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Genome polyprotein

 B1PNU8_9FLAV            Unreviewed;      3391 AA.
B1PNU8;
29-APR-2008, integrated into UniProtKB/TrEMBL.
29-APR-2008, sequence version 1.
13-FEB-2019, entry version 96.
RecName: Full=Genome polyprotein {ECO:0000256|SAAS:SAAS00368684};
Dengue virus 2.
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Flaviviridae; Flavivirus.
NCBI_TaxID=11060 {ECO:0000313|EMBL:ACA48864.1, ECO:0000313|Proteomes:UP000150062};
[1] {ECO:0000313|EMBL:ACA48864.1, ECO:0000313|Proteomes:UP000137806, ECO:0000313|Proteomes:UP000150062}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DENV-2/NI/BID-V609/2005 {ECO:0000313|EMBL:ACA48864.1}, and
DENV-2/NI/BID-V623/2005 {ECO:0000313|EMBL:ACA48867.1};
Broad Institute Genome Sequencing Platform;
Broad Institute Microbial Sequencing Center;
Genome Resources in Dengue Consortium;
Henn M.R., Balmaseda A., Young S., Kodira C., Koehrsen M., Jaffe D.,
Young S., Berlin A., Heiman D., Hepburn T., Sykes S., Borenstein D.,
Crawford M., Engels R., Freedman E., Howarth C., Jen D., Larson L.,
Ledlie T., Lewis B., Montgomery P., Park D., Pearson M., Roberts A.,
Sisk P., Stolte C., White J., Zeng Q., Yandava C., Oleary S.,
Alvarado L., Alvarez P., Brockman W., Butler J., Gnerre S.,
Grabherr M., Kleber M., Mauceli E., MacCallum I., Gomez T., Nunez A.,
Castillo P., Lander E., Galagan J., Nusbaum C., Harris E., Birren B.;
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:ACA49037.1, ECO:0000313|Proteomes:UP000124350}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DENV-2/NI/BID-V527/2005 {ECO:0000313|EMBL:ACA49037.1};
Broad Institute Genome Sequencing Platform;
Broad Institute Microbial Sequencing Center;
Genome Resources in Dengue Consortium;
Henn M.R., Balmaseda A., Young S., Kodira C., Koehrsen M., Jaffe D.,
Young S., Berlin A., Heiman D., Hepburn T., Sykes S., Borenstein D.,
Crawford M., Engels R., Freedman E., Howarth C., Jen D., Larson L.,
Ledlie T., Lewis B., Montgomery P., Park D., Pearson M., Roberts A.,
Sisk P., Stolte C., White J., Zeng Q., Yandava C., Oleary S.,
Alvarado L., Alvarez P., Brockman W., Butler J., Gnerre S.,
Grabherr M., Kleber M., Mauceli E., MacCallum I., Gomez T., Nunez A.,
Garcia O., Lander E., Galagan J., Nusbaum C., Harris E., Birren B.;
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|Proteomes:UP000117646, ECO:0000313|Proteomes:UP000120869, ECO:0000313|Proteomes:UP000130400}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DENV-2/NI/BID-V620/2005 {ECO:0000313|EMBL:ACA48899.1},
DENV-2/NI/BID-V631/2006 {ECO:0000313|EMBL:ACA48900.1},
DENV-2/NI/BID-V654/2005 {ECO:0000313|EMBL:ACA48903.1}, and
DENV-2/NI/BID-V658/2005 {ECO:0000313|EMBL:ACA48904.1};
Broad Institute Genome Sequencing Platform;
Broad Institute Microbial Sequencing Center;
Genome Resources in Dengue Consortium;
Henn M.R., Balmaseda A., Young S., Kodira C., Koehrsen M., Jaffe D.,
Young S., Berlin A., Heiman D., Hepburn T., Sykes S., Borenstein D.,
Crawford M., Engels R., Freedman E., Howarth C., Jen D., Larson L.,
Ledlie T., Lewis B., Montgomery P., Park D., Pearson M., Roberts A.,
Sisk P., Stolte C., White J., Zeng Q., Yandava C., Oleary S.,
Alvarado L., Alvarez P., Brockman W., Butler J., Gnerre S.,
Grabherr M., Kleber M., Mauceli E., MacCallum I., Gomez T., Nunez A.,
Jiron L., Lander E., Galagan J., Nusbaum C., Harris E., Birren B.;
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:ACA49025.1, ECO:0000313|Proteomes:UP000158831}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DENV-2/NI/BID-V539/2005 {ECO:0000313|EMBL:ACA49025.1};
Broad Institute Genome Sequencing Platform;
Broad Institute Microbial Sequencing Center;
Genome Resources in Dengue Consortium;
