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Conserved domains on  [gi|119964698|ref|NP_001028343|]
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killer cell lectin-like receptor subfamily G member 2 [Mus musculus]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10132518)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein may bind carbohydrate in a calcium-dependent manner

CATH:  3.10.100.10
Gene Ontology:  GO:0030246
PubMed:  16336259|10508765
SCOP:  4002453

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); ...
 271-382 1.32e-26

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: 102.41  E-value: 1.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698 271 CPQGWMWSQEQCYYLSEEAQDWEGSQAFCSAHHATLPLLSHT--QDFLRKYRITKGSWVGARRGPEG--WHWTDGVPLPS 346
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEeeLEFLQSQIGSSSYWIGLSREKSEkpWKWIDGSPLNN 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119964698 347 QLFPadSEDHPDFSCGGLEEGRLVALDCSSPRPWVC 382
Cdd:cd03593   81 LFNI--RGSTKSGNCAYLSSTGIYSEDCSTKKRWIC 114
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 4-197 1.09e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698    4 PQVPAEAPQPRA----SEDSPRPERTGWEEPDAQPQELPEKSPSPAlsgsprvpPLSLGYGAFRRLGSCSRELPSPSPSW 79
Cdd:PHA03247 2589 PDAPPQSARPRApvddRGDPRGPAPPSPLPPDTHAPDPPPPSPSPA--------ANEPDPHPPPTVPPPERPRDDPAPGR 2660

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   80 AEQPRDGEAELEPWTASGEP-------APASWAPVELQVDVRVKPvgaagasRAPSPAPSTRFLTVPVPESPAFARRSAP 152
Cdd:PHA03247 2661 VSRPRRARRLGRAAQASSPPqrprrraARPTVGSLTSLADPPPPP-------PTPEPAPHALVSATPLPPGPAAARQASP 2733

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119964698  153 TLQWLPRAPS-------PGSTWSRGSPLAANATESVSPAEGcmvPPGSPACR 197
Cdd:PHA03247 2734 ALPAAPAPPAvpagpatPGGPARPARPPTTAGPPAPAPPAA---PAAGPPRR 2782
 
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); ...
 271-382 1.32e-26

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: 102.41  E-value: 1.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698 271 CPQGWMWSQEQCYYLSEEAQDWEGSQAFCSAHHATLPLLSHT--QDFLRKYRITKGSWVGARRGPEG--WHWTDGVPLPS 346
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEeeLEFLQSQIGSSSYWIGLSREKSEkpWKWIDGSPLNN 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119964698 347 QLFPadSEDHPDFSCGGLEEGRLVALDCSSPRPWVC 382
Cdd:cd03593   81 LFNI--RGSTKSGNCAYLSSTGIYSEDCSTKKRWIC 114
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 271-382 8.76e-18

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: 78.80  E-value: 8.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   271 CPQGWMWSQEQCYYLSEEAQDWEGSQAFCSAHHATLPLL--SHTQDFLRKY----RITKGSWVGARRGPE--GWHWTDGV 342
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIhsEAENDFVASLlknsGSSDYYWIGLSDPDSngSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 119964698   343 PLPSQLFPADSEdhPDFSCGG-----LEEGRLVALDCSSPRPWVC 382
Cdd:smart00034  81 GPVSYSNWAPGE--PNNSSGDcvvlsTSGGKWNDVSCTSKLPFVC 123
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 237-384 3.05e-12

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 65.52  E-value: 3.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698 237 KSLRWALVVMAVLLAVCTVAVVALASRGGTKCQP------CPQGWMWSQEQCYYLSEEAQDWEGSQAFCSAHHATLPLLS 310
Cdd:PHA02642  48 EKLYCCIITICILITINLVPIIILMAFKSDTQEPtikyvtCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVE 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119964698 311 HTQD--FLRKYRITKGSWVGARRGPEG--WHWTDGVPLPSQLFPADSEDhpdfsCGGLEEGRLVALDCSSPRPWVCAR 384
Cdd:PHA02642 128 TEEElnFLKRYKDSSDHWIGLNRESSNhpWKWADNSNYNASFVITGTGE-----CAYLNDIRISSSRVYANRKWICSK 200
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 292-382 7.31e-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: 52.87  E-value: 7.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698  292 WEGSQAFCSAHHATLPLL--SHTQDFLRKY--RITKGSWVG-ARRGPEG-WHWTDGVPL-PSQLFPADSEDHPDFSCGGL 364
Cdd:pfam00059   4 WDEAREACRKLGGHLVSInsAEELDFLSSTlkKSNKYFWIGlTDRKNEGtWKWVDGSPVnYTNWAPEPNNNGENEDCVEL 83

                          90       100
                  ....*....|....*....|
gi 119964698  365 EE--GRLVALDCSSPRPWVC 382
Cdd:pfam00059  84 SSssGKWNDENCNSKNPFVC 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 4-197 1.09e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698    4 PQVPAEAPQPRA----SEDSPRPERTGWEEPDAQPQELPEKSPSPAlsgsprvpPLSLGYGAFRRLGSCSRELPSPSPSW 79
Cdd:PHA03247 2589 PDAPPQSARPRApvddRGDPRGPAPPSPLPPDTHAPDPPPPSPSPA--------ANEPDPHPPPTVPPPERPRDDPAPGR 2660

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   80 AEQPRDGEAELEPWTASGEP-------APASWAPVELQVDVRVKPvgaagasRAPSPAPSTRFLTVPVPESPAFARRSAP 152
Cdd:PHA03247 2661 VSRPRRARRLGRAAQASSPPqrprrraARPTVGSLTSLADPPPPP-------PTPEPAPHALVSATPLPPGPAAARQASP 2733

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119964698  153 TLQWLPRAPS-------PGSTWSRGSPLAANATESVSPAEGcmvPPGSPACR 197
Cdd:PHA03247 2734 ALPAAPAPPAvpagpatPGGPARPARPPTTAGPPAPAPPAA---PAAGPPRR 2782
 
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); ...
 271-382 1.32e-26

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: 102.41  E-value: 1.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698 271 CPQGWMWSQEQCYYLSEEAQDWEGSQAFCSAHHATLPLLSHT--QDFLRKYRITKGSWVGARRGPEG--WHWTDGVPLPS 346
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEeeLEFLQSQIGSSSYWIGLSREKSEkpWKWIDGSPLNN 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 119964698 347 QLFPadSEDHPDFSCGGLEEGRLVALDCSSPRPWVC 382
Cdd:cd03593   81 LFNI--RGSTKSGNCAYLSSTGIYSEDCSTKKRWIC 114
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 271-382 8.76e-18

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: 78.80  E-value: 8.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   271 CPQGWMWSQEQCYYLSEEAQDWEGSQAFCSAHHATLPLL--SHTQDFLRKY----RITKGSWVGARRGPE--GWHWTDGV 342
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIhsEAENDFVASLlknsGSSDYYWIGLSDPDSngSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 119964698   343 PLPSQLFPADSEdhPDFSCGG-----LEEGRLVALDCSSPRPWVC 382
Cdd:smart00034  81 GPVSYSNWAPGE--PNNSSGDcvvlsTSGGKWNDVSCTSKLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 282-382 4.75e-14

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: 68.03  E-value: 4.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698 282 CYYLSEEAQDWEGSQAFCSAHHATlpLLS-HT---QDFLRKY---RITKGSWVGARRGPE--GWHWTDGVPLPSQLFPAD 352
Cdd:cd00037    2 CYKFSTEKLTWEEAQEYCRSLGGH--LASiHSeeeNDFLASLlkkSSSSDVWIGLNDLSSegTWKWSDGSPLVDYTNWAP 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 119964698 353 SEDHPDFS--CGGL---EEGRLVALDCSSPRPWVC 382
Cdd:cd00037   80 GEPNPGGSedCVVLsssSDGKWNDVSCSSKLPFIC 114
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 237-384 3.05e-12

