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 24-JUL-2024, entry version 187. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 iPTMnet; P19711; -. 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:0050780; F:dopamine receptor binding; IEA:TreeGrafter. 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:symbiont-mediated suppression of host 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:0019049; P:virus-mediated perturbation of host defense response; 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-like. 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 InterPro; IPR052317; Viral_replicn-host_int_reg. 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 //