Henn M.R., Balmaseda A., Young S., Kodira C., Koehrsen M., Jaffe D.,
Young S., Berlin A., Heiman D., Hepburn T., Sykes S., Borenstein D.,
Crawford M., Engels R., Freedman E., Howarth C., Jen D., Larson L.,
Ledlie T., Lewis B., Montgomery P., Park D., Pearson M., Roberts A.,
Sisk P., Stolte C., White J., Zeng Q., Yandava C., Oleary S.,
Alvarado L., Alvarez P., Brockman W., Butler J., Gnerre S.,
Grabherr M., Kleber M., Mauceli E., MacCallum I., Gomez T., Nunez A.,
Silva J., Lander E., Galagan J., Nusbaum C., Harris E., Birren B.;
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|EMBL:ACB87125.1, ECO:0000313|Proteomes:UP000108715}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DENV-2/NI/BID-V660/2005 {ECO:0000313|EMBL:ACB87125.1};
Broad Institute Genome Sequencing Platform;
Broad Institute Microbial Sequencing Center;
Genome Resources in Dengue Consortium;
Henn M.R., Balmaseda A., Young S., Kodira C., Koehrsen M., Jaffe D.,
Berlin A., Heiman D., Hepburn T., Sykes S., Borenstein D., Engels R.,
Freedman E., Howarth C., Jen D., Larson L., Lewis B., Montgomery P.,
Park D., Pearson M., Roberts A., Sisk P., Stolte C., White J.,
Zeng Q., Yandava C., Oleary S., Alvarado L., Alvarez P., Brockman W.,
Butler J., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
MacCallum I., Gomez T., Nunez A., Perez C., Lander E., Galagan J.,
Nusbaum C., Harris E., Birren B.;
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|EMBL:ACO06177.1, ECO:0000313|Proteomes:UP000167746}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DENV-2/NI/BID-V634/2005 {ECO:0000313|EMBL:ACO06177.1};
Broad Institute Genome Sequencing Platform;
Broad Institute Microbial Sequencing Center;
Genome Resources in Dengue Consortium;
Henn M.R., Balmaseda A., Young S., Kodira C., Koehrsen M., Jaffe D.,
Berlin A., Heiman D., Hepburn T., Sykes S., Borenstein D., Engels R.,
Freedman E., Howarth C., Jen D., Larson L., Lewis B., Montgomery P.,
Park D., Pearson M., Roberts A., Sisk P., Stolte C., White J.,
Zeng Q., Yandava C., Oleary S., Alvarado L., Alvarez P., Brockman W.,
Butler J., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
MacCallum I., Gomez T., Nunez A., Perez C., Lander E., Galagan J.,
Nusbaum C., Harris E., Birren B.;
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000313|EMBL:ACQ44474.1, ECO:0000313|Proteomes:UP000170712}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DENV-2/NI/BID-V648/2005 {ECO:0000313|EMBL:ACQ44474.1};
Broad Institute Genome Sequencing Platform;
Broad Institute Microbial Sequencing Center;
Genome Resources in Dengue Consortium;
Henn M.R., Balmaseda A., Young S., Koehrsen M., Jaffe D., Lennon N.,
Erlich R., Anderson S., Rizzolo K., Green L., Ryan E., Yu Q.,
Berlin A., Heiman D., Hepburn T., Sykes S., Borenstein D., Engels R.,
Freedman E., Gellesch M., Heilman E., Howarth C., Jen D., Larson L.,
Lewis B., Montgomery P., Park D., Pearson M., Richards J., Roberts A.,
Sisk P., Stolte C., White J., Alvarado L., Champion M., Godfrey P.,
Shenoy N., Yandava C., Zeng Q., Alvarez P., Brockman W., Butler J.,
Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I., Gomez T.,
Nunez A., Nusbaum C., Harris E., Birren B.;
Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
Evidence={ECO:0000256|SAAS:SAAS01122357};
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside
5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
Evidence={ECO:0000256|SAAS:SAAS01122355};
-!- CATALYTIC ACTIVITY:
Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
ChEBI:CHEBI:83400; EC=2.7.7.48;
Evidence={ECO:0000256|SAAS:SAAS01133029};
-!- SUBCELLULAR LOCATION: Host endoplasmic reticulum
{ECO:0000256|SAAS:SAAS00941764}. Virion membrane
{ECO:0000256|SAAS:SAAS00980400}; Multi-pass membrane protein
{ECO:0000256|SAAS:SAAS00980400}.
