ID POLG_BVDVN Reviewed; 3988 AA.
AC P19711;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 27-MAR-2024, entry version 185.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=N-terminal protease;
DE Short=N-pro;
DE EC=3.4.22.-;
DE AltName: Full=Autoprotease p20;
DE Contains:
DE RecName: Full=Capsid protein C;
DE AltName: Full=p14;
DE Contains:
DE RecName: Full=E(rns) glycoprotein;
DE AltName: Full=gp44/48;
DE EC=4.6.1.19 {ECO:0000250|UniProtKB:Q96662};
DE Contains:
DE RecName: Full=Envelope glycoprotein E1;
DE AltName: Full=gp33;
DE Contains:
DE RecName: Full=Envelope glycoprotein E2;
DE AltName: Full=gp55;
DE Contains:
DE RecName: Full=Viroporin p7 {ECO:0000250|UniProtKB:P19712};
DE Contains:
DE RecName: Full=Non-structural protein 2-3;
DE Contains:
DE RecName: Full=Cysteine protease NS2;
DE EC=3.4.22.-;
DE AltName: Full=Non-structural protein 2;
DE AltName: Full=p54;
DE Contains:
DE RecName: Full=Serine protease NS3;
DE EC=3.4.21.113;
DE EC=3.6.1.15;
DE EC=3.6.4.13;
DE AltName: Full=Non-structural protein 3;
DE AltName: Full=p80;
DE Contains:
DE RecName: Full=Non-structural protein 4A;
DE Short=NS4A;
DE AltName: Full=p10;
DE Contains:
DE RecName: Full=Non-structural protein 4B;
DE Short=NS4B;
DE AltName: Full=p30;
DE Contains:
DE RecName: Full=Non-structural protein 5A;
DE Short=NS5A;
DE AltName: Full=p58;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=NS5B;
DE AltName: Full=p75;
OS Bovine viral diarrhea virus (isolate NADL) (BVDV) (Mucosal disease virus).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Pestivirus; Pestivirus bovis.
OX NCBI_TaxID=11100;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2838957; DOI=10.1016/0042-6822(88)90672-1;
RA Collett M.S., Larson R., Gold C., Strick D., Anderson D.K., Purchio A.F.;
RT "Molecular cloning and nucleotide sequence of the pestivirus bovine viral
RT diarrhea virus.";
RL Virology 165:191-199(1988).
RN [2]
RP GENOMIC ORGANIZATION.
RX PubMed=2838958; DOI=10.1016/0042-6822(88)90673-3;
RA Collett M.S., Larson R., Belzer S.K., Retzel E.;
RT "Proteins encoded by bovine viral diarrhea virus: the genomic organization
RT of a pestivirus.";
RL Virology 165:200-208(1988).
RN [3]
RP PROTEIN SEQUENCE OF 2363-2376; 2427-2441; 2774-2788 AND 3270-3284, AND
RP PROTEOLYTIC PROCESSING (GENOME POLYPROTEIN).
RX PubMed=9188600; DOI=10.1128/jvi.71.7.5312-5322.1997;
RA Xu J., Mendez E., Caron P.R., Lin C., Murcko M.A., Collett M.S., Rice C.M.;
RT "Bovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage
RT sites, cofactor requirements, and molecular model of an enzyme essential
RT for pestivirus replication.";
RL J. Virol. 71:5312-5322(1997).
RN [4]
RP SUBCELLULAR LOCATION (E(RNS) GLYCOPROTEIN), AND SUBCELLULAR LOCATION
RP (ENVELOPE GLYCOPROTEIN E2).
RX PubMed=10355762; DOI=10.1099/0022-1317-80-5-1157;
RA Weiland F., Weiland E., Unger G., Saalmuller A., Thiel H.-J.;
RT "Localization of pestiviral envelope proteins E(rns) and E2 at the cell
RT surface and on isolated particles.";
RL J. Gen. Virol. 80:1157-1165(1999).
RN [5]
RP ROLE OF BOVINE LOW-DENSITY-LIPOPROTEIN RECEPTOR IN VIRUS ATTACHMENT TO HOST
RP CELL.
RX PubMed=10535997; DOI=10.1073/pnas.96.22.12766;
RA Agnello V., Abel G., Elfahal M., Knight G.B., Zhang Q.X.;
RT "Hepatitis C virus and other flaviviridae viruses enter cells via low
RT density lipoprotein receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12766-12771(1999).
RN [6]
RP INTERACTION WITH CELL SURFACE GLYCOSAMINOGLYCANS (E(RNS) GLYCOPROTEIN).
RX PubMed=10644844; DOI=10.1099/0022-1317-81-2-451;
RA Iqbal M., Flick-Smith H., McCauley J.W.;
RT "Interactions of bovine viral diarrhoea virus glycoprotein E(rns) with cell
RT surface glycosaminoglycans.";
RL J. Gen. Virol. 81:451-459(2000).
RN [7]
RP FUNCTION (NON-STRUCTURAL PROTEIN 2-3).
RC STRAIN=Isolate NADL Jiv 90(-);
RX PubMed=14963137; DOI=10.1128/jvi.78.5.2414-2425.2004;
RA Agapov E.V., Murray C.L., Frolov I., Qu L., Myers T.M., Rice C.M.;
RT "Uncleaved NS2-3 is required for production of infectious bovine viral
RT diarrhea virus.";
RL J. Virol. 78:2414-2425(2004).
RN [8]
RP FUNCTION (ENVELOPE GLYCOPROTEIN E1), AND FUNCTION (ENVELOPE GLYCOPROTEIN
RP E2).
RX PubMed=14747544; DOI=10.1128/jvi.78.4.1792-1799.2004;
RA Maurer K., Krey T., Moennig V., Thiel H.-J., Ruemenapf T.;
RT "CD46 is a cellular receptor for bovine viral diarrhea virus.";
RL J. Virol. 78:1792-1799(2004).
RN [9]
RP FUNCTION OF E1/E2 HETERODIMER.
RX PubMed=16051874; DOI=10.1128/jvi.79.16.10826-10829.2005;
RA Lecot S., Belouzard S., Dubuisson J., Rouille Y.;
RT "Bovine viral diarrhea virus entry is dependent on clathrin-mediated
RT endocytosis.";
RL J. Virol. 79:10826-10829(2005).
RN [10]
RP FUNCTION (N-TERMINAL PROTEASE).
RX PubMed=17531282; DOI=10.1016/j.virol.2007.04.023;
RA Chen Z., Rijnbrand R., Jangra R.K., Devaraj S.G., Qu L., Ma Y., Lemon S.M.,
RA Li K.;
RT "Ubiquitination and proteasomal degradation of interferon regulatory
RT factor-3 induced by Npro from a cytopathic bovine viral diarrhea virus.";
RL Virology 366:277-292(2007).
RN [11]
RP FUNCTION (NON-STRUCTURAL PROTEIN 4B), AND INTERACTION WITH HOST IFIH1/MDA5.
RX PubMed=34097933; DOI=10.1016/j.virusres.2021.198471;
RA Shan Y., Tong Z., Jinzhu M., Yu L., Zecai Z., Chenhua W., Wenjing H.,
RA Siyu L., Nannan C., Siyu S., Tongtong B., Jiang H., Biaohui B., Xin J.,
RA Yulong Z., Zhanbo Z.;
RT "Bovine viral diarrhea virus NS4B protein interacts with 2CARD of MDA5
RT domain and negatively regulates the RLR-mediated IFN-beta production.";
RL Virus Res. 302:198471-198471(2021).
RN [12] {ECO:0007744|PDB:1S48, ECO:0007744|PDB:1S49, ECO:0007744|PDB:1S4F}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 3348-3948 IN COMPLEX WITH GTP,
RP AND FUNCTION (RNA-DIRECTED RNA POLYMERASE).
RX PubMed=15070734; DOI=10.1073/pnas.0400660101;
RA Choi K.H., Groarke J.M., Young D.C., Kuhn R.J., Smith J.L., Pevear D.C.,
RA Rossmann M.G.;
RT "The structure of the RNA-dependent RNA polymerase from bovine viral
RT diarrhea virus establishes the role of GTP in de novo initiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4425-4430(2004).
RN [13] {ECO:0007744|PDB:4ILD, ECO:0007744|PDB:4JNT}
RP X-RAY CRYSTALLOGRAPHY (3.27 ANGSTROMS) OF 781-1030 IN COMPLEX WITH CA(2+),
RP GLYCOSYLATION AT ASN-809; ASN-878; ASN-922 AND ASN-990, SUBUNIT (ENVELOPE
RP GLYCOPROTEIN E2), FUNCTION (ENVELOPE GLYCOPROTEIN E2), AND DISULFIDE BONDS
RP (ENVELOPE GLYCOPROTEIN E2).
RX PubMed=23569276; DOI=10.1073/pnas.1300524110;
RA Li Y., Wang J., Kanai R., Modis Y.;
RT "Crystal structure of glycoprotein E2 from bovine viral diarrhea virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6805-6810(2013).
CC -!- FUNCTION: [N-terminal protease]: Leader cysteine autoprotease that
CC cleaves itself from the nascent polyprotein during translation of the
CC viral mRNA. Once released, plays a role in the inhibition of host
CC innate immune response by interacting with host IRF3 and inducing its
CC proteasomal degradation (PubMed:17531282).
CC {ECO:0000269|PubMed:17531282}.
CC -!- FUNCTION: [Capsid protein C]: Packages viral RNA to form a viral
CC nucleocapsid and thereby protects viral RNA. Also plays a role in
CC transcription regulation. Protects the incoming virus against IFN-
CC induced effectors. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [E(rns) glycoprotein]: Initial binding to target cell
CC probably involves interaction of E(rns) with glycosaminoglycans
CC (PubMed:10644844). Possesses also intrinsic ribonuclease (RNase)
CC activity that can inhibit the production of type I interferon and
CC assist in the development of persistent infections (By similarity).
CC {ECO:0000250|UniProtKB:Q96662, ECO:0000269|PubMed:10644844}.
CC -!- FUNCTION: [Envelope glycoprotein E1]: E1 and/or E2 are probably
CC responsible of cell attachment with CD46 and subsequent fusion after
CC internalization of the virion by endocytosis.
CC {ECO:0000305|PubMed:14747544}.
CC -!- FUNCTION: [Envelope glycoprotein E2]: E1 and/or E2 are probably
CC responsible of cell attachment with CD46 and subsequent fusion after
CC internalization of the virion by endocytosis (Probable). Probably
CC functions as a coeffector of fusion providing structural integrity to
CC the fusion complex and possibly controlling exposure of the fusion
CC motif in E1 (PubMed:23569276). {ECO:0000269|PubMed:23569276,
CC ECO:0000305|PubMed:14747544}.
CC -!- FUNCTION: [Viroporin p7]: Plays an essential role in the virus
CC replication cycle by acting as a viroporin (By similarity). Forms ion
CC conductive pores, which alters the cell permeability allowing the
CC transport of ions and other small molecules (By similarity). Forms a
CC leader sequence to properly orient NS2 in the membrane.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Non-structural protein 2-3]: Uncleaved NS2-3 is required for
CC production of infectious virus. {ECO:0000269|PubMed:14963137}.
CC -!- FUNCTION: [Cysteine protease NS2]: Plays a role in the regulation of
CC viral RNA replication. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Serine protease NS3]: Multifunctional protein that contains
CC an N-terminal protease and a C-terminal helicase, playing essential
CC roles in viral polyprotein processing and viral genome replication. The
CC chymotrypsin-like serine protease activity utilizes NS4A as an
CC essential cofactor and catalyzes the cleavage of the polyprotein
CC leading to the release of NS4A, NS4B, NS5A, and NS5B. Interacts with
CC NS5B to enhance RNA-dependent RNA polymerase activity.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Non-structural protein 4A]: Acts as a cofactor for the NS3
CC protease activity. {ECO:0000250|UniProtKB:P19712}.
CC -!- FUNCTION: [Non-structural protein 4B]: Induces a specific membrane
CC alteration that serves as a scaffold for the virus replication complex
CC (By similarity). Plays a role in the inhibition of host innate immune
CC response by inhibiting RIGI/IFIH1-mediated IFN-beta production
CC (PubMed:34097933). {ECO:0000250|UniProtKB:P19712,
CC ECO:0000269|PubMed:34097933}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral (+) and
CC (-) genome. Initiates the primer-independent RNA replication via a de
CC novo mechanism requiring GTP (PubMed:15070734).
CC {ECO:0000269|PubMed:15070734}.
CC -!- CATALYTIC ACTIVITY: [Serine protease NS3]:
CC Reaction=Leu is conserved at position P1 for all four cleavage sites.
CC Alanine is found at position P1' of the NS4A-NS4B cleavage site,
CC whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A
CC and NS5A-NS5B cleavage sites.; EC=3.4.21.113;
CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY: [Serine protease NS3]:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY: [Serine protease NS3]:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- CATALYTIC ACTIVITY: [E(rns) glycoprotein]:
CC Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-
CC phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA +
CC H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-
CC COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173118; EC=4.6.1.19;
CC Evidence={ECO:0000250|UniProtKB:Q96662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68053;
CC Evidence={ECO:0000250|UniProtKB:Q96662};
CC -!- CATALYTIC ACTIVITY: [E(rns) glycoprotein]:
CC Reaction=a ribonucleotidyl-ribonucleotide-RNA = a 3'-end 2',3'-
CC cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-
CC RNA; Xref=Rhea:RHEA:67796, Rhea:RHEA-COMP:10464, Rhea:RHEA-
CC COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:83064,
CC ChEBI:CHEBI:138284, ChEBI:CHEBI:173118;
CC Evidence={ECO:0000250|UniProtKB:Q96662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67797;
CC Evidence={ECO:0000250|UniProtKB:Q96662};
CC -!- CATALYTIC ACTIVITY: [E(rns) glycoprotein]:
CC Reaction=a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + H2O = a 3'-
CC end 3'-phospho-ribonucleotide-RNA + H(+); Xref=Rhea:RHEA:68056,
CC Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:10464, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:83064;
CC Evidence={ECO:0000250|UniProtKB:Q96662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68057;
CC Evidence={ECO:0000250|UniProtKB:Q96662};
CC -!- ACTIVITY REGULATION: [E(rns) glycoprotein]: Inhibited by Zn(2+), which
CC binds the catalytic site. {ECO:0000250|UniProtKB:Q96662}.
CC -!- SUBUNIT: [E(rns) glycoprotein]: Homodimer (By similarity). E(rns)
CC homodimer is disulfide-linked in other strains, but the cysteine
CC involved in the bond is not conserved in isolate NADL (Probable).
CC {ECO:0000250|UniProtKB:Q96662, ECO:0000305}.
CC -!- SUBUNIT: [Envelope glycoprotein E1]: Homodimer; disulfide-linked (By
CC similarity). Heterodimer with E1; disulfide-linked (By similarity).
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBUNIT: [Envelope glycoprotein E2]: Homodimer; disulfide-linked
CC (PubMed:23569276). Heterodimer with E1; disulfide-linked (By
CC similarity). {ECO:0000250|UniProtKB:P19712,
CC ECO:0000269|PubMed:23569276}.
CC -!- SUBUNIT: [Non-structural protein 4B]: Interacts with host IFIH1/MDA5;
CC this interaction is involved in the inhibition of IFN-beta production.
CC {ECO:0000269|PubMed:34097933}.
CC -!- INTERACTION:
CC P19711; P19711: -; NbExp=3; IntAct=EBI-9350498, EBI-9350498;
CC PRO_0000038031; Q95J56: DNAJC14; Xeno; NbExp=2; IntAct=EBI-9612504, EBI-9612178;
CC PRO_0000038033; F1MUM9: ADAR; Xeno; NbExp=6; IntAct=EBI-9350731, EBI-9350738;
CC PRO_0000038035; P68103: EEF1A1; Xeno; NbExp=6; IntAct=EBI-9350549, EBI-352178;
CC PRO_0000038035; Q32PH0: TRAPPC9; Xeno; NbExp=7; IntAct=EBI-9350549, EBI-9522367;
CC -!- SUBCELLULAR LOCATION: [Capsid protein C]: Virion
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBCELLULAR LOCATION: [E(rns) glycoprotein]: Host membrane
CC {ECO:0000269|PubMed:10355762}; Peripheral membrane protein. Virion
CC membrane {ECO:0000305|PubMed:10355762}; Peripheral membrane protein
CC {ECO:0000305}. Note=The C-terminus membrane anchor of Erns represents
CC an amphipathic helix embedded in plane into the membrane.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein E1]: Host endoplasmic
CC reticulum membrane; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q96662}. Virion membrane
CC {ECO:0000250|UniProtKB:P19712}; Single-pass type I membrane protein.
CC Note=The C-terminal transmembrane domain acts as a signal sequence and
CC forms a hairpin structure before cleavage by host signal peptidase.
CC This explains that E1 and E2 are mostly lumenal. After cleavage, the C-
CC terminus transmembrane sequence acts as ER membrane anchor.
CC {ECO:0000250|UniProtKB:Q96662}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein E2]: Host endoplasmic
CC reticulum membrane; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q96662}. Virion membrane
CC {ECO:0000305|PubMed:10355762}; Single-pass type I membrane protein.
CC Note=The C-terminal transmembrane domain acts as a signal sequence and
CC forms a hairpin structure before cleavage by host signal peptidase.
CC This explains that E1 and E2 are mostly lumenal. After cleavage, the C-
CC terminus transmembrane sequence acts as ER membrane anchor.
CC {ECO:0000250|UniProtKB:Q96662}.
CC -!- SUBCELLULAR LOCATION: [Cysteine protease NS2]: Host membrane
CC {ECO:0000255|PROSITE-ProRule:PRU01029}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU01029}.
CC -!- SUBCELLULAR LOCATION: [Serine protease NS3]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 4B]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 5A]: Host membrane
CC {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96662}. Note=The N-terminus membrane anchor
CC represents an amphipathic helix embedded in plane into the membrane.
CC {ECO:0000250|UniProtKB:Q96662}.
CC -!- DOMAIN: [Envelope glycoprotein E1]: The transmembrane domain is
CC responsible for ER localization. {ECO:0000250|UniProtKB:Q96662}.
CC -!- DOMAIN: [Envelope glycoprotein E2]: The transmembrane domain is
CC responsible for ER localization. {ECO:0000250|UniProtKB:Q96662}.
CC -!- PTM: [E(rns) glycoprotein]: Heavily glycosylated.
CC {ECO:0000250|UniProtKB:P19712}.
CC -!- PTM: The viral RNA of pestiviruses is expressed as a single polyprotein
CC which undergoes post-translational proteolytic processing resulting in
CC the production of at least eleven individual proteins. The N-terminal
CC protease cleaves itself from the nascent polyprotein autocatalytically
CC and thereby generates the N-terminus of the adjacent viral capsid
CC protein C (By similarity). {ECO:0000250}.
CC -!- PTM: [Genome polyprotein]: Cleavage between E2 and p7 is partial.
CC -!- MISCELLANEOUS: BVDV is divided in two types: cytopathic and non-
CC cytopathic. Both types of viruses can be found in animals suffering
CC from mucosal disease, as a cytopathic BVDV can develop from a non-
CC cytopathic virus within the infected animal by deletions, mutations or
CC insertions. Both types express uncleaved NS2-3, but cytopathic strains
CC also express NS3. The cytopathic NADL strain contains an insertion (Jiv
CC 90) that potentiate the partial cleavage of NS2-3. Removal of this
CC insertion in the NADL Jiv 90(-) strain results in a non-cytopathic
CC strain in which NS2-3 remains uncleaved.
CC -!- SIMILARITY: Belongs to the pestivirus polyprotein family.
CC {ECO:0000305}.
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DR EMBL; M31182; AAA42854.1; -; Genomic_RNA.
DR PIR; A29198; GNWVBV.
DR RefSeq; NP_040937.1; NC_001461.1.
DR PDB; 1S48; X-ray; 3.00 A; A=3340-3948.
DR PDB; 1S49; X-ray; 3.00 A; A=3340-3948.
DR PDB; 1S4F; X-ray; 3.00 A; A/B/C/D=3348-3948.
DR PDB; 4ILD; X-ray; 3.27 A; A/B=781-1030.
DR PDB; 4JNT; X-ray; 4.09 A; A/B=693-1030.
DR PDB; 5GVU; X-ray; 2.82 A; A/B/C=1887-2362.
DR PDB; 5WSO; X-ray; 2.82 A; A/B/C=1887-2362.
DR PDBsum; 1S48; -.
DR PDBsum; 1S49; -.
DR PDBsum; 1S4F; -.
DR PDBsum; 4ILD; -.
DR PDBsum; 4JNT; -.
DR PDBsum; 5GVU; -.
DR PDBsum; 5WSO; -.
DR SMR; P19711; -.
DR IntAct; P19711; 128.
DR BindingDB; P19711; -.
DR DrugBank; DB04137; Guanosine-5'-Triphosphate.
DR MEROPS; C53.001; -.
DR MEROPS; C74.001; -.
DR MEROPS; S31.001; -.
DR ABCD; P19711; 2 sequenced antibodies.
DR GeneID; 1489735; -.
DR KEGG; vg:1489735; -.
DR EvolutionaryTrace; P19711; -.
DR Proteomes; UP000002317; Genome.
DR GO; GO:0044161; C:host cell cytoplasmic vesicle; IDA:AgBase.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:CAFA.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:CAFA.
DR GO; GO:1990814; F:DNA/DNA annealing activity; IDA:CAFA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IDA:CAFA.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0033592; F:RNA strand annealing activity; IDA:CAFA.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0043489; P:RNA stabilization; IDA:CAFA.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR GO; GO:0019072; P:viral genome packaging; IEP:DisProt.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR CDD; cd17931; DEXHc_viral_Ns3; 1.
DR CDD; cd23201; Pestivirus_RdRp; 1.
DR DisProt; DP00675; -.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.60.40.4200; Pestivirus envelope glycoprotein E2, C-terminal domain; 1.
DR Gene3D; 2.60.320.20; Pestivirus envelope glycoprotein E2, domain A; 1.
DR Gene3D; 2.60.40.3000; Pestivirus envelope glycoprotein E2, domain B; 1.
DR Gene3D; 2.30.140.40; Pestivirus Npro endopeptidase C53, interaction domain; 1.
DR Gene3D; 3.90.730.10; Ribonuclease T2-like; 1.
DR InterPro; IPR021824; Capsid-C_pestivirus.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR011492; Flavi_DEAD.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR032843; Jiv.
DR InterPro; IPR022120; NS2.
DR InterPro; IPR030399; NS2_C74.
DR InterPro; IPR049486; NS3-hel_C_flaviviridae.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008751; Peptidase_C53.
DR InterPro; IPR042542; Peptidase_C53_interaction.
DR InterPro; IPR032521; Pestivirus_E2.
DR InterPro; IPR042309; Pestivirus_E2_A.
DR InterPro; IPR042310; Pestivirus_E2_B.
DR InterPro; IPR042311; Pestivirus_E2_D.
DR InterPro; IPR000280; Pestivirus_NS3_S31.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002166; RNA_pol_HCV.
DR InterPro; IPR036430; RNase_T2-like_sf.
DR InterPro; IPR033130; RNase_T2_His_AS_2.
DR PANTHER; PTHR44665; DNAJ HOMOLOG SUBFAMILY C MEMBER 14; 1.
DR PANTHER; PTHR44665:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 14; 1.
DR Pfam; PF11889; Capsid_pestivir; 1.
DR Pfam; PF20907; Flav_NS3-hel_C; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF14901; Jiv90; 1.
DR Pfam; PF05550; Peptidase_C53; 1.
DR Pfam; PF12387; Peptidase_C74; 1.
DR Pfam; PF05578; Peptidase_S31; 1.
DR Pfam; PF16329; Pestivirus_E2; 1.
DR Pfam; PF00998; RdRP_3; 1.
DR PRINTS; PR00729; CDVENDOPTASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF55895; Ribonuclease Rh-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51692; PESTIVIRUS_NS2_PRO; 1.
DR PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1.
DR PROSITE; PS51876; PV_NPRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS00531; RNASE_T2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activation of host autophagy by virus; ATP-binding;
KW Clathrin-mediated endocytosis of virus by host; Direct protein sequencing;
KW Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein; GTP-binding;
KW Helicase; Host cytoplasm; Host endoplasmic reticulum; Host membrane;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host IRF3 by virus; Inhibition of host RLR pathway by virus;
KW Ion channel; Ion transport; Lyase; Membrane; Nuclease; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; Reference proteome;
KW RNA-directed RNA polymerase; Serine protease; Thiol protease; Transferase;
KW Transmembrane; Transmembrane helix; Transport;
KW Viral attachment to host cell; Viral immunoevasion; Viral ion channel;
KW Viral penetration into host cytoplasm; Viral RNA replication; Virion;
KW Virus endocytosis by host; Virus entry into host cell.
FT CHAIN 1..3988
FT /note="Genome polyprotein"
FT /id="PRO_0000450891"
FT CHAIN 1..168
FT /note="N-terminal protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038024"
FT CHAIN 169..270
FT /note="Capsid protein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038025"
FT CHAIN 271..497
FT /note="E(rns) glycoprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038026"
FT CHAIN 498..692
FT /note="Envelope glycoprotein E1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038027"
FT CHAIN 693..1066
FT /note="Envelope glycoprotein E2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038028"
FT CHAIN 1067..1136
FT /note="Viroporin p7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038029"
FT CHAIN 1137..2362
FT /note="Non-structural protein 2-3"
FT /id="PRO_0000038030"
FT CHAIN 1137..1679
FT /note="Cysteine protease NS2"
FT /id="PRO_0000038031"
FT CHAIN 1680..2362
FT /note="Serine protease NS3"
FT /id="PRO_0000038032"
FT CHAIN 2363..2426
FT /note="Non-structural protein 4A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038033"
FT CHAIN 2427..2773
FT /note="Non-structural protein 4B"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038034"
FT CHAIN 2774..3269
FT /note="Non-structural protein 5A"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038035"
FT CHAIN 3270..3988
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000038036"
FT TOPO_DOM 498..666
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96662"
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 688..1035
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96662"
FT TRANSMEM 1036..1056
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1079..1099
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1108..1128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1144..1164
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1189..1209
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1217..1237
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1247..1267
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1281..1301
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1360..1380
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT TRANSMEM 1658..1678
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT DOMAIN 1..168
FT /note="Peptidase C53"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT DOMAIN 1441..1679
FT /note="Peptidase C74"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT DOMAIN 1680..1853
FT /note="Peptidase S31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT DOMAIN 1892..2050
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 2068..2233
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 3608..3731
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 43..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2000..2003
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 174..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 49
FT /note="For N-terminal protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT ACT_SITE 69
FT /note="For N-terminal protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT ACT_SITE 344
FT /note="For E(rns) glycoprotein RNase activity"
FT /evidence="ECO:0000250|UniProtKB:Q96662"
FT ACT_SITE 345
FT /note="For E(rns) glycoprotein RNase activity"
FT /evidence="ECO:0000250|UniProtKB:Q96662"
FT ACT_SITE 348
FT /note="For E(rns) glycoprotein RNase activity"
FT /evidence="ECO:0000250|UniProtKB:Q96662"
FT ACT_SITE 349
FT /note="For E(rns) glycoprotein RNase activity"
FT /evidence="ECO:0000250|UniProtKB:Q96662"
FT ACT_SITE 1447
FT /note="For cysteine protease NS2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT ACT_SITE 1461
FT /note="For cysteine protease NS2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT ACT_SITE 1512
FT /note="For cysteine protease NS2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01029"
FT ACT_SITE 1748
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1785
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1842
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00868"
FT BINDING 1905..1912
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 3589
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:15070734"
FT BINDING 3591
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:15070734"
FT BINDING 3786
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:15070734"
FT BINDING 3794
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:15070734"
FT SITE 168..169
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01224"
FT SITE 270..271
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P19712"
FT SITE 300
FT /note="Hydrogen donor to release the cleavage products of
FT E(rns) glycoprotein RNase activity"
FT /evidence="ECO:0000250|UniProtKB:Q96662"
FT SITE 497..498
FT /note="Cleavage"
FT SITE 692..693
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250|UniProtKB:P19712"
FT SITE 762
FT /note="Serves as pH sensor to control fusion"
FT /evidence="ECO:0000269|PubMed:23569276"
FT SITE 1066..1067
FT /note="Cleavage; by host signal peptidase; partial"
FT /evidence="ECO:0000250"
FT SITE 1136..1137
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 1679..1680
FT /note="Cleavage; partial; cysteine protease NS2"
FT SITE 2362..2363
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250"
FT SITE 2426..2427
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250"
FT SITE 2773..2774
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250"
FT SITE 3269..3270
FT /note="Cleavage; by serine protease NS3"
FT /evidence="ECO:0000250"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:23569276"
FT CARBOHYD 878
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:23569276"
FT CARBOHYD 922
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:23569276"
FT CARBOHYD 990
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:23569276"
FT CARBOHYD 1357
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1419
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1451
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1803
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2224
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2307
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2584
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2772
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 2981
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3778
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3867
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 3883
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 308..352
FT /evidence="ECO:0000250|UniProtKB:Q96662"
FT DISULFID 338..339
FT /evidence="ECO:0000250|UniProtKB:Q96662"
FT DISULFID 380..425
FT /evidence="ECO:0000250|UniProtKB:Q96662"
FT DISULFID 384..408
FT /evidence="ECO:0000250|UniProtKB:Q96662"
FT DISULFID 696..740
FT /evidence="ECO:0000269|PubMed:23569276"
FT DISULFID 751..798
FT /evidence="ECO:0000269|PubMed:23569276"
FT DISULFID 987
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:23569276"
FT STRAND 784..786
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 793..795
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 803..805
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 811..814
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 817..820
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 828..835
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 837..839
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 842..850
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 863..866
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 869..875
FT /evidence="ECO:0007829|PDB:4ILD"
FT TURN 878..880
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 882..886
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 894..899
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 902..906
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 910..914
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 916..922
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 925..928
