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Conserved domains on  [gi|836937729|ref|NP_001296870|]
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killer cell lectin-like receptor 2 [Microcebus murinus]

Protein Classification

Ly49 and CLECT_NK_receptors_like domain-containing protein( domain architecture ID 10280461)

Ly49 and CLECT_NK_receptors_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 150-264 5.41e-41

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: 137.46  E-value: 5.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729 150 HWTCCGLSCYYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQIYKNNYWIGLSYDERESKWKWVDSGSSPgiNV 229
Cdd:cd03593    4 DWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSPLN--NL 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 836937729 230 GIMNSSSGRGKCAFLSSTRVAAIDCIQTYNCICEK 264
Cdd:cd03593   82 FNIRGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
Ly49 super family cl07131
Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or ...
 41-161 1.75e-35

Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or are similar to, Ly49 receptors. These are type II transmembrane receptors expressed by mouse natural killer (NK) cells. They are classified as being activating (e.g.Ly49D and H) or inhibitory (e.g. Ly49A and G), depending on their effect on NK cell function. They are members of the C-type lectin receptor superfamily, and in fact in many family members this region is found immediately N-terminal to a lectin C-type domain (pfam00059).


The actual alignment was detected with superfamily member pfam08391:

Pssm-ID: 462461 [Multi-domain]  Cd Length: 119  Bit Score: 123.62  E-value: 1.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729   41 SVSWRLIAVSLGILCLVLLVIVTVLVTKIFQCIQERHHQQEILGH-----LSQKDNYLKEQLLINKTLEYDILKNEslqq 115
Cdd:pfam08391   1 SVPWHLIVIALGILCSLLLVTVAVLGTKIFQYIQEKHELEETLNLhqncsIMQNDIYLKEEMLRNKSIECSILNNL---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 836937729  116 kkkLDSLFLKNNICHIKNEIFSKSLENTGKRYEAHWTCCGLSCYYF 161
Cdd:pfam08391  77 ---LDSLNREQNRWYRKTKTVLKSLQHTGKGVEIHWFCYGIKCYYF 119
 
Name Accession Description Interval E-value
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 150-264 5.41e-41

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: 137.46  E-value: 5.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729 150 HWTCCGLSCYYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQIYKNNYWIGLSYDERESKWKWVDSGSSPgiNV 229
Cdd:cd03593    4 DWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSPLN--NL 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 836937729 230 GIMNSSSGRGKCAFLSSTRVAAIDCIQTYNCICEK 264
Cdd:cd03593   82 FNIRGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
Ly49 pfam08391
Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or ...
 41-161 1.75e-35

Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or are similar to, Ly49 receptors. These are type II transmembrane receptors expressed by mouse natural killer (NK) cells. They are classified as being activating (e.g.Ly49D and H) or inhibitory (e.g. Ly49A and G), depending on their effect on NK cell function. They are members of the C-type lectin receptor superfamily, and in fact in many family members this region is found immediately N-terminal to a lectin C-type domain (pfam00059).


Pssm-ID: 462461 [Multi-domain]  Cd Length: 119  Bit Score: 123.62  E-value: 1.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729   41 SVSWRLIAVSLGILCLVLLVIVTVLVTKIFQCIQERHHQQEILGH-----LSQKDNYLKEQLLINKTLEYDILKNEslqq 115
Cdd:pfam08391   1 SVPWHLIVIALGILCSLLLVTVAVLGTKIFQYIQEKHELEETLNLhqncsIMQNDIYLKEEMLRNKSIECSILNNL---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 836937729  116 kkkLDSLFLKNNICHIKNEIFSKSLENTGKRYEAHWTCCGLSCYYF 161
Cdd:pfam08391  77 ---LDSLNREQNRWYRKTKTVLKSLQHTGKGVEIHWFCYGIKCYYF 119
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 151-263 4.52e-23

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: 91.51  E-value: 4.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729   151 WTCCGLSCYYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQIYKN----NYWIGLSYDERESKWKWVD-SGSSP 225
Cdd:smart00034   5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSgssdYYWIGLSDPDSNGSWQWSDgSGPVS 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 836937729   226 GINVGIMNSSSGRGKCAFLSSTRV--AAIDCIQTYNCICE 263
Cdd:smart00034  85 YSNWAPGEPNNSSGDCVVLSTSGGkwNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 166-264 4.64e-14

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 66.73  E-value: 4.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729  166 KNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQI--YKNNYWIGLSYDERESKWKWVD-SGSSPGINVGIMNSSSGRGKCA 242
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLkkSNKYFWIGLTDRKNEGTWKWVDgSPVNYTNWAPEPNNNGENEDCV 81

                          90       100
                  ....*....|....*....|....
gi 836937729  243 FLSST--RVAAIDCIQTYNCICEK 264
Cdd:pfam00059  82 ELSSSsgKWNDENCNSKNPFVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 151-264 5.04e-14

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 69.37  E-value: 5.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729 151 WTCCGLSCYYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQIYKNNYWIGLSYDERESKWKWVDSGSspginvg 230
Cdd:PHA02642  92 WIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNRESSNHPWKWADNSN------- 164

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 836937729 231 iMNSS---SGRGKCAFLSSTRVAAIDCIQTYNCICEK 264
Cdd:PHA02642 165 -YNASfviTGTGECAYLNDIRISSSRVYANRKWICSK 200
 
Name Accession Description Interval E-value
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 150-264 5.41e-41

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: 137.46  E-value: 5.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729 150 HWTCCGLSCYYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQIYKNNYWIGLSYDERESKWKWVDSGSSPgiNV 229
Cdd:cd03593    4 DWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSPLN--NL 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 836937729 230 GIMNSSSGRGKCAFLSSTRVAAIDCIQTYNCICEK 264
Cdd:cd03593   82 FNIRGSTKSGNCAYLSSTGIYSEDCSTKKRWICEK 116
Ly49 pfam08391
Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or ...
 41-161 1.75e-35

Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or are similar to, Ly49 receptors. These are type II transmembrane receptors expressed by mouse natural killer (NK) cells. They are classified as being activating (e.g.Ly49D and H) or inhibitory (e.g. Ly49A and G), depending on their effect on NK cell function. They are members of the C-type lectin receptor superfamily, and in fact in many family members this region is found immediately N-terminal to a lectin C-type domain (pfam00059).


Pssm-ID: 462461 [Multi-domain]  Cd Length: 119  Bit Score: 123.62  E-value: 1.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729   41 SVSWRLIAVSLGILCLVLLVIVTVLVTKIFQCIQERHHQQEILGH-----LSQKDNYLKEQLLINKTLEYDILKNEslqq 115
Cdd:pfam08391   1 SVPWHLIVIALGILCSLLLVTVAVLGTKIFQYIQEKHELEETLNLhqncsIMQNDIYLKEEMLRNKSIECSILNNL---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 836937729  116 kkkLDSLFLKNNICHIKNEIFSKSLENTGKRYEAHWTCCGLSCYYF 161
Cdd:pfam08391  77 ---LDSLNREQNRWYRKTKTVLKSLQHTGKGVEIHWFCYGIKCYYF 119
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 151-263 4.52e-23

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: 91.51  E-value: 4.52e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729   151 WTCCGLSCYYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQIYKN----NYWIGLSYDERESKWKWVD-SGSSP 225
Cdd:smart00034   5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSgssdYYWIGLSDPDSNGSWQWSDgSGPVS 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 836937729   226 GINVGIMNSSSGRGKCAFLSSTRV--AAIDCIQTYNCICE 263
Cdd:smart00034  85 YSNWAPGEPNNSSGDCVVLSTSGGkwNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 157-264 2.31e-18

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: 78.82  E-value: 2.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729 157 SCYYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQIYKNN---YWIGLSYDERESKWKWVD-SGSSPGIN-VGI 231
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssdVWIGLNDLSSEGTWKWSDgSPLVDYTNwAPG 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 836937729 232 MNSSSGRGKCAFLSST---RVAAIDCIQTYNCICEK 264
Cdd:cd00037   81 EPNPGGSEDCVVLSSSsdgKWNDVSCSSKLPFICEK 116
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 148-264 9.35e-17

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 74.65  E-value: 9.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729 148 EAHWTCCGLSCYYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFV-QLQIYKNNYWIGLSYDERESKWKWVDsGSSPG 226
Cdd:cd03590    2 PTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFIsKILSGNRSYWIGLSDEETEGEWKWVD-GTPLN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 836937729 227 INVGIM-----NSSSGRG-KCAFLSSTRVAAID--CIQTYNCICEK 264
Cdd:cd03590   81 SSKTFWhpgepNNWGGGGeDCAELVYDSGGWNDvpCNLEYRWICEK 126
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 166-264 4.64e-14

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 66.73  E-value: 4.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729  166 KNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQI--YKNNYWIGLSYDERESKWKWVD-SGSSPGINVGIMNSSSGRGKCA 242
Cdd:pfam00059   2 KTWDEAREACRKLGGHLVSINSAEELDFLSSTLkkSNKYFWIGLTDRKNEGTWKWVDgSPVNYTNWAPEPNNNGENEDCV 81

                          90       100
                  ....*....|....*....|....
gi 836937729  243 FLSST--RVAAIDCIQTYNCICEK 264
Cdd:pfam00059  82 ELSSSsgKWNDENCNSKNPFVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 151-264 5.04e-14

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 69.37  E-value: 5.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729 151 WTCCGLSCYYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQIYKNNYWIGLSYDERESKWKWVDSGSspginvg 230
Cdd:PHA02642  92 WIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGLNRESSNHPWKWADNSN------- 164