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EMBL; EU482597; ACA48864.1; -; Genomic_RNA.
EMBL; EU482600; ACA48867.1; -; Genomic_RNA.
EMBL; EU482632; ACA48899.1; -; Genomic_RNA.
EMBL; EU482633; ACA48900.1; -; Genomic_RNA.
EMBL; EU482636; ACA48903.1; -; Genomic_RNA.
EMBL; EU482637; ACA48904.1; -; Genomic_RNA.
EMBL; EU482758; ACA49025.1; -; Genomic_RNA.
EMBL; EU482770; ACA49037.1; -; Genomic_RNA.
EMBL; EU596484; ACB87125.1; -; Genomic_RNA.
EMBL; FJ850115; ACO06177.1; -; Genomic_RNA.
EMBL; FJ898435; ACQ44474.1; -; Genomic_RNA.
MEROPS; S07.001; -.
Proteomes; UP000108715; Genome.
Proteomes; UP000117646; Genome.
Proteomes; UP000120869; Genome.
Proteomes; UP000124350; Genome.
Proteomes; UP000130400; Genome.
Proteomes; UP000135315; Genome.
Proteomes; UP000137806; Genome.
Proteomes; UP000150062; Genome.
Proteomes; UP000158831; Genome.
Proteomes; UP000167746; Genome.
Proteomes; UP000170712; Genome.
GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:InterPro.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:InterPro.
GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:InterPro.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd12149; Flavi_E_C; 1.
Gene3D; 1.10.10.930; -; 1.
Gene3D; 1.10.8.970; -; 1.
Gene3D; 1.20.1280.260; -; 1.
Gene3D; 2.60.260.50; -; 1.
Gene3D; 2.60.40.350; -; 1.
Gene3D; 2.60.98.10; -; 1.
Gene3D; 3.30.387.10; -; 1.
Gene3D; 3.30.67.10; -; 1.
InterPro; IPR011492; DEAD_Flavivir.
InterPro; IPR000069; Env_glycoprot_M_flavivir.
InterPro; IPR038302; Env_glycoprot_M_sf_flavivir.
InterPro; IPR013755; Flav_gly_cen_dom_subdom1.
InterPro; IPR001122; Flavi_capsidC.
InterPro; IPR037172; Flavi_capsidC_sf.
InterPro; IPR027287; Flavi_E_Ig-like.
InterPro; IPR026470; Flavi_E_Stem/Anchor_dom.
InterPro; IPR038345; Flavi_E_Stem/Anchor_dom_sf.
InterPro; IPR001157; Flavi_NS1.
InterPro; IPR000752; Flavi_NS2A.
InterPro; IPR000487; Flavi_NS2B.
InterPro; IPR000404; Flavi_NS4A.
InterPro; IPR001528; Flavi_NS4B.
InterPro; IPR002535; Flavi_propep.
InterPro; IPR038688; Flavi_propep_sf.
InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
InterPro; IPR001850; Flavivirus_NS3_S7.
InterPro; IPR014412; Gen_Poly_FLV.
InterPro; IPR011998; Glycoprot_cen/dimer.
InterPro; IPR036253; Glycoprot_cen/dimer_sf.
InterPro; IPR038055; Glycoprot_E_dimer_dom.
InterPro; IPR013756; GlyE_cen_dom_subdom2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR026490; mRNA_cap_0/1_MeTrfase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR000208; RNA-dir_pol_flavivirus.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF01003; Flavi_capsid; 1.
Pfam; PF07652; Flavi_DEAD; 1.
Pfam; PF02832; Flavi_glycop_C; 1.
Pfam; PF00869; Flavi_glycoprot; 1.
Pfam; PF01004; Flavi_M; 1.
Pfam; PF00948; Flavi_NS1; 1.
Pfam; PF01005; Flavi_NS2A; 1.
Pfam; PF01002; Flavi_NS2B; 1.
Pfam; PF01350; Flavi_NS4A; 1.
Pfam; PF01349; Flavi_NS4B; 1.
Pfam; PF00972; Flavi_NS5; 1.