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 934..936
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 939..941
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 946..951
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 954..960
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 969..971
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 987..993
FT /evidence="ECO:0007829|PDB:4ILD"
FT TURN 1005..1007
FT /evidence="ECO:0007829|PDB:4ILD"
FT STRAND 1014..1022
FT /evidence="ECO:0007829|PDB:4ILD"
FT HELIX 1889..1892
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 1900..1903
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 1911..1923
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 1929..1935
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 1936..1949
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 1951..1953
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 1955..1961
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 1970..1975
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 1976..1979
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 1984..1991
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 1995..1999
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2002..2004
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2007..2016
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2017..2022
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2025..2028
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2045..2049
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2064..2066
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2069..2071
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2073..2076
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2080..2083
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2089..2098
FT /evidence="ECO:0007829|PDB:5GVU"
FT TURN 2099..2101
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2114..2120
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2121..2124
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2126..2129
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2144..2147
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2149..2158
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2160..2173
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2176..2183
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2188..2190
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2192..2196
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2202..2204
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2208..2214
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2215..2218
FT /evidence="ECO:0007829|PDB:5GVU"
FT TURN 2219..2222
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2225..2235
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2243..2256
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2263..2271
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2278..2283
FT /evidence="ECO:0007829|PDB:5GVU"
FT TURN 2284..2286
FT /evidence="ECO:0007829|PDB:5GVU"
FT STRAND 2324..2327
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2328..2336
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 2347..2361
FT /evidence="ECO:0007829|PDB:5GVU"
FT HELIX 3364..3372
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3373..3376
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3382..3384
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3388..3392
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3402..3404
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3406..3414
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3419..3421
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3422..3427
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3431..3440
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3453..3462
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3467..3469
FT /evidence="ECO:0007829|PDB:1S48"
FT TURN 3470..3472
FT /evidence="ECO:0007829|PDB:1S4F"
FT HELIX 3478..3481
FT /evidence="ECO:0007829|PDB:1S48"
FT TURN 3482..3484
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3501..3504
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3507..3518
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3527..3531
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3535..3537
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3539..3543
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3549..3551
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3555..3558
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3563..3570
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3572..3575
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3586..3588
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3591..3593
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3594..3603
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3605..3612
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3615..3617
FT /evidence="ECO:0007829|PDB:1S4F"
FT HELIX 3618..3621
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3624..3637
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3640..3642
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3643..3652
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3655..3660
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3665..3668
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3679..3699
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3703..3705
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3706..3709
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3710..3715
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3718..3724
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3725..3741
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3750..3753
