NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039774391|ref|XP_017176903|]
View 

killer cell lectin-like receptor 2 isoform X2 [Mus musculus]

Protein Classification

Ly49 and CLECT_NK_receptors_like domain-containing protein( domain architecture ID 10551997)

Ly49 and CLECT_NK_receptors_like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Ly49 pfam08391
Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or ...
 147-266 7.88e-58

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: 184.48  E-value: 7.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391 147 SVPWKFIVIVLGILCFLLLVTVAVLVIHIFRDGQEKHEQEKTLNnLRQEYQVMKNDSSLMEEMLRNKSSECKALNDSLHY 226
Cdd:pfam08391   1 SVPWHLIVIALGILCSLLLVTVAVLGTKIFQYIQEKHELEETLN-LHQNCSIMQNDIYLKEEMLRNKSIECSILNNLLDS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039774391 227 LNREQNRCLRKTKIVLDCSQNKGKQVEGYWFCCGMKCYYF 266
Cdd:pfam08391  80 LNREQNRWYRKTKTVLKSLQHTGKGVEIHWFCYGIKCYYF 119
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 253-368 1.32e-32

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: 118.59  E-value: 1.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391 253 EGYWFCCGMKCYYFIMDDKKLKGCKQICQAYNLTLLKTNDEDELKFLKSQLQRNTYWIALTHHESKEESQQIGDRPSKPV 332
Cdd:cd03593     2 PKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSPLNNL 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039774391 333 SAARNSVPNREkCAYLNSFSTEEDDRARNHGCICEK 368
Cdd:cd03593    82 FNIRGSTKSGN-CAYLSSTGIYSEDCSTKKRWICEK 116
 
Name Accession Description Interval E-value
Ly49 pfam08391
Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or ...
 147-266 7.88e-58

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: 184.48  E-value: 7.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391 147 SVPWKFIVIVLGILCFLLLVTVAVLVIHIFRDGQEKHEQEKTLNnLRQEYQVMKNDSSLMEEMLRNKSSECKALNDSLHY 226
Cdd:pfam08391   1 SVPWHLIVIALGILCSLLLVTVAVLGTKIFQYIQEKHELEETLN-LHQNCSIMQNDIYLKEEMLRNKSIECSILNNLLDS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039774391 227 LNREQNRCLRKTKIVLDCSQNKGKQVEGYWFCCGMKCYYF 266
Cdd:pfam08391  80 LNREQNRWYRKTKTVLKSLQHTGKGVEIHWFCYGIKCYYF 119
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 253-368 1.32e-32

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: 118.59  E-value: 1.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391 253 EGYWFCCGMKCYYFIMDDKKLKGCKQICQAYNLTLLKTNDEDELKFLKSQLQRNTYWIALTHHESKEESQQIGDRPSKPV 332
Cdd:cd03593     2 PKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSPLNNL 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039774391 333 SAARNSVPNREkCAYLNSFSTEEDDRARNHGCICEK 368
Cdd:cd03593    82 FNIRGSTKSGN-CAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 256-367 2.39e-11

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 60.69  E-value: 2.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391  256 WFCCGMKCYYFIMDDKKLKGCKQICQAYNLTLLKTNDEDELKFLKSQLQRNT----YWIALTHHESKEESQQIGDRPSKP 331
Cdd:smart00034   5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGssdyYWIGLSDPDSNGSWQWSDGSGPVS 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1039774391  332 VSAARNSVPN--REKCAYLNSFSTEEDDRA--RNHGCICE 367
Cdd:smart00034  85 YSNWAPGEPNnsSGDCVVLSTSGGKWNDVSctSKLPFVCE 124
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 256-380 7.36e-09

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 55.51  E-value: 7.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391 256 WFCCGMKCYYFIMDDKKLKGCKQICQAYNLTLLKTNDEDELKFLKSQLQRNTYWIALtHHESKEESQQIGDRPSKPVSAA 335
Cdd:PHA02642   92 WIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGL-NRESSNHPWKWADNSNYNASFV 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1039774391 336 rnsVPNREKCAYLNSFSTEEDDRARNHGCICEKRLNKFPIPGSCA 380
Cdd:PHA02642  171 ---ITGTGECAYLNDIRISSSRVYANRKWICSKTYTNIYIPSNNS 212
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 275-368 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: 43.24  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391 275 GCKQICQAYNLTLLKTNDEDELKFLKSQLQRNT--YWIALTHHESKEESQQIGDRP--SKPVSAARNSVPNREKCAYLNS 350
Cdd:pfam00059   6 EAREACRKLGGHLVSINSAEELDFLSSTLKKSNkyFWIGLTDRKNEGTWKWVDGSPvnYTNWAPEPNNNGENEDCVELSS 85