Pfam; PF01570; Flavi_propep; 1.
Pfam; PF01728; FtsJ; 1.
Pfam; PF00949; Peptidase_S7; 1.
PIRSF; PIRSF003817; Gen_Poly_FLV; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF101257; SSF101257; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF56983; SSF56983; 1.
SUPFAM; SSF81296; SSF81296; 1.
TIGRFAMs; TIGR04240; flavi_E_stem; 1.
PROSITE; PS51527; FLAVIVIRUS_NS2B; 1.
PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51591; RNA_CAP01_NS5_MT; 1.
4: Predicted;
Activation of host autophagy by virus {ECO:0000256|SAAS:SAAS00445756};
ATP-binding {ECO:0000256|SAAS:SAAS01124208};
Capsid protein {ECO:0000256|SAAS:SAAS00969288};
Complete proteome {ECO:0000313|Proteomes:UP000108715,
ECO:0000313|Proteomes:UP000117646, ECO:0000313|Proteomes:UP000120869,
ECO:0000313|Proteomes:UP000124350};
Disulfide bond {ECO:0000256|PIRSR:PIRSR003817-3,
ECO:0000256|SAAS:SAAS00139753};
Fusion of virus membrane with host endosomal membrane
{ECO:0000256|SAAS:SAAS00489633};
Fusion of virus membrane with host membrane
{ECO:0000256|SAAS:SAAS00489633};
Helicase {ECO:0000256|SAAS:SAAS01124208};
Host membrane {ECO:0000256|SAAS:SAAS00445977};
Host-virus interaction {ECO:0000256|SAAS:SAAS00445756,
ECO:0000256|SAAS:SAAS00445995, ECO:0000256|SAAS:SAAS00941647};
Hydrolase {ECO:0000256|SAAS:SAAS01124208};
Inhibition of host innate immune response by virus
{ECO:0000256|SAAS:SAAS00941647};
Membrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAAS:SAAS00445977, ECO:0000256|SAM:Phobius};
Metal-binding {ECO:0000256|PIRSR:PIRSR003817-4,
ECO:0000256|SAAS:SAAS00940329};
Methyltransferase {ECO:0000256|SAAS:SAAS00817755};
mRNA capping {ECO:0000256|SAAS:SAAS00075918};
mRNA processing {ECO:0000256|SAAS:SAAS00075918};
Nucleotide-binding {ECO:0000256|SAAS:SAAS01124208};
Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00076304};
RNA-binding {ECO:0000256|SAAS:SAAS00076745};
RNA-directed RNA polymerase {ECO:0000256|SAAS:SAAS00076304};
S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00076715};
Transferase {ECO:0000256|SAAS:SAAS00076304,
ECO:0000256|SAAS:SAAS00817755};
Transmembrane {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00445939,
ECO:0000256|SAM:Phobius};
Viral attachment to host cell {ECO:0000256|SAAS:SAAS00445995};
Viral immunoevasion {ECO:0000256|SAAS:SAAS00941647};
Viral penetration into host cytoplasm {ECO:0000256|SAAS:SAAS00489633};
Viral RNA replication {ECO:0000256|SAAS:SAAS01123964};
Virion {ECO:0000256|SAAS:SAAS00445995, ECO:0000256|SAAS:SAAS00969288};
Virus entry into host cell {ECO:0000256|SAAS:SAAS00445995,
ECO:0000256|SAAS:SAAS00489633};
Zinc {ECO:0000256|PIRSR:PIRSR003817-4}.
TRANSMEM 722 748 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 754 773 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 1159 1177 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2148 2167 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2174 2191 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2197 2214 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 2226 2243 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 1346 1475 FLAVIVIRUS_NS2B.
{ECO:0000259|PROSITE:PS51527}.
DOMAIN 1476 1653 Peptidase S7.
{ECO:0000259|PROSITE:PS51528}.
DOMAIN 1655 1811 Helicase ATP-binding.
{ECO:0000259|PROSITE:PS51192}.
DOMAIN 1821 1988 Helicase C-terminal.
{ECO:0000259|PROSITE:PS51194}.
DOMAIN 2493 2755 MRNA cap 0-1 NS5-type MT.
{ECO:0000259|PROSITE:PS51591}.
DOMAIN 3019 3168 RdRp catalytic.
{ECO:0000259|PROSITE:PS50507}.
