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Conserved domains on  [gi|2044175645|ref|XP_041607186|]
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killer cell lectin-like receptor subfamily G member 2 [Vulpes lagopus]

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); ...
 266-379 5.08e-25

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: 98.17  E-value: 5.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 266 CPQGWMWSEEHCYYLSTEAQAWEASQAFCSTHHATLPLLSHT--QDFLSRYPVSKHSWVGARR--GRHGWHWIDGAPVSP 341
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEeeLEFLQSQIGSSSYWIGLSRekSEKPWKWIDGSPLNN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2044175645 342 QLLPEDDEDrlDPQCGGLEEGKLVALDCASPRPWVCAK 379
Cdd:cd03593    81 LFNIRGSTK--SGNCAYLSSTGIYSEDCSTKKRWICEK 116
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
69-186 5.76e-06

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK14951:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 618  Bit Score: 48.17  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  69 QVPSPRPARLRLPPPGLGYGAFRRQASAGSEPPSPgPAAAEPVPGEPPGVWAPVElqvdVRVKSVGAAGGSRAPSPAPST 148
Cdd:PRK14951  383 RPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAP-PAAAPPAPVAAPAAAAPAA----APAAAPAAVALAPAPPAQAAP 457

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2044175645 149 RFLTVPVPESPACPRRAFPAPPLLQRPPARPERGPDAE 186
Cdd:PRK14951  458 ETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEGD 495
 
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); ...
 266-379 5.08e-25

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: 98.17  E-value: 5.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 266 CPQGWMWSEEHCYYLSTEAQAWEASQAFCSTHHATLPLLSHT--QDFLSRYPVSKHSWVGARR--GRHGWHWIDGAPVSP 341
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEeeLEFLQSQIGSSSYWIGLSRekSEKPWKWIDGSPLNN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2044175645 342 QLLPEDDEDrlDPQCGGLEEGKLVALDCASPRPWVCAK 379
Cdd:cd03593    81 LFNIRGSTK--SGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 266-377 2.17e-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: 80.34  E-value: 2.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  266 CPQGWMWSEEHCYYLSTEAQAWEASQAFCSTHHATLPLL--SHTQDFL----SRYPVSKHSWVGARRG--RHGWHWIDGA 337
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIhsEAENDFVasllKNSGSSDYYWIGLSDPdsNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2044175645  338 PVSPQLLPEDDE-DRLDPQCGGL--EEGKLVALDCASPRPWVC 377
Cdd:smart00034  81 GPVSYSNWAPGEpNNSSGDCVVLstSGGKWNDVSCTSKLPFVC 123
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 238-379 1.29e-11

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 63.60  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 238 LAVMAVFLAVSAVAIVALASRAGARCQP------CPQGWMWSEEHCYYLSTEAQAWEASQAFCSTHHATLPLLSHTQD-- 309
Cdd:PHA02642   54 IITICILITINLVPIIILMAFKSDTQEPtikyvtCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEEln 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044175645 310 FLSRYPVSKHSWVGARR--GRHGWHWIDGAPVSPQLLPEDDEdrldpQCGGLEEGKLVALDCASPRPWVCAK 379
Cdd:PHA02642  134 FLKRYKDSSDHWIGLNResSNHPWKWADNSNYNASFVITGTG-----ECAYLNDIRISSSRVYANRKWICSK 200
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 287-377 2.78e-10

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 57.10  E-value: 2.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 287 WEASQAFCSTHHATLPLL--SHTQDFLS--RYPVSKHSWVG-ARRGR-HGWHWIDGAPVSP-QLLPEDDEDRLDPQCGGL 359
Cdd:pfam00059   4 WDEAREACRKLGGHLVSInsAEELDFLSstLKKSNKYFWIGlTDRKNeGTWKWVDGSPVNYtNWAPEPNNNGENEDCVEL 83

                          90       100
                  ....*....|....*....|
gi 2044175645 360 EE--GKLVALDCASPRPWVC 377
Cdd:pfam00059  84 SSssGKWNDENCNSKNPFVC 103
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 69-186 5.76e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 48.17  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  69 QVPSPRPARLRLPPPGLGYGAFRRQASAGSEPPSPgPAAAEPVPGEPPGVWAPVElqvdVRVKSVGAAGGSRAPSPAPST 148
Cdd:PRK14951  383 RPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAP-PAAAPPAPVAAPAAAAPAA----APAAAPAAVALAPAPPAQAAP 457