                          90       100
                  ....*....|....*....|
gi 1039774391 351 FSTEEDDRARN--HGCICEK 368
Cdd:pfam00059  86 SSGKWNDENCNskNPFVCEK 105
 
Name Accession Description Interval E-value
Ly49 pfam08391
Ly49-like protein, N-terminal region; The sequences making up this family are annotated as, or ...
 147-266 7.88e-58

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: 184.48  E-value: 7.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391 147 SVPWKFIVIVLGILCFLLLVTVAVLVIHIFRDGQEKHEQEKTLNnLRQEYQVMKNDSSLMEEMLRNKSSECKALNDSLHY 226
Cdd:pfam08391   1 SVPWHLIVIALGILCSLLLVTVAVLGTKIFQYIQEKHELEETLN-LHQNCSIMQNDIYLKEEMLRNKSIECSILNNLLDS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039774391 227 LNREQNRCLRKTKIVLDCSQNKGKQVEGYWFCCGMKCYYF 266
Cdd:pfam08391  80 LNREQNRWYRKTKTVLKSLQHTGKGVEIHWFCYGIKCYYF 119
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 253-368 1.32e-32

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: 118.59  E-value: 1.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391 253 EGYWFCCGMKCYYFIMDDKKLKGCKQICQAYNLTLLKTNDEDELKFLKSQLQRNTYWIALTHHESKEESQQIGDRPSKPV 332
Cdd:cd03593     2 PKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSYWIGLSREKSEKPWKWIDGSPLNNL 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039774391 333 SAARNSVPNREkCAYLNSFSTEEDDRARNHGCICEK 368
Cdd:cd03593    82 FNIRGSTKSGN-CAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 256-367 2.39e-11

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 60.69  E-value: 2.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391  256 WFCCGMKCYYFIMDDKKLKGCKQICQAYNLTLLKTNDEDELKFLKSQLQRNT----YWIALTHHESKEESQQIGDRPSKP 331
Cdd:smart00034   5 WISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGssdyYWIGLSDPDSNGSWQWSDGSGPVS 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1039774391  332 VSAARNSVPN--REKCAYLNSFSTEEDDRA--RNHGCICE 367
Cdd:smart00034  85 YSNWAPGEPNnsSGDCVVLSTSGGKWNDVSctSKLPFVCE 124
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 256-380 7.36e-09

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 55.51  E-value: 7.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391 256 WFCCGMKCYYFIMDDKKLKGCKQICQAYNLTLLKTNDEDELKFLKSQLQRNTYWIALtHHESKEESQQIGDRPSKPVSAA 335
Cdd:PHA02642   92 WIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYKDSSDHWIGL-NRESSNHPWKWADNSNYNASFV 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1039774391 336 rnsVPNREKCAYLNSFSTEEDDRARNHGCICEKRLNKFPIPGSCA 380
Cdd:PHA02642  171 ---ITGTGECAYLNDIRISSSRVYANRKWICSKTYTNIYIPSNNS 212
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 262-368 1.03e-07

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


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 49.93  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391 262 KCYYFIMDDKKLKGCKQICQAYNLTLLKTNDEDELKFLKSQLQRNT---YWIALTHHESKEESQQIGDRPSKPVSAARNS 338
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSssdVWIGLNDLSSEGTWKWSDGSPLVDYTNWAPG 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039774391 339 VPN---REKCAYLNSFSTEE-DDRA--RNHGCICEK 368
Cdd:cd00037    81 EPNpggSEDCVVLSSSSDGKwNDVScsSKLPFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 275-368 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: 43.24  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391 275 GCKQICQAYNLTLLKTNDEDELKFLKSQLQRNT--YWIALTHHESKEESQQIGDRP--SKPVSAARNSVPNREKCAYLNS 350
Cdd:pfam00059   6 EAREACRKLGGHLVSINSAEELDFLSSTLKKSNkyFWIGLTDRKNEGTWKWVDGSPvnYTNWAPEPNNNGENEDCVELSS 85

                          90       100
                  ....*....|....*....|
gi 1039774391 351 FSTEEDDRARN--HGCICEK 368
Cdd:pfam00059  86 SSGKWNDENCNskNPFVCEK 105
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 262-370 3.85e-04

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 40.62  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774391 262 KCYYFIMDDKKLKGCKQICQAYNLTLLKTNDEDELKFLKSQLQRNTYWIALTHHESKEESQQIGDRPSKPvsaarnsvPN 341
Cdd:PHA03097   56 KCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYKGGQDLWIGIEKKKGDDDDREVLDKVVKP--------PK 127

                          90       100
                  ....*....|....*....|....*....
gi 1039774391 342 REKCAYLNSFSTEEDDRARNHGCICEKRL 370
Cdd:PHA03097  128 SGKCAYLKDKTIISSNCNATKGWICFDRL 156
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH