---GRWYAALCSALKPFICYD 108
CLECT super family cl02432
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 162-275 1.02e-26

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.


The actual alignment was detected with superfamily member cd03602:

Pssm-ID: 470576  Cd Length: 108  Bit Score: 102.84  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772 162 QTFMRFDQVMTWSSALLYCRSHHTDLADLQMVTDetgKEALR--SIMSETEAWIGLYlnANSGSLSWSSDLGASIPSWLQ 239
Cdd:cd03602     1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQED---NALLSnlSRVSNSAAWIGLY--RDVDSWRWSDGSESSFRNWNT 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2057079772 240 VPMMVRGLCtalgIYMTYSPKVYSVNCSSLLPFFCF 275
Cdd:cd03602    76 FQPFGQGDC----ATMYSSGRWYAALCSALKPFICY 107
 
Name Accession Description Interval E-value
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 22-132 1.21e-37

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: 131.73  E-value: 1.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772  22 RDLVLVKEALSWYDAQQHCRLHYTDLADLQPSGLWKLYSLMT---STPAWIGLFFDasTSGLRWSSGSTFTALEWGQkLP 98
Cdd:cd03602     1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSrvsNSAAWIGLYRD--VDSWRWSDGSESSFRNWNT-FQ 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2057079772  99 EFGVGFCATLYTWlklPSIGAASCTAQKPFLCYC 132
Cdd:cd03602    78 PFGQGDCATMYSS---GRWYAALCSALKPFICYD 108
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 162-275 1.02e-26

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: 102.84  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772 162 QTFMRFDQVMTWSSALLYCRSHHTDLADLQMVTDetgKEALR--SIMSETEAWIGLYlnANSGSLSWSSDLGASIPSWLQ 239
Cdd:cd03602     1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQED---NALLSnlSRVSNSAAWIGLY--RDVDSWRWSDGSESSFRNWNT 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2057079772 240 VPMMVRGLCtalgIYMTYSPKVYSVNCSSLLPFFCF 275
Cdd:cd03602    76 FQPFGQGDC----ATMYSSGRWYAALCSALKPFICY 107
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 26-130 1.34e-10

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: 58.38  E-value: 1.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772   26 LVKEALSWYDAQQHCRLHYTDLADLQPSG----LWKLYSLMT-STPAWIGLFFDASTSGLRWSSGSTFTALE-WGQKLPE 99
Cdd:smart00034  15 FSTEKKTWEDAQAFCQSLGGHLASIHSEAendfVASLLKNSGsSDYYWIGLSDPDSNGSWQWSDGSGPVSYSnWAPGEPN 94

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2057079772  100 FGVGFCATLYT----WLklpsigAASCTAQKPFLC 130
Cdd:smart00034  95 NSSGDCVVLSTsggkWN------DVSCTSKLPFVC 123
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 30-131 7.42e-10

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 55.95  E-value: 7.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772  30 ALSWYDAQQHCRLHYTDLADLQPSGLWKLYSLMT---STPAWIGLFFDASTSGLRWSSGSTFTALEWGQKLPEFGV-GFC 105
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLkksNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGEnEDC 80

                          90       100
                  ....*....|....*....|....*.
gi 2057079772 106 ATLYtwLKLPSIGAASCTAQKPFLCY 131
Cdd:pfam00059  81 VELS--SSSGKWNDENCNSKNPFVCE 104
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 167-274 2.14e-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: 54.91  E-value: 2.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772  167 FDQVMTWSSALLYCRSHHTDLAdlqMVTDETGKEALRSIMSE----TEAWIGLYLNANSGSLSWSSDLGASIPSWLQ--V 240
Cdd:smart00034  16 STEKKTWEDAQAFCQSLGGHLA---SIHSEAENDFVASLLKNsgssDYYWIGLSDPDSNGSWQWSDGSGPVSYSNWApgE 92

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2057079772  241 PMMVRGLCTALgiyMTYSPKVYSVNCSSLLPFFC 274
Cdd:smart00034  93 PNNSSGDCVVL---STSGGKWNDVSCTSKLPFVC 123
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 171-274 9.70e-09