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2044175645 149 RFLTVPVPESPACPRRAFPAPPLLQRPPARPERGPDAE 186
Cdd:PRK14951  458 ETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEGD 495
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 71-262 3.94e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 39.47  E-value: 3.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645   71 PSPRPARLRLPPPglgygAFRRQASAGSEPPSPGPAAAEPVPGEPPGVWAPVELQVDVRVKSVGAAGGSRAPSPAPSTRF 150
Cdd:COG3321    854 PGRGRRRVPLPTY-----PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAA 928

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  151 LTVPVPESPACPRRAFPAPPLLQRPPARPERGPDAEPPGAPPGRGRCREPGPRGKEDAALLPGADQKLPRAVELVGLPMY 230
Cdd:COG3321    929 LLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAA 1008

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2044175645  231 MKSLRWALAVMAVFLAVSAVAIVALASRAGAR 262
Cdd:COG3321   1009 ALLLAAAAAAAALLALAALLAAAAAALAAAAA 1040
 
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); ...
 266-379 5.08e-25

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: 98.17  E-value: 5.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 266 CPQGWMWSEEHCYYLSTEAQAWEASQAFCSTHHATLPLLSHT--QDFLSRYPVSKHSWVGARR--GRHGWHWIDGAPVSP 341
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEeeLEFLQSQIGSSSYWIGLSRekSEKPWKWIDGSPLNN 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2044175645 342 QLLPEDDEDrlDPQCGGLEEGKLVALDCASPRPWVCAK 379
Cdd:cd03593    81 LFNIRGSTK--SGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 266-377 2.17e-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: 80.34  E-value: 2.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  266 CPQGWMWSEEHCYYLSTEAQAWEASQAFCSTHHATLPLL--SHTQDFL----SRYPVSKHSWVGARRG--RHGWHWIDGA 337
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIhsEAENDFVasllKNSGSSDYYWIGLSDPdsNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2044175645  338 PVSPQLLPEDDE-DRLDPQCGGL--EEGKLVALDCASPRPWVC 377
Cdd:smart00034  81 GPVSYSNWAPGEpNNSSGDCVVLstSGGKWNDVSCTSKLPFVC 123
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 276-379 4.93e-12

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: 62.25  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 276 HCYYLSTEAQAWEASQAFCSTHHATlpLLS-HT---QDFLSRY---PVSKHSWVGARR--GRHGWHWIDGAPVSPQLLPE 346
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGH--LASiHSeeeNDFLASLlkkSSSSDVWIGLNDlsSEGTWKWSDGSPLVDYTNWA 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2044175645 347 DDE--DRLDPQCGGL---EEGKLVALDCASPRPWVCAK 379
Cdd:cd00037    79 PGEpnPGGSEDCVVLsssSDGKWNDVSCSSKLPFICEK 116
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 238-379 1.29e-11

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 63.60  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 238 LAVMAVFLAVSAVAIVALASRAGARCQP------CPQGWMWSEEHCYYLSTEAQAWEASQAFCSTHHATLPLLSHTQD-- 309
Cdd:PHA02642   54 IITICILITINLVPIIILMAFKSDTQEPtikyvtCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEEln 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044175645 310 FLSRYPVSKHSWVGARR--GRHGWHWIDGAPVSPQLLPEDDEdrldpQCGGLEEGKLVALDCASPRPWVCAK 379
Cdd:PHA02642  134 FLKRYKDSSDHWIGLNResSNHPWKWADNSNYNASFVITGTG-----ECAYLNDIRISSSRVYANRKWICSK 200
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 266-341 2.53e-11

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: 60.40  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 266 CPQGWMWSEEHCYYLSTEAQAWEASQAFCSTHHATLPLLsHT---QDFLSRY-PVSKHSWVGAR-RGRHG-WHWIDGAPV 339
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVII-NSqeeQEFISKIlSGNRSYWIGLSdEETEGeWKWVDGTPL 79


                  ..
gi 2044175645 340 SP 341
Cdd:cd03590    80 NS 81
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 287-377 2.78e-10

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 57.10  E-value: 2.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 287 WEASQAFCSTHHATLPLL--SHTQDFLS--RYPVSKHSWVG-ARRGR-HGWHWIDGAPVSP-QLLPEDDEDRLDPQCGGL 359
Cdd:pfam00059   4 WDEAREACRKLGGHLVSInsAEELDFLSstLKKSNKYFWIGlTDRKNeGTWKWVDGSPVNYtNWAPEPNNNGENEDCVEL 83

                          90       100
                  ....*....|....*....|
gi 2044175645 360 EE--GKLVALDCASPRPWVC 377
Cdd:pfam00059  84 SSssGKWNDENCNSKNPFVC 103
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 278-377 9.09e-08

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: 50.06  E-value: 9.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 278 YYLSTEAQAWEASQAFCSTHHATLPLLSHTQDFLSRYPVSKHS----WVGARRGRHGWHWIDGAPVSP----QLLPEDDE 349
Cdd:cd03602     3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSnsaaWIGLYRDVDSWRWSDGSESSFrnwnTFQPFGQG 82

                          90       100
                  ....*....|....*....|....*....
gi 2044175645 350 DrldpqCGGLE-EGKLVALDCASPRPWVC 377
Cdd:cd03602    83 D-----CATMYsSGRWYAALCSALKPFIC 106
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 69-186 5.76e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 48.17  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  69 QVPSPRPARLRLPPPGLGYGAFRRQASAGSEPPSPgPAAAEPVPGEPPGVWAPVElqvdVRVKSVGAAGGSRAPSPAPST 148
Cdd:PRK14951  383 RPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAP-PAAAPPAPVAAPAAAAPAA----APAAAPAAVALAPAPPAQAAP 457

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2044175645 149 RFLTVPVPESPACPRRAFPAPPLLQRPPARPERGPDAE 186
Cdd:PRK14951  458 ETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEGD 495
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 266-337 1.77e-05

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: 43.90  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 266 CPQGWMWSEEHCYYLSTEAQAWEASQAFCSTHHATLPLLS-HTQ---DFLSRYPVSKHS-----WVGARR--GRHGWHWI 334
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYGPGAHLASiHSPaeaAAIASLISSYQKayqpvWIGLHDpqQSRGWEWS 80


                  ...
gi 2044175645 335 DGA 337
Cdd:cd03594    81 DGS 83
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 76-216 1.58e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  76 ARLRLPPPGLGYGAfrrqASAGSEPPSPGPAAAEPVPGEPPGVWAPVelqvdvrvkSVGAAGGSRAPSPAPSTRFLTVPV 155
Cdd:PRK07764  376 ARLERLERRLGVAG----GAGAPAAAAPSAAAAAPAAAPAPAAAAPA---------AAAAPAPAAAPQPAPAPAPAPAPP 442

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2044175645 156 PESPACPRRAFPAPPLLQRPPARPERGP-DAEPPGAPPGRGRCREPGPRGKEDAALLPGADQ 216
Cdd:PRK07764  443 SPAGNAPAGGAPSPPPAAAPSAQPAPAPaAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPA 504
PHA03247 PHA03247
large tegument protein UL36; Provisional
 21-220 1.65e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645   21 PLGRQVPGPEPPQVPAEERRPDSPESSPSPARAARQAAGAAQDLSggKQVPSPRPARLRLPPPGlgygafrrQASAGSEP 100
Cdd:PHA03247  2569 PPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAP--PSPLPPDTHAPDPPPPS--------PSPAANEP 2638

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  101 PSPGPAAAePVPGEPPGVWAPVELQVDVRVKSVGAAGGSRAPSPAPSTRFLTVPVPESPACPRRafPAPPLLQRPPARPE 180
Cdd:PHA03247  2639 DPHPPPTV-PPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADP--PPPPPTPEPAPHAL 2715

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2044175645  181 RGPDAEPPGAPPGRGRC----REPGPRGKEDAALLPGADQKLPR 220
Cdd:PHA03247  2716 VSATPLPPGPAAARQASpalpAAPAPPAVPAGPATPGGPARPAR 2759
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
27-192 3.03e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.94  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  27 PGPEPPQVPAEERRPDSPESSPSPARAARQAAGAAQDLSGGKQVPSPRPARLRLPPPGLGYGAFRRQASAGSEPPSPGPA 106
Cdd:PRK12323  406 PAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAP 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 107 AAEPVP---GEPPGVWAPVELQVDVRVKSVGA-AGGSRAPSPAPSTRFLTVPVPESPACPRRAFPAPPLLQRPPARPERG 182
Cdd:PRK12323  486 AAAPAPaddDPPPWEELPPEFASPAPAQPDAApAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRP 565

                         170
                  ....*....|
gi 2044175645 183 PDAEPPGAPP 192
Cdd:PRK12323  566 PRASASGLPD 575
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 18-210 3.62e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  18 PMEPLGRQVPGPEPPQVPAEERRPDSPESSPSPARAARQAagaaqdlSGGKQVPSPRPARLRLPPPGLGYGAFRRQASAG 97
Cdd:PRK07764  602 APASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASA-------APAPGVAAPEHHPKHVAVPDASDGGDGWPAKAG 674

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  98 SEPPSPGPAAAEPVPGEPPGVWAPVELQVDVRVKSVGAAGGSRAPSPAPSTRfLTVPVPESPACPRRAFPAPPLLQRPPA 177
Cdd:PRK07764  675 GAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQ-GASAPSPAADDPVPLPPEPDDPPDPAG 753

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2044175645 178 RPERGPDAEPPGAPPGRGRCREPGPRGKEDAAL 210
Cdd:PRK07764  754 APAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMA 786
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 73-202 4.11e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 42.36  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  73 PRPARLRLPPPGLGYGAfrrqASAGSEPPSPGPAAAEPVPgePPGVWAPVELQVDVRVKSVGAAGGSRAPSPAPSTRflt 152
Cdd:PRK14959  363 PRLMPVESLRPSGGGAS----APSGSAAEGPASGGAATIP--TPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSPR--- 433

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2044175645 153 VPVPESPACPRR----AFPAPPLLQRPPARPERGPDAEPPGAPPGRGRCREPGP 202
Cdd:PRK14959  434 VPWDDAPPAPPRsgipPRPAPRMPEASPVPGAPDSVASASDAPPTLGDPSDTAE 487
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
69-188 6.51e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.79  E-value: 6.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  69 QVPSPRPARLRLPPPglgygafrrqASAGSEPPSPGPAAAEPVPGEPPGVWAPVELQVDVRVKSVGAAGGSRAPSPAPST 148
Cdd:PRK12323  393 AAAAPAPAAPPAAPA----------AAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAA 462

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2044175645 149 RfltvPVPESPACPRRAFPAPPLLQRPPARPERGPDAEPP 188
Cdd:PRK12323  463 R----PAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPP 498
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 266-380 8.85e-04

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: 39.10  E-value: 8.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 266 CPQGWMWSEEHCYYLSTEAQAWEASQAFCSTH--HATLPLLSHTQDFLSRYpVSKHSWVGA--RRGRHGWHWIDGAPVSP 341
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQqgHLSSIVTPEEQEFVNNN-AQDYQWIGLndRTIEGDFRWSDGHPLQF 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2044175645 342 QLLPEDDEDRL---DPQCG---GLEEGKLVALDCASPRPWVCAKG 380
Cdd:cd03588    80 ENWRPNQPDNFfatGEDCVvmiWHEEGEWNDVPCNYHLPFTCKKG 124
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 27-227 1.25e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  27 PGPEPPQVPAEERRPDSPESSPSPARAARQAAGAAQDLSGGKQVPSPRPARLRLPPPGLGYGAFRRQASAGSEPPSPGPA 106
Cdd:PRK07764  622 AAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQP 701

