RPOA_SHFV
ID RPOA_SHFV Reviewed; 3595 AA.
AC Q68772; P89132; Q87077;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 4.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Replicase polyprotein 1ab;
DE AltName: Full=ORF1ab polyprotein;
DE Contains:
DE RecName: Full=Nsp1-alpha papain-like cysteine proteinase;
DE EC=3.4.22.-;
DE AltName: Full=PCP1-alpha;
DE Contains:
DE RecName: Full=Nsp1-beta papain-like cysteine proteinase;
DE EC=3.4.22.-;
DE AltName: Full=PCP1-beta;
DE Contains:
DE RecName: Full=Nsp2 cysteine proteinase;
DE EC=3.4.22.-;
DE AltName: Full=CP2;
DE Short=CP;
DE Contains:
DE RecName: Full=Non-structural protein 3;
DE Short=Nsp3;
DE Contains:
DE RecName: Full=3C-like serine proteinase;
DE Short=3CLSP;
DE EC=3.4.21.-;
DE AltName: Full=Nsp4;
DE Contains:
DE RecName: Full=Non-structural protein 5-6-7;
DE Short=Nsp5-6-7;
DE Contains:
DE RecName: Full=Non-structural protein 5;
DE Short=Nsp5;
DE Contains:
DE RecName: Full=Non-structural protein 6;
DE Short=Nsp6;
DE Contains:
DE RecName: Full=Non-structural protein 7-alpha;
DE Short=Nsp7-alpha;
DE Contains:
DE RecName: Full=Non-structural protein 7-beta;
DE Short=Nsp7-beta;
DE Contains:
DE RecName: Full=Non-structural protein 8;
DE Short=Nsp8;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=Pol;
DE Short=RdRp;
DE EC=2.7.7.48;
DE AltName: Full=Nsp9;
DE Contains:
DE RecName: Full=Helicase;
DE Short=Hel;
DE EC=3.6.4.12;
DE EC=3.6.4.13;
DE AltName: Full=Nsp10;
DE Contains:
DE RecName: Full=Uridylate-specific endoribonuclease nsp11;
DE EC=4.6.1.-;
DE AltName: Full=Non-structural protein 11;
DE Short=Nsp11;
DE Contains:
DE RecName: Full=Non-structural protein 12;
DE Short=Nsp12;
GN Name=rep; ORFNames=1a-1b;
OS Simian hemorrhagic fever virus (SHFV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; Simarterivirinae;
OC Deltaarterivirus; Hedartevirus; Deltaarterivirus hemfev.
OX NCBI_TaxID=38143;
OH NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
OH NCBI_TaxID=9539; Macaca (macaques).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=LVR 42-0/M6941;
RA Maines T.R., Starling H.H., Methven S.L., Chen L., Kumar S.N.,
RA Geisbert J.B., Jahrling P.B., Brinton M.A.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE REVISION.
RA Vatter H., Di H., Donaldson E.F., Brinton M.A.;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2509-2548.
RX PubMed=8837898; DOI=10.1016/0168-1702(95)00093-3;
RA Chen Z., Plagemann P.G.W.;
RT "Detection of related positive-strand RNA virus genomes by reverse
RT transcription/polymerase chain reaction using degenerate primers for common
RT replicase sequences.";
RL Virus Res. 39:365-375(1995).
CC -!- FUNCTION: The replicase polyprotein 1ab is a multifunctional protein:
CC it contains the activities necessary for the transcription of negative
CC stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as
CC well as proteinases responsible for the cleavage of the polyprotein
CC into functional products.
CC -!- FUNCTION: The Nsp1 chain is essential for viral subgenomic mRNA
CC synthesis. {ECO:0000250}.
CC -!- FUNCTION: The 3C-like serine proteinase chain is responsible for the
CC majority of cleavages as it cleaves the C-terminus of the polyprotein.
CC {ECO:0000250}.