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 65.52  E-value: 3.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698 237 KSLRWALVVMAVLLAVCTVAVVALASRGGTKCQP------CPQGWMWSQEQCYYLSEEAQDWEGSQAFCSAHHATLPLLS 310
Cdd:PHA02642  48 EKLYCCIITICILITINLVPIIILMAFKSDTQEPtikyvtCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVE 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119964698 311 HTQD--FLRKYRITKGSWVGARRGPEG--WHWTDGVPLPSQLFPADSEDhpdfsCGGLEEGRLVALDCSSPRPWVCAR 384
Cdd:PHA02642 128 TEEElnFLKRYKDSSDHWIGLNRESSNhpWKWADNSNYNASFVITGTGE-----CAYLNDIRISSSRVYANRKWICSK 200
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 271-382 1.47e-10

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: 58.47  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698 271 CPQGWMWSQEQCYYLSEEAQDWEGSQAFCSAHHATLPLLsHT---QDFLRKYRITKGS-WVGAR-RGPEG-WHWTDGVPL 344
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVII-NSqeeQEFISKILSGNRSyWIGLSdEETEGeWKWVDGTPL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 119964698 345 -PSQLFPADSEdhPDfSCGGLEE--GRLVALD-------CSSPRPWVC 382
Cdd:cd03590   80 nSSKTFWHPGE--PN-NWGGGGEdcAELVYDSggwndvpCNLEYRWIC 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 292-382 7.31e-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: 52.87  E-value: 7.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698  292 WEGSQAFCSAHHATLPLL--SHTQDFLRKY--RITKGSWVG-ARRGPEG-WHWTDGVPL-PSQLFPADSEDHPDFSCGGL 364
Cdd:pfam00059   4 WDEAREACRKLGGHLVSInsAEELDFLSSTlkKSNKYFWIGlTDRKNEGtWKWVDGSPVnYTNWAPEPNNNGENEDCVEL 83

                          90       100
                  ....*....|....*....|
gi 119964698  365 EE--GRLVALDCSSPRPWVC 382
Cdd:pfam00059  84 SSssGKWNDENCNSKNPFVC 103
PHA03247 PHA03247
large tegument protein UL36; Provisional
 4-197 1.09e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698    4 PQVPAEAPQPRA----SEDSPRPERTGWEEPDAQPQELPEKSPSPAlsgsprvpPLSLGYGAFRRLGSCSRELPSPSPSW 79
Cdd:PHA03247 2589 PDAPPQSARPRApvddRGDPRGPAPPSPLPPDTHAPDPPPPSPSPA--------ANEPDPHPPPTVPPPERPRDDPAPGR 2660

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   80 AEQPRDGEAELEPWTASGEP-------APASWAPVELQVDVRVKPvgaagasRAPSPAPSTRFLTVPVPESPAFARRSAP 152
Cdd:PHA03247 2661 VSRPRRARRLGRAAQASSPPqrprrraARPTVGSLTSLADPPPPP-------PTPEPAPHALVSATPLPPGPAAARQASP 2733

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119964698  153 TLQWLPRAPS-------PGSTWSRGSPLAANATESVSPAEGcmvPPGSPACR 197
Cdd:PHA03247 2734 ALPAAPAPPAvpagpatPGGPARPARPPTTAGPPAPAPPAA---PAAGPPRR 2782
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 283-382 1.61e-06

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: 46.21  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698 283 YYLSEEAQDWEGSQAFCSAHHATLPLLSHTQDfLRKYRIT-----KGSWVGARRGPEGWHWTDG---VPLPSQLFPADSE 354
Cdd:cd03602    3 FYLVNESKTWSEAQQYCRENYTDLATVQNQED-NALLSNLsrvsnSAAWIGLYRDVDSWRWSDGsesSFRNWNTFQPFGQ 81