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 107 AAEPVPGEPPGVWAPVELQvdvrvksvgAAGGSRAPSPAPSTRFLTVPVPESPacprrafPAPPLLQRPPARPERGPDAE 186
Cdd:PRK07764  702 APAPAATPPAGQADDPAAQ---------PPQAAQGASAPSPAADDPVPLPPEP-------DDPPDPAGAPAQPPPPPAPA 765

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2044175645 187 PPGAPPGRGRCREPGPRGKEDAALLPGADQKLPRAVELVGL 227
Cdd:PRK07764  766 PAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAM 806
PRK14965 PRK14965
DNA polymerase III subunits gamma and tau; Provisional
 139-225 1.40e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237871 [Multi-domain]  Cd Length: 576  Bit Score: 40.50  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 139 SRAPSPAPSTRFLTVPVPESPACPRRAFPAPPLLQRPPArpERGPDAEPPGAPPgrgrcrEPGPRGKEDAALLPGADQKL 218
Cdd:PRK14965  379 RGAPAPPSAAWGAPTPAAPAAPPPAAAPPVPPAAPARPA--AARPAPAPAPPAA------AAPPARSADPAAAASAGDRW 450


                  ....*..
gi 2044175645 219 PRAVELV 225
Cdd:PRK14965  451 RAFVAFV 457
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
23-221 1.89e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.22  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  23 GRQVPGPEPPQVPAEERRPDSPESSPSPARAARQAAGAAQDLSggKQVPSPRPARLRLPPPGlgyGAFRRQASAGSEPPS 102
Cdd:PRK07003  369 GGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALA--PKAAAAAAATRAEAPPA---APAPPATADRGDDAA 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 103 PGPAAAePVPGEPPGvwapvelqvdvrvkSVGAAGGSRAPSPAPSTRFLTVPVPESPACPRRAfPAPPLLQRPPARPERG 182
Cdd:PRK07003  444 DGDAPV-PAKANARA--------------SADSRCDERDAQPPADSGSASAPASDAPPDAAFE-PAPRAAAPSAATPAAV 507

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2044175645 183 PDAEPPGAPPGRGRCREPGPRGKEDAALLPGADQKLPRA 221
Cdd:PRK07003  508 PDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARA 546
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 89-202 2.76e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 39.70  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  89 AFRRQASAGS------EPPSPGPAAAEPVPGEPPGVWAPVELQVDVRVKSVGAAGGSRAPSPAPSTRFLTVPVPESPACP 162
Cdd:PRK14951  363 AFKPAAAAEAaapaekKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAP 442

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2044175645 163 RRAFPAPPLLQRPPARPERGP-DAEPPGAPPGRGRCREPGP 202
Cdd:PRK14951  443 AAVALAPAPPAQAAPETVAIPvRVAPEPAVASAAPAPAAAP 483
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
89-221 3.06e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.47  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  89 AFRRQASAGSEPPSpgPAAAEPVPGEPPGVWAPvelqvdvrvkSVGAAGGSRAPSPAPSTRFLTVPVPESPACPRRAFPA 168
Cdd:PRK12323  362 AFRPGQSGGGAGPA--TAAAAPVAQPAPAAAAP----------AAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPA 429

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2044175645 169 PPLL----QRPPARP--ERGPDAEPPGAPPGRGRCREPGPRGKEDAALLPGADQKLPRA 221
Cdd:PRK12323  430 PEALaaarQASARGPggAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAA 488
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 70-223 3.43e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 39.46  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  70 VPSPRPARLRLPPPGlgygafrrqasAGSEPPSPGPAAAEPVPGEPPGVWAPVELQVDVRVKSVGAAGGSRAPSPAPSTR 149
Cdd:PRK07994  365 LPEPEVPPQSAAPAA-----------SAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQ 433

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044175645 150 FLTVPVPESPACPRRAFPAPPLLQRPPARPERGPDAEPPGAPPGRGRCREPGPrgkEDAALLPGADQK-LPRAVE 223
Cdd:PRK07994  434 GATKAKKSEPAAASRARPVNSALERLASVRPAPSALEKAPAKKEAYRWKATNP---VEVKKEPVATPKaLKKALE 505
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 71-262 3.94e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 39.47  E-value: 3.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645   71 PSPRPARLRLPPPglgygAFRRQASAGSEPPSPGPAAAEPVPGEPPGVWAPVELQVDVRVKSVGAAGGSRAPSPAPSTRF 150
Cdd:COG3321    854 PGRGRRRVPLPTY-----PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAA 928