CC -!- FUNCTION: [Uridylate-specific endoribonuclease nsp11]: Plays a role in
CC viral transcription/replication and prevents the simultaneous
CC activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, and PKR
CC (By similarity). Acts by degrading the 5'-polyuridines generated during
CC replication of the poly(A) region of viral genomic and subgenomic RNAs.
CC Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-
CC cP) is first generated by 2'-O transesterification, which is then
CC hydrolyzed to a 3'-phosphate (3'-P) (By similarity). If not degraded,
CC poly(U) RNA would hybridize with poly(A) RNA tails and activate host
CC dsRNA sensors (By similarity). {ECO:0000250|UniProtKB:P0C6X7,
CC ECO:0000250|UniProtKB:P19811}.
CC -!- FUNCTION: The helicase chain, which contains a zinc finger structure,
CC displays RNA and DNA duplex-unwinding activities with 5' to 3'
CC polarity. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
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:
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=3.6.4.12;
CC -!- CATALYTIC ACTIVITY:
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: [Uridylate-specific endoribonuclease nsp11]:
CC Reaction=uridylyl-uridylyl-ribonucleotide-RNA = a 3'-end uridylyl-
CC 2',3'-cyclophospho-uridine-RNA + a 5'-end dephospho-ribonucleoside-
CC RNA; Xref=Rhea:RHEA:67732, Rhea:RHEA-COMP:13936, Rhea:RHEA-
CC COMP:17334, Rhea:RHEA-COMP:17335, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173079, ChEBI:CHEBI:173080;
CC Evidence={ECO:0000250|UniProtKB:P19811};
CC -!- SUBCELLULAR LOCATION: [Nsp2 cysteine proteinase]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 3]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein 5-6-7]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [3C-like serine proteinase]: Host cytoplasm
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasm,
CC host perinuclear region {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Helicase]: Host cytoplasm, host perinuclear
CC region {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Replicase polyprotein 1ab; Synonyms=pp1ab;
CC IsoId=Q68772-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=Q68772-2; Sequence=VSP_032894;
CC -!- DOMAIN: The hydrophobic domains (HD) could mediate the membrane
CC association of the replication complex and thereby alter the
CC architecture of the host cell membrane. {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages in vivo by its own proteases yield
CC mature proteins. There are two alternative pathways for processing.
CC Either nsp4-5 is cleaved, which represents the major pathway or the
CC nsp5-6 and nsp6-7 are processed, which represents the minor pathway.
CC The major pathway occurs when nsp2 acts as cofactor for nsp4 (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1ab]: Produced by -1
CC ribosomal frameshifting at the 1a-1b genes boundary.
CC -!- MISCELLANEOUS: [Isoform Replicase polyprotein 1a]: Produced by
CC conventional translation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the arteriviridae 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; AF180391; AAA68933.3; -; Genomic_RNA.
DR EMBL; AF180391; AAB63390.4; -; Genomic_RNA.
DR EMBL; U28864; AAB40002.1; -; mRNA.
DR RefSeq; NP_203542.2; NC_003092.2.
DR RefSeq; YP_009109556.3; NC_003092.2. [Q68772-1]
DR SMR; Q68772; -.
DR MEROPS; C32.002; -.
DR PRIDE; Q68772; -.
DR GeneID; 22220025; -.
DR KEGG; vg:22220025; -.
DR Proteomes; UP000106311; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0019082; P:viral protein processing; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd21410; 1B_av_Nsp10-like; 1.
DR CDD; cd21160; NendoU_av_Nsp11-like; 1.
DR CDD; cd21166; NTD_av_Nsp11-like; 1.
DR CDD; cd21405; ZBD_av_Nsp10-like; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.1330.220; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.90.70.70; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR031932; Arteri_nsp7a.
DR InterPro; IPR038451; Arteri_nsp7a_sf.
DR InterPro; IPR008743; Arterivirus_Nsp2_C33.
DR InterPro; IPR023338; Arterivirus_NSP4_peptidase.
DR InterPro; IPR008741; AV_PCPalpha.
DR InterPro; IPR025773; AV_PCPbeta.
DR InterPro; IPR038154; AV_PCPbeta_sf.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR008760; EAV_peptidase_S32.