                         90       100
                 ....*....|....*....|....*....
gi 119964698 355 DHpdfsCGGLE-EGRLVALDCSSPRPWVC 382
Cdd:cd03602   82 GD----CATMYsSGRWYAALCSALKPFIC 106
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 2-197 9.04e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.86  E-value: 9.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698    2 EPPQVPAEAPQPRASEDSPRPERTGWEEPDAQPQELPEKSPSPALSGSPRVPPLSLGYGAFRRLGSCSRELPSPSPSWAE 81
Cdd:PHA03307  147 PPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGR 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   82 QPRDGEAELEPWTASGEPAPASWAPVELQVDVRVKPVGAAGASRAPSPAPSTRFLTVPVPESPAFARRSAPTLQWLPRAP 161
Cdd:PHA03307  227 SAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSG 306

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 119964698  162 SPGST------WSRGSPLAANATESVSPA-EGCMVPPGSPACR 197
Cdd:PHA03307  307 PAPSSprasssSSSSRESSSSSTSSSSESsRGAAVSPGPSPSR 349
PHA03247 PHA03247
large tegument protein UL36; Provisional
 4-203 2.69e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698    4 PQVPAEAPQPRASEDSPRPeRTGWEEPDAQPQElPEKSPSPALSGSPRVPPLSLGYGAFRRLGSCSreLPSPSPSWAEQP 83
Cdd:PHA03247 2676 ASSPPQRPRRRAARPTVGS-LTSLADPPPPPPT-PEPAPHALVSATPLPPGPAAARQASPALPAAP--APPAVPAGPATP 2751

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   84 RDGEAELEPWTASGEPAPASWAPVELQVDVRVKPVGAAGASRAPSPAPSTRFLTVPVPESPAFARRSAPTLQWLPRAPSP 163
Cdd:PHA03247 2752 GGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP 2831

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 119964698  164 GSTWSRGSPLAANATESVSPAEGCMVPPGSPACRCRCREP 203
Cdd:PHA03247 2832 TSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP 2871
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 2-163 8.82e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 8.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   2 EPPQVPAEAPQPRASEDSPRPERTGWEEPDAQPQELPEKSPSPALSGSPRVPPLSLGYGAFRRLGSCSRELPSPSPSWAE 81
Cdd:PRK07764 610 EEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAA 689

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698  82 QPRDG------EAELEPWTASGEPAPASWAPVELQVDVRVKPVGAAGASRAPSPAPSTRFLTVPVPESPAFARRSAPTLQ 155
Cdd:PRK07764 690 PAAPAgaapaqPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAA 769


                 ....*...
gi 119964698 156 WLPRAPSP 163
Cdd:PRK07764 770 PAAAPPPS 777
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
3-205 1.77e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   3 PPQVPAEAPQPRASEDSP-RPERTGWEEPDAQPQELPEKSPSPALSGSPRVPPLSLGYGA----FRRLGSCSRELPSPSP 77
Cdd:PRK12323 377 AAAAPVAQPAPAAAAPAAaAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAArqasARGPGGAPAPAPAPAA 456

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698  78 SWAEQPRDGEAELEPWTASGEPAPASWAPvelqvdvrvkpvgAAGASRAPSPAPSTRFLTVPVPESPAFARRSAPTLQWL 157
Cdd:PRK12323 457 APAAAARPAAAGPRPVAAAAAAAPARAAP-------------AAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVA 523

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 119964698 158 PRAPSPGSTWSRG--SPLAANATESVSPAEGCMVPPGSPACRCRCREPGL 205
Cdd:PRK12323 524 ESIPDPATADPDDafETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGL 573
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 5-190 2.36e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 42.99  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   5 QVPAEAPQPRASEDS----PRPERTGWEEPDAQPQElpeKSPSPALSGSPRvpPLSlGYGAFRRLGSCSRELPSPSPSWA 80
Cdd:PLN03209 322 KIPSQRVPPKESDAAdgpkPVPTKPVTPEAPSPPIE---EEPPQPKAVVPR--PLS-PYTAYEDLKPPTSPIPTPPSSSP 395

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698  81 EQPRDGEAELEPWTASGEPAPaswapvELQVDVRVKPVGAAGASRAPSPAPSTRFLTVPVPESPAfarRSAPTLQWLPRA 160
Cdd:PLN03209 396 ASSKSVDAVAKPAEPDVVPSP------GSASNVPEVEPAQVEAKKTRPLSPYARYEDLKPPTSPS---PTAPTGVSPSVS 466