FT /evidence="ECO:0007829|PDB:1S4F"
FT STRAND 3756..3759
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3760..3762
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3768..3775
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3780..3785
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3788..3797
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3802..3804
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3808..3810
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3811..3822
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3826..3837
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3846..3854
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3856..3864
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3868..3870
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3871..3874
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3876..3882
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3885..3888
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3896..3908
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3910..3912
FT /evidence="ECO:0007829|PDB:1S48"
FT TURN 3915..3918
FT /evidence="ECO:0007829|PDB:1S48"
FT HELIX 3920..3926
FT /evidence="ECO:0007829|PDB:1S48"
FT STRAND 3935..3939
FT /evidence="ECO:0007829|PDB:1S48"
SQ SEQUENCE 3988 AA; 449163 MW; 4474212F338661B8 CRC64;
MELITNELLY KTYKQKPVGV EEPVYDQAGD PLFGERGAVH PQSTLKLPHK RGERDVPTNL
ASLPKRGDCR SGNSRGPVSG IYLKPGPLFY QDYKGPVYHR APLELFEEGS MCETTKRIGR
VTGSDGKLYH IYVCIDGCII IKSATRSYQR VFRWVHNRLD CPLWVTTCSD TKEEGATKKK
TQKPDRLERG KMKIVPKESE KDSKTKPPDA TIVVEGVKYQ VRKKGKTKSK NTQDGLYHNK
NKPQESRKKL EKALLAWAII AIVLFQVTMG ENITQWNLQD NGTEGIQRAM FQRGVNRSLH
GIWPEKICTG VPSHLATDIE LKTIHGMMDA SEKTNYTCCR LQRHEWNKHG WCNWYNIEPW
ILVMNRTQAN LTEGQPPREC AVTCRYDRAS DLNVVTQARD SPTPLTGCKK GKNFSFAGIL
MRGPCNFEIA ASDVLFKEHE RISMFQDTTL YLVDGLTNSL EGARQGTAKL TTWLGKQLGI
LGKKLENKSK TWFGAYAASP YCDVDRKIGY IWYTKNCTPA CLPKNTKIVG PGKFGTNAED
GKILHEMGGH LSEVLLLSLV VLSDFAPETA SVMYLILHFS IPQSHVDVMD CDKTQLNLTV
ELTTAEVIPG SVWNLGKYVC IRPNWWPYET TVVLAFEEVS QVVKLVLRAL RDLTRIWNAA
TTTAFLVCLV KIVRGQMVQG ILWLLLITGV QGHLDCKPEF SYAIAKDERI GQLGAEGLTT
TWKEYSPGMK LEDTMVIAWC EDGKLMYLQR CTRETRYLAI LHTRALPTSV VFKKLFDGRK
QEDVVEMNDN FEFGLCPCDA KPIVRGKFNT TLLNGPAFQM VCPIGWTGTV SCTSFNMDTL
ATTVVRTYRR SKPFPHRQGC ITQKNLGEDL HNCILGGNWT CVPGDQLLYK GGSIESCKWC
GYQFKESEGL PHYPIGKCKL ENETGYRLVD STSCNREGVA IVPQGTLKCK IGKTTVQVIA
MDTKLGPMPC RPYEIISSEG PVEKTACTFN YTKTLKNKYF EPRDSYFQQY MLKGEYQYWF
DLEVTDHHRD YFAESILVVV VALLGGRYVL WLLVTYMVLS EQKALGIQYG SGEVVMMGNL
LTHNNIEVVT YFLLLYLLLR EESVKKWVLL LYHILVVHPI KSVIVILLMI GDVVKADSGG
QEYLGKIDLC FTTVVLIVIG LIIARRDPTI VPLVTIMAAL RVTELTHQPG VDIAVAVMTI
TLLMVSYVTD YFRYKKWLQC ILSLVSAVFL IRSLIYLGRI EMPEVTIPNW RPLTLILLYL
ISTTIVTRWK VDVAGLLLQC VPILLLVTTL WADFLTLILI LPTYELVKLY YLKTVRTDTE
RSWLGGIDYT RVDSIYDVDE SGEGVYLFPS RQKAQGNFSI LLPLIKATLI SCVSSKWQLI
YMSYLTLDFM YYMHRKVIEE ISGGTNIISR LVAALIELNW SMEEEESKGL KKFYLLSGRL
RNLIIKHKVR NETVASWYGE EEVYGMPKIM TIIKASTLSK SRHCIICTVC EGREWKGGTC
PKCGRHGKPI TCGMSLADFE ERHYKRIFIR EGNFEGMCSR CQGKHRRFEM DREPKSARYC
AECNRLHPAE EGDFWAESSM LGLKITYFAL MDGKVYDITE WAGCQRVGIS PDTHRVPCHI
SFGSRMPFRQ EYNGFVQYTA RGQLFLRNLP VLATKVKMLM VGNLGEEIGN LEHLGWILRG
PAVCKKITEH EKCHINILDK LTAFFGIMPR GTTPRAPVRF PTSLLKVRRG LETAWAYTHQ
GGISSVDHVT AGKDLLVCDS MGRTRVVCQS NNRLTDETEY GVKTDSGCPD GARCYVLNPE
AVNISGSKGA VVHLQKTGGE FTCVTASGTP AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV
GKNEESKPTK IMSGIQTVSK NRADLTEMVK KITSMNRGDF KQITLATGAG KTTELPKAVI
EEIGRHKRVL VLIPLRAAAE SVYQYMRLKH PSISFNLRIG DMKEGDMATG ITYASYGYFC
QMPQPKLRAA MVEYSYIFLD EYHCATPEQL AIIGKIHRFS ESIRVVAMTA TPAGSVTTTG
QKHPIEEFIA PEVMKGEDLG SQFLDIAGLK IPVDEMKGNM LVFVPTRNMA VEVAKKLKAK
GYNSGYYYSG EDPANLRVVT SQSPYVIVAT NAIESGVTLP DLDTVIDTGL KCEKRVRVSS
KIPFIVTGLK RMAVTVGEQA QRRGRVGRVK PGRYYRSQET ATGSKDYHYD LLQAQRYGIE
DGINVTKSFR EMNYDWSLYE EDSLLITQLE ILNNLLISED LPAAVKNIMA RTDHPEPIQL
AYNSYEVQVP VLFPKIRNGE VTDTYENYSF LNARKLGEDV PVYIYATEDE DLAVDLLGLD
WPDPGNQQVV ETGKALKQVT GLSSAENALL VALFGYVGYQ ALSKRHVPMI TDIYTIEDQR
LEDTTHLQYA PNAIKTDGTE TELKELASGD VEKIMGAISD YAAGGLEFVK SQAEKIKTAP
LFKENAEAAK GYVQKFIDSL IENKEEIIRY GLWGTHTALY KSIAARLGHE TAFATLVLKW
LAFGGESVSD HVKQAAVDLV VYYVMNKPSF PGDSETQQEG RRFVASLFIS ALATYTYKTW
NYHNLSKVVE PALAYLPYAT SALKMFTPTR LESVVILSTT IYKTYLSIRK GKSDGLLGTG
ISAAMEILSQ NPVSVGISVM LGVGAIAAHN AIESSEQKRT LLMKVFVKNF LDQAATDELV
KENPEKIIMA LFEAVQTIGN PLRLIYHLYG VYYKGWEAKE LSERTAGRNL FTLIMFEAFE
LLGMDSQGKI RNLSGNYILD LIYGLHKQIN RGLKKMVLGW APAPFSCDWT PSDERIRLPT
DNYLRVETRC PCGYEMKAFK NVGGKLTKVE ESGPFLCRNR PGRGPVNYRV TKYYDDNLRE
IKPVAKLEGQ VEHYYKGVTA KIDYSKGKML LATDKWEVEH GVITRLAKRY TGVGFNGAYL
GDEPNHRALV ERDCATITKN TVQFLKMKKG CAFTYDLTIS NLTRLIELVH RNNLEEKEIP
TATVTTWLAY TFVNEDVGTI KPVLGERVIP DPVVDINLQP EVQVDTSEVG ITIIGRETLM
TTGVTPVLEK VEPDASDNQN SVKIGLDEGN YPGPGIQTHT LTEEIHNRDA RPFIMILGSR
NSISNRAKTA RNINLYTGND PREIRDLMAA GRMLVVALRD VDPELSEMVD FKGTFLDREA
LEALSLGQPK PKQVTKEAVR NLIEQKKDVE IPNWFASDDP VFLEVALKND KYYLVGDVGE
LKDQAKALGA TDQTRIIKEV GSRTYAMKLS SWFLKASNKQ MSLTPLFEEL LLRCPPATKS
NKGHMASAYQ LAQGNWEPLG CGVHLGTIPA RRVKIHPYEA YLKLKDFIEE EEKKPRVKDT
VIREHNKWIL KKIRFQGNLN TKKMLNPGKL SEQLDREGRK RNIYNHQIGT IMSSAGIRLE
KLPIVRAQTD TKTFHEAIRD KIDKSENRQN PELHNKLLEI FHTIAQPTLK HTYGEVTWEQ
LEAGVNRKGA AGFLEKKNIG EVLDSEKHLV EQLVRDLKAG RKIKYYETAI PKNEKRDVSD
DWQAGDLVVE KRPRVIQYPE AKTRLAITKV MYNWVKQQPV VIPGYEGKTP LFNIFDKVRK
EWDSFNEPVA VSFDTKAWDT QVTSKDLQLI GEIQKYYYKK EWHKFIDTIT DHMTEVPVIT
ADGEVYIRNG QRGSGQPDTS AGNSMLNVLT MMYGFCESTG VPYKSFNRVA RIHVCGDDGF
LITEKGLGLK FANKGMQILH EAGKPQKITE GEKMKVAYRF EDIEFCSHTP VPVRWSDNTS
SHMAGRDTAV ILSKMATRLD SSGERGTTAY EKAVAFSFLL MYSWNPLVRR ICLLVLSQQP
ETDPSKHATY YYKGDPIGAY KDVIGRNLSE LKRTGFEKLA NLNLSLSTLG VWTKHTSKRI
IQDCVAIGKE EGNWLVKPDR LISSKTGHLY IPDKGFTLQG KHYEQLQLRT ETNPVMGVGT
ERYKLGPIVN LLLRRLKILL MTAVGVSS
//