DR InterPro; IPR037227; EndoU-like.
DR InterPro; IPR043609; NendoU_nidovirus.
DR InterPro; IPR044863; NIRAN.
DR InterPro; IPR044348; NSP10_1B_Av.
DR InterPro; IPR027355; NSP10_Av_ZBD.
DR InterPro; IPR044320; NSP11_Av_N.
DR InterPro; IPR044314; NSP11_NendoU_Av.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF16749; Arteri_nsp7a; 1.
DR Pfam; PF19215; CoV_NSP15_C; 1.
DR Pfam; PF05411; Peptidase_C32; 2.
DR Pfam; PF05412; Peptidase_C33; 1.
DR Pfam; PF05579; Peptidase_S32; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR SUPFAM; SSF142877; SSF142877; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51538; AV_CP; 1.
DR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1.
DR PROSITE; PS51493; AV_NSP4_PRO; 1.
DR PROSITE; PS51539; AV_PCP_ALPHA; 1.
DR PROSITE; PS51540; AV_PCP_BETA; 1.
DR PROSITE; PS51652; AV_ZBD; 1.
DR PROSITE; PS51958; NENDOU; 1.
DR PROSITE; PS51947; NIRAN; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Endonuclease; Helicase; Host cytoplasm; Host membrane;
KW Hydrolase; Lyase; Membrane; Metal-binding; Nuclease; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; Reference proteome;
KW Ribosomal frameshifting; RNA-directed RNA polymerase; Serine protease;
KW Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW Viral RNA replication; Zinc; Zinc-finger.
FT CHAIN 1..3595
FT /note="Replicase polyprotein 1ab"
FT /id="PRO_0000036709"
FT CHAIN 1..?
FT /note="Nsp1-alpha papain-like cysteine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036711"
FT CHAIN ?..350
FT /note="Nsp1-beta papain-like cysteine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036712"
FT CHAIN 351..1236
FT /note="Nsp2 cysteine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036713"
FT CHAIN 1237..1463
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036714"
FT CHAIN 1464..1664
FT /note="3C-like serine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036715"
FT CHAIN 1665..2055
FT /note="Non-structural protein 5-6-7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036716"
FT CHAIN 1665..1830
FT /note="Non-structural protein 5"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423138"
FT CHAIN 1831..1843
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423139"
FT CHAIN 1844..1999
FT /note="Non-structural protein 7-alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423140"
FT CHAIN 2000..2055
FT /note="Non-structural protein 7-beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423141"
FT CHAIN 2056..2746
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036717"
FT CHAIN 2056..2104
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036718"
FT CHAIN 2746..3195
FT /note="Helicase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036719"
FT CHAIN 3196..3418
FT /note="Uridylate-specific endoribonuclease nsp11"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036720"
FT CHAIN 3419..3595
FT /note="Non-structural protein 12"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036721"
FT TRANSMEM 922..942
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 951..971
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1019..1039
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1239..1259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1316..1336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1345..1365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1381..1401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1673..1693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1711..1731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1744..1764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1784..1804
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 56..164
FT /note="Peptidase C31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT DOMAIN 239..350
FT /note="Peptidase C32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT DOMAIN 633..736
FT /note="Peptidase C33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT DOMAIN 1464..1664
FT /note="Peptidase S32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT DOMAIN 2083..2253
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 2491..2625
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 2746..2812
FT /note="AV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT DOMAIN 2862..3022
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 3023..3157
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 3196..3292
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 3294..3416
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ZN_FING 3..23
FT /note="C4-type; atypical"
FT REGION 482..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..1039
FT /note="HD1"
FT REGION 1239..1399
FT /note="HD2"
FT REGION 1687..1804
FT /note="HD3"
FT COMPBIAS 848..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 63
FT /note="For Nsp1-alpha papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT ACT_SITE 130
FT /note="For Nsp1-alpha papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT ACT_SITE 246
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT ACT_SITE 309
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT ACT_SITE 378
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT ACT_SITE 430
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT ACT_SITE 1502
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 1527
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 1580
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 3325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 3340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 3369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT BINDING 2752
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2755
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2765
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2770
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2773
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2777
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2779
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2782
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2789
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2791
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2798
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2801
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2897..2904
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 164..165
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255"
FT SITE 350..351
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255"
FT SITE 1236..1237
FT /note="Cleavage; by CP2"
FT /evidence="ECO:0000250"
FT SITE 1463..1464
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 1664..1665
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 1830..1831
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 1843..1844
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 1999..2000
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 2055..2056
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 2745..2746
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 3195..3196