                        170       180       190
                 ....*....|....*....|....*....|
gi 119964698 161 PSPGSTWSRGSPLAANATESVSPAEGCMVP 190
Cdd:PLN03209 467 STSSVPAVPDTAPATAATDAAAPPPANMRP 496
PHA03247 PHA03247
large tegument protein UL36; Provisional
 3-194 8.65e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 8.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698    3 PPQVPAEAPQPRASEdSPRPERTGWEEPDAQPQELPEKSPSPALSGSPRVPPLSLGYGAFRRLGSCSRELPSPSPSWAEQ 82
Cdd:PHA03247 2702 PPPPPTPEPAPHALV-SATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   83 PRDGEAELEPWTASGEPAPASWAPVELQVDVrvkPVGAAGASRAPSPAPSTRFLTVPVPESPAFARRSAPTLQWLPRAPS 162
Cdd:PHA03247 2781 RRLTRPAVASLSESRESLPSPWDPADPPAAV---LAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA 2857

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 119964698  163 PGSTWSR----GSPLAANATESVSPAEGCMVPPGSP 194
Cdd:PHA03247 2858 PGGDVRRrppsRSPAAKPAAPARPPVRRLARPAVSR 2893
PHA03247 PHA03247
large tegument protein UL36; Provisional
 3-175 9.03e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 9.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698    3 PPQVPAEAPQPRASEDSPRPERT-GWEEPDAQPQELPEKSPSPALSGSPRVPPLSLGYGAFRRLGSCSRELPSPSPSWAE 81
Cdd:PHA03247 2830 PPTSAQPTAPPPPPGPPPPSLPLgGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPP 2909

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   82 QPRDGEAELEPWTASGEPAPASWAPVELQVDVRVKPVGAAGASRAPSPAPSTRFLTVPVPESPAFARRSAPTLQWLPRAP 161
Cdd:PHA03247 2910 QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAP 2989

                         170
                  ....*....|....
gi 119964698  162 SPGSTWSRGSPLAA 175
Cdd:PHA03247 2990 ASSTPPLTGHSLSR 3003
PHA02867 PHA02867
C-type lectin protein; Provisional
 271-319 2.08e-03

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 38.51  E-value: 2.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119964698 271 CPQGWMWSQEQCYYLSEEAQDWEGSQAFCSAHHATLPLLSHTQ--DFLRKY 319
Cdd:PHA02867  49 CPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIEtlNFVSRY 99
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
7-172 2.37e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.22  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   7 PAEAPQP-RASEDSPRPERTGWEEPDAQPQELPEKSPSPALSGSPRVPPLSLGYGAFRRLGSCSRELPSPSPSWAEQPRD 85
Cdd:PRK07003 442 AADGDAPvPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDA 521

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698  86 GEAELEPWTASGEPAPASWAPVE------LQVDV-----------RVKPVGAAGASRAPSPA---PSTRFLTVPVPeSPA 145
Cdd:PRK07003 522 PAAAAPPAPEARPPTPAAAAPAAraggaaAALDVlrnagmrvssdRGARAAAAAKPAAAPAAapkPAAPRVAVQVP-TPR 600

                        170       180
                 ....*....|....*....|....*..
gi 119964698 146 fARRSAPTLQWLPRAPSPGSTWSRGSP 172
Cdd:PRK07003 601 -ARAATGDAPPNGAARAEQAAESRGAP 626
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 6-195 2.99e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   6 VPAEAPQPRASEDSPRPERTGWEEPDAQPQ--ELPEKSPSPALSGSPRVPPLSLGYGAFRRLGSCSRELPSPSPSWAEQP 83
Cdd:PRK07764 587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAapAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698  84 RDGEAELEPWTASGEPAPASWAPVElQVDVRVKPVGAAGASRAPSPAPSTRFLTVPVPESPAFARRSAPTLQWLPRAPSP 163
Cdd:PRK07764 667 DGWPAKAGGAAPAAPPPAPAPAAPA-APAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEP 745