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 52.48  E-value: 9.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772 171 MTWSSALLYCRSHHTDLADLQmvTDETGKeALRSIM--SETEAWIGLYLNANSGSLSWSSDLGASIPSWLQVPMMV--RG 246
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSIN--SAEELD-FLSSTLkkSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNgeNE 78

                          90       100
                  ....*....|....*....|....*....
gi 2057079772 247 LCtalgIYMTYSP-KVYSVNCSSLLPFFC 274
Cdd:pfam00059  79 DC----VELSSSSgKWNDENCNSKNPFVC 103
 
Name Accession Description Interval E-value
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 22-132 1.21e-37

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: 131.73  E-value: 1.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772  22 RDLVLVKEALSWYDAQQHCRLHYTDLADLQPSGLWKLYSLMT---STPAWIGLFFDasTSGLRWSSGSTFTALEWGQkLP 98
Cdd:cd03602     1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSrvsNSAAWIGLYRD--VDSWRWSDGSESSFRNWNT-FQ 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2057079772  99 EFGVGFCATLYTWlklPSIGAASCTAQKPFLCYC 132
Cdd:cd03602    78 PFGQGDCATMYSS---GRWYAALCSALKPFICYD 108
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 162-275 1.02e-26

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: 102.84  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772 162 QTFMRFDQVMTWSSALLYCRSHHTDLADLQMVTDetgKEALR--SIMSETEAWIGLYlnANSGSLSWSSDLGASIPSWLQ 239
Cdd:cd03602     1 RTFYLVNESKTWSEAQQYCRENYTDLATVQNQED---NALLSnlSRVSNSAAWIGLY--RDVDSWRWSDGSESSFRNWNT 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2057079772 240 VPMMVRGLCtalgIYMTYSPKVYSVNCSSLLPFFCF 275
Cdd:cd03602    76 FQPFGQGDC----ATMYSSGRWYAALCSALKPFICY 107
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 26-131 4.46e-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: 65.33  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772  26 LVKEALSWYDAQQHCRLHYTDLADLQPSG----LWKLYSLMTSTPAWIGLFFDASTSGLRWSSGST-FTALEWGQKLPEF 100
Cdd:cd00037     5 FSTEKLTWEEAQEYCRSLGGHLASIHSEEendfLASLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPGEPNP 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2057079772 101 -GVGFCATLYTWlKLPSIGAASCTAQKPFLCY 131
Cdd:cd00037    85 gGSEDCVVLSSS-SDGKWNDVSCSSKLPFICE 115
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 26-130 1.34e-10

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: 58.38  E-value: 1.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772   26 LVKEALSWYDAQQHCRLHYTDLADLQPSG----LWKLYSLMT-STPAWIGLFFDASTSGLRWSSGSTFTALE-WGQKLPE 99
Cdd:smart00034  15 FSTEKKTWEDAQAFCQSLGGHLASIHSEAendfVASLLKNSGsSDYYWIGLSDPDSNGSWQWSDGSGPVSYSnWAPGEPN 94

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2057079772  100 FGVGFCATLYT----WLklpsigAASCTAQKPFLC 130
Cdd:smart00034  95 NSSGDCVVLSTsggkWN------DVSCTSKLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 164-274 1.90e-10

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: 58.01  E-value: 1.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772 164 FMRFDQVMTWSSALLYCRSHHTDLAdlqMVTDETGKEALRSIMSE---TEAWIGLYLNANSGSLSWSSDLGASIPS-WL- 238
Cdd:cd00037     3 YKFSTEKLTWEEAQEYCRSLGGHLA---SIHSEEENDFLASLLKKsssSDVWIGLNDLSSEGTWKWSDGSPLVDYTnWAp 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2057079772 239 -QVPMMVRGLCTALgiYMTYSPKVYSVNCSSLLPFFC 274
Cdd:cd00037    80 gEPNPGGSEDCVVL--SSSSDGKWNDVSCSSKLPFIC 114
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 30-131 7.42e-10

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 55.95  E-value: 7.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772  30 ALSWYDAQQHCRLHYTDLADLQPSGLWKLYSLMT---STPAWIGLFFDASTSGLRWSSGSTFTALEWGQKLPEFGV-GFC 105
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLkksNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNGEnEDC 80