ACT_SITE 1526 1526 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1550 1550 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
ACT_SITE 1610 1610 Charge relay system; for serine protease
NS3 activity.
{ECO:0000256|PIRSR:PIRSR003817-1}.
METAL 2929 2929 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 2933 2933 Zinc 1; via tele nitrogen.
{ECO:0000256|PIRSR:PIRSR003817-4}.
METAL 2938 2938 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 2941 2941 Zinc 1. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 3203 3203 Zinc 2; via tele nitrogen.
{ECO:0000256|PIRSR:PIRSR003817-4}.
METAL 3219 3219 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
4}.
METAL 3338 3338 Zinc 2. {ECO:0000256|PIRSR:PIRSR003817-
4}.
BINDING 2547 2547 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003817-2}.
BINDING 2577 2577 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR003817-
2}.
BINDING 2578 2578 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR003817-
2}.
BINDING 2595 2595 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003817-2}.
BINDING 2596 2596 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR003817-
2}.
BINDING 2622 2622 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003817-2}.
BINDING 2623 2623 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|PIRSR:PIRSR003817-
2}.
BINDING 2710 2710 S-adenosyl-L-methionine.
{ECO:0000256|PIRSR:PIRSR003817-2}.
DISULFID 283 310 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 340 396 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 354 385 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 372 401 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 465 565 {ECO:0000256|PIRSR:PIRSR003817-3}.
DISULFID 582 613 {ECO:0000256|PIRSR:PIRSR003817-3}.
SEQUENCE 3391 AA; 379202 MW; 6E0D3260DE1FC6A7 CRC64;
MNNQRKKARS TPFNMLKRER NRVSTVQQLT KRFSLGMLQG RGPLKLFMAL VAFLRFLTIP
PTAGILKRWG TIKKSKAINV LRGFRKEIGR MLNILNKRRR TAGVIVMLIP TAMAFHLTTR
NGEPHMIVGR QEKGKSLLFK TEDGVNMCTL MAIDLGELCE DTITYKCPLL RQNEPEDIDC
WCNSTSTWVT YGTCTTTGEH RREKRSVALV PHVGMGLETR TETWMSSEGA WKHVQRIETW
ILRHPGFTIM AAILAYTIGT THFQRALIFI LLTAVAPSMT MRCIGISNRD FVEGVSGGSW
VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC IEAKLTNTTT ESRCPTQGEP
SLSEEQDKRF ICKHSMVDRG WGNGCGLFGK GGIVTCAMFT CKKNMEGKVV QPENLEYTIV
ITPHSGEEHA VGNDTGKHGK EIKITPQSSI TEAELTGYGT VTMECSPRTG LDFNEMVLLQ
MEDKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF KNPHAKKQDV VVLGSQEGAM
HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS MCTGKFKIVK EIAETQHGTI
VIRVQYEGDG SPCKIPFEIT DLEKRHVLGR LITVNPIVTE KDSPVNIEAE PPFGDSYIII
GVEPGQLKLN WFKKGSSIGQ MFETTMRGAK RMAILGDTAW DFGSLGGVFT SIGKALHQVF
GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVSLV LVGVVTLYLG AMVQADSGCV
VSWKNKELKC GSGIFITDNV HTWTEQYKFQ PESPSKLASA IQKAHEEGIC GIRSVTRLEN
LMWKQITPEL NHILSENEVK LTIMTGDIRG IMQAGKRSLR PQPTELKYSW KTWGKAKMLS
TESHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT NIWLKLREKQ DVFCDSKLMS