                        170       180       190
                 ....*....|....*....|....*....|..
gi 119964698 164 gstwsrGSPLAANATESVSPAEGCMVPPGSPA 195
Cdd:PRK07764 746 ------DDPPDPAGAPAQPPPPPAPAPAAAPA 771
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 3-178 3.18e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 39.46  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   3 PPQVPAEAPQPRASEDSPRPERTGWEEPDAQPQElPEKSPSPALSGSPRVPPLSLGYGAFRRLGSCSRElPSPSPSWAEQ 82
Cdd:PRK07994 371 PPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPA-SAPQQAPAVPLPETTSQLLAARQQLQRAQGATKA-KKSEPAAASR 448

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698  83 PRDGEAELEPWTASGEPAPASWAPVELQVDVRVKPVGAAGASRAPSPAPS---TRFLTVPVPESPA-FARRSAPTLQWL- 157
Cdd:PRK07994 449 ARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNPVEVKKEPVATPKalkKALEHEKTPELAAkLAAEAIERDPWAa 528

                        170       180
                 ....*....|....*....|...
gi 119964698 158 --PRAPSPGSTWSrgspLAANAT 178
Cdd:PRK07994 529 lvSQLGLPGLVEQ----LALNAW 547
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 271-382 3.33e-03

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 37.17  E-value: 3.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698 271 CPQGWMWSQEQCYYLSEEAQDWEGSQAFCSAH--HATLPLLSHTQDFLRKyRITKGSWVGAR-RGPEG-WHWTDGVPLps 346
Cdd:cd03588    1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQqgHLSSIVTPEEQEFVNN-NAQDYQWIGLNdRTIEGdFRWSDGHPL-- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119964698 347 qLFPADSEDHPD--FSCG-------GLEEGRLVALDCSSPRPWVC 382
Cdd:cd03588   78 -QFENWRPNQPDnfFATGedcvvmiWHEEGEWNDVPCNYHLPFTC 121
dnaA PRK14086
chromosomal replication initiator protein DnaA;
2-185 4.96e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 39.04  E-value: 4.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   2 EPPQVPAEAPQPRASEDSPRPERTGWEEPDAQPQElpekSPSPALSGSPRVPPLSLGYGAFRRLGSCSRELPSPSPSWAE 81
Cdd:PRK14086  93 GEPAPPPPHARRTSEPELPRPGRRPYEGYGGPRAD----DRPPGLPRQDQLPTARPAYPAYQQRPEPGAWPRAADDYGWQ 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698  82 QPRDGEAELEPWTASGEPAPAS--WAPVELQVDVRVKPVGAAGASRAPSPAPSTRFLT-VPVPESPAFAR-RSAPTLQWL 157
Cdd:PRK14086 169 QQRLGFPPRAPYASPASYAPEQerDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRTdRPEPPPGAGHVhRGGPGPPER 248

                        170       180
                 ....*....|....*....|....*...
gi 119964698 158 PRAPSPGSTWSRGSPLAANATESVSPAE 185
Cdd:PRK14086 249 DDAPVVPIRPSAPGPLAAQPAPAPGPGE 276
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
3-204 5.50e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.06  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698   3 PPQVPAEAPQPRASEdsprpertgweEPDAQPQELPEKSPSPALSGSPRVPPLSLGYGAFRRLGSCSRELPSPSPSWAEQ 82
Cdd:PRK07003 373 PARVAGAVPAPGARA-----------AAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDD 441

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119964698  83 PRDGEAElepwTASGEPAPAswapvelqvdvrvkPVGAAGASRAPSPAPSTRFLTVPVPESPAFARrsaptlqWLPRAPS 162
Cdd:PRK07003 442 AADGDAP----VPAKANARA--------------SADSRCDERDAQPPADSGSASAPASDAPPDAA-------FEPAPRA 496

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 119964698 163 PGSTWSRGSPLAANATESVSPAEGCMVPPGSPACRCRCREPG 204
Cdd:PRK07003 497 AAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPA 538
 
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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