                          90       100
                  ....*....|....*....|....*.
gi 2057079772 106 ATLYtwLKLPSIGAASCTAQKPFLCY 131
Cdd:pfam00059  81 VELS--SSSGKWNDENCNSKNPFVCE 104
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 167-274 2.14e-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: 54.91  E-value: 2.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772  167 FDQVMTWSSALLYCRSHHTDLAdlqMVTDETGKEALRSIMSE----TEAWIGLYLNANSGSLSWSSDLGASIPSWLQ--V 240
Cdd:smart00034  16 STEKKTWEDAQAFCQSLGGHLA---SIHSEAENDFVASLLKNsgssDYYWIGLSDPDSNGSWQWSDGSGPVSYSNWApgE 92

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2057079772  241 PMMVRGLCTALgiyMTYSPKVYSVNCSSLLPFFC 274
Cdd:smart00034  93 PNNSSGDCVVL---STSGGKWNDVSCTSKLPFVC 123
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 171-274 9.70e-09

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 52.48  E-value: 9.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772 171 MTWSSALLYCRSHHTDLADLQmvTDETGKeALRSIM--SETEAWIGLYLNANSGSLSWSSDLGASIPSWLQVPMMV--RG 246
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSIN--SAEELD-FLSSTLkkSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNgeNE 78

                          90       100
                  ....*....|....*....|....*....
gi 2057079772 247 LCtalgIYMTYSP-KVYSVNCSSLLPFFC 274
Cdd:pfam00059  79 DC----VELSSSSgKWNDENCNSKNPFVC 103
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 31-132 5.81e-07

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 48.14  E-value: 5.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772  31 LSWYDAQQHCRLHY--TDLADLQPSG----LWKL--YSLMTSTPAWIGLFFDASTSGLRWSSGSTFTALEWGQKLPEFGV 102
Cdd:cd03594    20 LSWSDAELFCQKYGpgAHLASIHSPAeaaaIASLisSYQKAYQPVWIGLHDPQQSRGWEWSDGSKLDYRSWDRNPPYARG 99

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2057079772 103 GFCATLY------TWlklpsiGAASCTAQKPFLCYC 132
Cdd:cd03594   100 GYCAELSrstgflKW------NDANCEERNPFICKY 129
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 172-274 3.94e-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: 39.62  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772 172 TWSSALLYCRSHHTDLADLQmvtDETGKEALRSIMSETEAWIGLYLNANSGSLSWssDLGASIPSWLQVPMMVR-GLCTA 250
Cdd:cd03593    21 TWNESKEACSSKNSSLLKID---DEEELEFLQSQIGSSSYWIGLSREKSEKPWKW--IDGSPLNNLFNIRGSTKsGNCAY 95

                          90       100
                  ....*....|....*....|....
gi 2057079772 251 LgiymtYSPKVYSVNCSSLLPFFC 274
Cdd:cd03593    96 L-----SSTGIYSEDCSTKKRWIC 114
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 167-276 1.67e-03

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 38.12  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772 167 FDQVMTWSSALLYCRSHH--TDLADLqmvtdETGKEAL---RSIMS----ETEAWIGLYLNANSGSLSWSSDLGASIPSW 237
Cdd:cd03594    16 FRQPLSWSDAELFCQKYGpgAHLASI-----HSPAEAAaiaSLISSyqkaYQPVWIGLHDPQQSRGWEWSDGSKLDYRSW 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2057079772 238 LQ-VPMMVRGLCTALGI---YMTYSpkvySVNCSSLLPFFCFY 276
Cdd:cd03594    91 DRnPPYARGGYCAELSRstgFLKWN----DANCEERNPFICKY 129
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 28-130 2.02e-03

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: 37.70  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2057079772  28 KEALSWYDAQQHCRLHYTDLADLQ-PSGLWKLYSLMTSTPAWIGLFFDASTSGLRWSSGSTFTAleWGQKLPEFGVGFCA 106
Cdd:cd03593    17 MEKKTWNESKEACSSKNSSLLKIDdEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSPLNN--LFNIRGSTKSGNCA 94

                          90       100
                  ....*....|....*....|....
gi 2057079772 107 tlytWLKLPSIGAASCTAQKPFLC 130
Cdd:cd03593    95 ----YLSSTGIYSEDCSTKKRWIC 114
 
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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