AAIKDNRAVH ADMGYWIESA LNDTWKMEKA SFIEVKSCHW PKSHTLWSNG VLESEMIIPK
NFAGPVSQHN YRPGYHTQTA GPWHLGKLEM DFDLCEGTTV VVTEDCGNRG PSLRTTTASG
KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL VNSLVTAGHG QIDNFSLGVL
GMALFLEEML RTRIGTKHAI LLVAVSFVTL ITGNMSFRDL GRVMVMVGAT MTDDIGMGVT
YLALLAAFKV RPTFAAGLLL RKLTSKELMM ATIGIALLSQ STIPETILEL TDALALGMMV
LKIVRNMEKY QLAVTIMAIS CVPNAVILQN AWKVSCTILA AVSVSPLLLT SSQQKADWIP
LALTIKGLNP TAIFLTTLSR TSKKRSWPLN EAIMAVGMVS ILASSLLKND IPMTGPLVAG
GLLTVCYVLT GRSADLELER AADVKWEDQA EISGSSPILS ITISEDGSMS IKNEEEEQTL
TILIRTGLLV ISGVFPVSIP ITAAAWYLWE VKKQRAGVLW DVPSPPPVEK AELEDGAYRI
KQRGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHRGKRI EPSWADVKKD LISYGGGWKL
EGEWKEGEEV QVLALEPGKN PRAVQTKPGI FKTNTGTIGA VSLDFSPGTS GSPIVDRKGK
VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK KRLTIMDLHP GAGKTKRYLP
AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTT AIKTEHTGRE IVDLMCHATF
TMRLLSPVRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT ATPPGSRDPF
PQSNAPIMDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KAGNDIAACL RKNGKKVIQL
SRKTFDSEYV KTRANDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT DGEERVILAG
PMPVTHSSAA QRRGRIGRNP KNENDQYIYM GEPLENDEDC AHWKEAKMLL DNINTPEGII
PSMFEPEREK VDAIDGEYRL RGEARKTFVD LMRRGDLPVW LAYKVAAEGI NYADRKWCFD
GIKNNQILEE NMEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA GRKSLTLNLI
TEMGRLPTFM TQKARNALDN LAVLHTAEAG GRAYNHALSE LPETLETLLL LTLLATVTGG
IFLFLMSGKG IGKMTLGMCC IITASILLWY AQIQPHWIAA SIILEFFLIV LLIPEPEKQR
TPQDNQLTYV VIAILTVVAA TMANEMGFLE KTKKDLGLGS ITTQESESNI LDIDLRPASA
WTLYAVATTF VTPMLRHSIE NSSVNVSLTA IANQATVLMG LGKGWPLSKM DIGVPLLAIG
CYSQVNPITL TAALLLLVAH YAIIGPGLQA KATREAQKRA AAGIMKNPTV DGITVIDLEP
IPYDPKFEKQ LGQVMLLILC VTQVLMMRTT WALCEALTLA TGPISTLWEG NPGRFWNTTI
AVSMANIFRG SYLAGAGLLF SIMKNTTNTR RGTGNIGETL GEKWKSRLNA LGKSEFQIYK
KSGIQEVDRT LAKEGIKRGE TDHHAVSRGS AKLRWFVERN MVTPEGKVVD LGCGRGGWSY
YCGGLKNVRE VKGLTKGGPG HEEPIPMSTY GWNLVRLQSG VDVFFTPPEK CDTLLCDIGE
SSPNPTIEAG RTLRVLNLVE NWLNNNTQFC IKVLNPYMPS VIEKMEALQR KYGGALVRNP
LSRNSTHEMY WVSNATGNIV SSVNMISRML INRFTMKHKK ATYEPDVDLG SGTRNIGIES
EIPNLDIIGK RIEKIKQEHE TSWHYDQDHP YKTWAYHGSY ETKQTGSASS MVNGVVRLLT
KPWDVVPMVT QMAMTDTTPF GQQRVFKEKV DTRTQEPKEG TKKLMKITAE WLWKELGKKK
TPRMCTREEF TRKVRSNAAL GAIFTDENKW KSAREAVEDG RFWELVDRER NLHLEGKCET
CVYNMMGKRE KKLGEFGKAK GSRAIWYMWL GARFLEFEAL GFLNEDHWFS RGNSLSGVEG
EGLHRLGYIL RDVGKKEGGA MYADDTAGWD TRITLEDLKN EEMVTNHMKG EHKKLAEAIF
KLTYQNKVVR VQRPTPRGTV MDIISRRDQR GSGQVGTYGL NTFTNMEAQL IRQMEGEGIF
KSIQHLTATE EIAVQNWLAR VGRERLSRMA ISGDDCVVKP IDDRFASALT ALNDMGKIRK
DIQQWEPSRG WNDWTQVPFC SHHFHELVMK DGRVLVVPCR NQDELIGRAR ISQGAGWSLK
ETACLGKSYA QMWTLMYFHR RDLRLAANAI CSAVPSHWVP TSRTTWSIHA KHEWMTTEDM
LAVWNRVWIQ ENPWMEDKTP VESWEEVPYL GKREDQWCGS LIGLTSRATW AKNIQTAINQ
VRSLIGNEEY TDYMPSMKRF RREEEEAGVL W


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Kits Elisa; taq POLYMERASE

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