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 836937729 231 iMNSS---SGRGKCAFLSSTRVAAIDCIQTYNCICEK 264
Cdd:PHA02642 165 -YNASfviTGTGECAYLNDIRISSSRVYANRKWICSK 200
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 159-224 5.59e-06

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: 44.72  E-value: 5.59e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 836937729 159 YYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQIYKN-NYWIGLSYDERESKWKWVDSGSS 224
Cdd:cd03603    3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYgASWIGASDAATEGTWKWSDGEES 69
PHA02867 PHA02867
C-type lectin protein; Provisional
 158-205 1.62e-04

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 41.21  E-value: 1.62e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 836937729 158 CYYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFVQlQIYKNNYWI 205
Cdd:PHA02867  60 CYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFVS-RYGKGSYWI 106
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 158-262 2.76e-04

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 40.62  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729 158 CYYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQIYKNNYWIGLSYderesKWKWVDSGSSPGINVGIMNSssg 237
Cdd:PHA03097  57 CYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGIEK-----KKGDDDDREVLDKVVKPPKS--- 128

                         90       100
                 ....*....|....*....|....*
gi 836937729 238 rGKCAFLSSTRVAAIDCIQTYNCIC 262
Cdd:PHA03097 129 -GKCAYLKDKTIISSNCNATKGWIC 152
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 157-247 3.26e-04

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: 39.66  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729 157 SCYYFAVENKNWKGCKQTCRSYKSS--LLKIDDEDELTFV-----QLQIYKNNYWIGLSYDERESKWKWVDsGSSPGINV 229
Cdd:cd03594   11 NCYGYFRQPLSWSDAELFCQKYGPGahLASIHSPAEAAAIaslisSYQKAYQPVWIGLHDPQQSRGWEWSD-GSKLDYRS 89

                         90
                 ....*....|....*....
gi 836937729 230 GIMNSSSGRGK-CAFLSST 247
Cdd:cd03594   90 WDRNPPYARGGyCAELSRS 108
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 159-262 1.10e-03

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: 37.74  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729 159 YYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQIYKNN--YWIGLSYDerESKWKWVDsGSSPGINVGIMNSSS 236
Cdd:cd03602    3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNsaAWIGLYRD--VDSWRWSD-GSESSFRNWNTFQPF 79

                         90       100
                 ....*....|....*....|....*..
gi 836937729 237 GRGKCAFLSST-RVAAIDCIQTYNCIC 262
Cdd:cd03602   80 GQGDCATMYSSgRWYAALCSALKPFIC 106
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 151-264 3.25e-03

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.


Pssm-ID: 153067  Cd Length: 129  Bit Score: 36.79  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729 151 WTCCGLSCYYFAVENKNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQIYKNNY-------WIGLsydeRE---SKWKWVD 220
Cdd:cd03597    5 WHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMtkqkltpWVGL----RKinvSYWCWED 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 836937729 221 sgSSPGINVGIM---NSSSGRGKCAFLSSTRVA---AIDCIQTYN-CICEK 264
Cdd:cd03597   81 --MSPFTNTTLQwlpGEPSDAGFCGYLEEPAVSglkANPCTNPVNgSVCER 129
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 151-224 3.61e-03

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


Pssm-ID: 153059  Cd Length: 137  Bit Score: 36.95  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836937729 151 WTCCGLSCYYFAVENKNWKGCKQTCRSYKSS-----LLKIDDEDELTFVqLQIYKN--------NYWIGLSYDERESKWK 217
Cdd:cd03589    5 WTAFGGYCYRFFGDRLTWEEAELRCRSFSIPgliahLVSIHSQEENDFV-YDLFESsrgpdtpyGLWIGLHDRTSEGPFE 83


                 ....*..
gi 836937729 218 WVDsGSS 224
Cdd:cd03589   84 WTD-GSP 89
PH_ORP9 cd13290
Human Oxysterol binding protein related protein 9 Pleckstrin homology (PH) domain; Human ORP9 ...
 155-221 3.91e-03

Human Oxysterol binding protein related protein 9 Pleckstrin homology (PH) domain; Human ORP9 is proposed to function in regulation of Akt phosphorylation. ORP9 has 2 forms, a long (ORP9L) and a short (ORP9S). ORP9L contains an N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP1S is truncated and contains a FFAT motif and an OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241444  Cd Length: 102  Bit Score: 36.27  E-value: 3.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 836937729 155 GLSCYYFAVEnKNWKGCKQTCRSYKSSLLKIDDEDELTFVQLQIYKNNYWIGLSYDEREskwKWVDS 221
Cdd:cd13290   27 GLLSYYTSKE-KMMRGSRRGCVRLKGAVVGIDDEDDSTFTITVDQKTFHFQARDAEERE---RWIRA 89
 
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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