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  151 LTVPVPESPACPRRAFPAPPLLQRPPARPERGPDAEPPGAPPGRGRCREPGPRGKEDAALLPGADQKLPRAVELVGLPMY 230
Cdd:COG3321    929 LLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAA 1008

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2044175645  231 MKSLRWALAVMAVFLAVSAVAIVALASRAGAR 262
Cdd:COG3321   1009 ALLLAAAAAAAALLALAALLAAAAAALAAAAA 1040
PTZ00429 PTZ00429
beta-adaptin; Provisional
 74-202 7.23e-03

beta-adaptin; Provisional


Pssm-ID: 240415 [Multi-domain]  Cd Length: 746  Bit Score: 38.37  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  74 RPARLRLPPPGLGYGAFRRQ------ASAGSEPPSPGPAAAEPVPGEPPGVWAPVELQVDVRVKSVGAAGGSRAPSPAPS 147
Cdd:PTZ00429  592 RPYQSFLPPYGLADVELDEEdtedddAVELPSTPSMGTQDGSPAPSAAPAGYDIFEFAGDGTGAPHPVASGSNGAQHADP 671

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2044175645 148 TRFLTVPVPESPACPRRAFPAPPLLQRPPARPERGPDAEP-PGAPPGRGRCREPGP 202
Cdd:PTZ00429  672 LGDLFSGLPSTVGASSPAFQAASGSQAPASPPTAASAIEDlFANGMGSGSQTVPLP 727
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
24-230 7.68e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 38.32  E-value: 7.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  24 RQVPGPEPPQVPAEERRPDSPESSPSPARAARQAAGAAQDLSGGKQVPSPR-PARLRLPPPGLGYGAFRRQASAGSEPPS 102
Cdd:PRK12323  376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRsPAPEALAAARQASARGPGGAPAPAPAPA 455

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645 103 PGPAAAEPVPGEPPGVWAPVELQVDVRvksvgaAGGSRAPSPAPSTRFLTVPVPESPACPRRAFPAPPLLQRPPARPERG 182
Cdd:PRK12323  456 AAPAAAARPAAAGPRPVAAAAAAAPAR------AAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDP 529

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2044175645 183 PDAEPPGAPPGRGRCREPGPRGKEDAALLPGADQKLPRAVELVGLPMY 230
Cdd:PRK12323  530 ATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMF 577
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 65-214 8.40e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 38.23  E-value: 8.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645   65 SGGKQVPSPRPARLRLPPPGLGYGAFRRQASAGSEPPSPGPAAAEPVPGEPPGvwAPVELQVDVRVKSVGAAGGSRAPSP 144
Cdd:PHA03307    92 LSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSP--GPPPAASPPAAGASPAAVASDAASS 169

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645  145 APSTRFLTVPvPESPACPRRAFPAPPLLQRPPARPERGPDAEPPGAPPGrgrcREPGPRGKEDAALLPGA 214
Cdd:PHA03307   170 RQAALPLSSP-EETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASA----SSPAPAPGRSAADDAGA 234
PHA03247 PHA03247
large tegument protein UL36; Provisional
 18-221 9.86e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.38  E-value: 9.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645   18 PMEPLGRQVPGPEPPQVPAEERRPDSPESSPSPARAARQAAGAAQDLSGGKQVPSPRPARLRLPppglgygafrRQASAG 97
Cdd:PHA03247  2601 PVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRP----------RRARRL 2670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044175645   98 SEPPSPGPAAAEPVPGEPPGVWAPVELQVDvrvksvgAAGGSRAPSPAPSTRFLTVPVPESPACPRRAFPAPPLLQRPPA 177
Cdd:PHA03247  2671 GRAAQASSPPQRPRRRAARPTVGSLTSLAD-------PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2044175645  178 RPErGPDAEPPGAPPGRGRCREPGPRGKEDAALLPGADQKLPRA 221
Cdd:PHA03247  2744 VPA-GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRP 2786
 
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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