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 3418..3419
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT VAR_SEQ 2105..3595
FT /note="Missing (in isoform Replicase polyprotein 1a)"
FT /evidence="ECO:0000305"
FT /id="VSP_032894"
SQ SEQUENCE 3595 AA; 391443 MW; 75E2CB1BE0242E18 CRC64;
MFCECPRSNL VVMCSGAFCC VLCGHRRRPR PASESDRAKY GPIVQYVEAR VAHVYSGLEG
RYCALEMIPI TYGNKFPYCK PLPVSFVIKT LAGVQGDLTR LEETPLPGGY GVIPCWGPHL
AAVGYLSPAH VGRDWFEGAT HAIVHIGSYG GHERPTTIPF NTTGGDVYQL GTCTIVETID
HVEWHAGVKP GTAICPLDRI DFAQKVITAF PEGFLANKAW LGDKRGTLKV EADPETAALS
FEHGRCWLKL FPDPACELTT ASTFGYQLNC GVQGKYIARR LQTNGLKLVQ NQEGKFIAYT
FHRGSWLGHI GHADESVPPD CQIIARFDVL PYNEWSPLPL LKLPGKTYFG GNASSVSWPE
WKYDEQLLYA DSLTAGFCWL QLFPPLSRKS EAQRAILAQQ VNNYGVTGTY LEYRLRQYGI
VLAECDYGEH YIYAAASDSS IRHISPVPIH DRHHVFVTRL TARFGAFDEG FDLGFGTRYG
RRRGGGKKSG QSSGVRAPGR TTPDLAGDWG KAVDDQEKTA SKVTTDKAMS TSEPAVVQVG
CETKPVADAA AVPASVNSTG CALLPVQADP CCTAGVAAKE SEPKAVAAPS IPITFGAPAG
ETLPVAASPL VVKKDKRCIS VKLTAKKALP KETFIPPPDG GCGVHAFAAI QYHINTGHWP
EQKPVVNWAY EAWTTNEDIG HMICSTETPA ALEPCLHARY VVRLDSDHWV VDHYPNRPMC
FVEACAHGWC SSLLSEPTGE EGEHLVDCSA LYDCLGKFRN GTEFADTVLG LSKTAHCCNK
RVPTPRKQAI MSLLNRPNCV PCIAPPSQVR TVDPSQPAAP LPPVPRPRKR KAAAQQVSKV
PSEQDPSLAH DPPEKPDSVR PPKLGYLDRA WNNMLARTHK LHNLQQRVFG LYPQLLSMLL
PSGARPSTPR LLGCYFSMAV AMFFLFLGSP LFILCAVLAG VIAPSARYPK ILCCCLVVVY
ICTLFADAIS SVCDNDDADC RAFLSDLGDR YSTNQPVYIT PGPATFFLAV SRNFFVVSVA
LFPLHLLLLM VDVLLVIGVL CMDGYCFRCF SRCVRKAPEE VSLLTIPQSR VSRRFLLDIC
DFYSAPPVDI IRLATGLNGC FRGDYSPIGS STSVITADKI DVKKVSCRTV CSFPSCPSEA
VKVLHVLSVR GQMCAHNEQK VEKVDALPCK NPLFPYDLSS KKIVPVDSGT YEILSSIGCD
MSHLVIGDGD FFKVMGVPRP SPFTVMRLRA CRVVGGGRIF RTALAAAWVL FFVCAGYWVQ
MSTPCGIGTN DPFCKSSFGV PTYVNQGVCH GQYCASSKGV SRATSILTVR NPAVAPYIVL
AACLVYLASV YVPGIIEVSL LVLNALLPAG PAISALRTLV MIIAAPHLSM KYIAFFCCTT
AFVDFTSVVV VLTALLVGWI LARYTGIGGF VTPYDIHDVV KSQRDGVAVA NAPPNTYLGA
VRRAALTGKP AFFVANNTGI VLEGLLREKT RASNSVSVYG VTCGSGGLFS DGNNTVCLTA
THVCGNNKAV VDYQGTRYEA VFTTKGDYAS AVVPIPGAFP PLKFAPQSYT GRAYWYANTG
VETGFVGTTG CLVFSGPGDS GSPIITPDGL IVGVHTGSDS KGSGAYTTPN GLTVSGPLSL
KEMGAHYEGP IVDVPTRLPR NVHNDTKSVP QPLARLLESS INLEGGLGTI QLIIVAVVLW
KYAVDPLSIP FVVAFFLLNE ILPKCLIRCF YNYSLFCLAA FSPLASRIFF IRLLTAALNR
NPTALICHAC FAGIAVLNDF IILGDIRLAL RFTSFYVVGV NHDAIAIAVI GALVCVAACC
LELFGLPQMA SVIGCHGSFD PTFLSRYVHE GIRQGVSSGF GTESLSTALA CALSEDELNF
LAQAVDHKAI VSAIHVHKTL QDYILSKNAK ILRASLASVH ANHNASKALA SLDKFLQGTS
TQLKPGDPVI LLGSTSAELV SVFSGDSEYI AEPIRSHPVA GTICTLCVVQ AKCEGGLVTQ
VNGKFSPAKY LAVAGKVLAD HPDYKLENDG RFPRTREDRV KDSVQVDTVD IGSHTFKKMW
NKTTGDVWYD IIMPESAANP LAVHDLDSAV AAIGMSKEIP EKDMNRLRAI ISKLQGLVSS
EALNLLTAAG CTSADRSGLV ITLDYAKIIT HHARTRAFSS IDFKVVSPDE AMRTARLSPS
PQPIIASFSD DKFLLLRRHP PSLLDVLTKG LDATCREPLH SPGDQGIDGY LWDFEAPHSK
EAIWLSNQII SACAARRGDA PGCYPYKLHP VRGDPYRVGN VLKNTRFGDV TYTAVSDSDS
PWLKVASINS GGCPVVTDRV LGSTIPVGSE IYLPTLPESV LDYLDSRPDC PTYYTQHGCE
AAALQDLKKF NLSTQGFILP EVLNIVRNYL LGTIGYRPAI YKPSTVPSND SHAGINGLSF
STKTLQALPD IDELCEKAIA EVWQTVTPVT LKKQFCSKAK TRTILGTNAM ASLALRALLS
GVTQGFQLAG KNSPICLGKS KFDPCTFEVK GRCLETDLAS CDRSTPAIVR HFATKLLFEM
ACAERALPLY VVNCCHDLIV TQTSAATKRG GLSSGDPVTS IANTIYSLVL YVQHMVLTLL
ENGHPLSLKF LSGKLNFQDL YKLQAFIVYS DDLILLNESD DLPNFERWVP HLELALGFKV
DPKKTVITSN PGFLGCEYRH GWLVPQKQRV LAALAYHVNA KDVHTYYINA TAILNDASAL
SAFEPDWFDD LVIGLADCAR KDGYSFPGPA AFREFFSRVS GYQFEGKEVQ VCSICCSTAR
TTSLCGMALC DFCAHRHYHP GCHVLSSFCK HVIGSNTCKM CSIPILKDRT KFAELLASDQ
YRSVCTVEVT VVDGYTDAAP GRYSYQKKQY MLRKERRGCP LDLPDGKYSM KLLPNSCSGI
CVPKAQENAT LSNFVVGPPG SGKTTFISNL LDDDAVVYCP THVSLIAYSK SLPAARFSVP
RGQDPAEYGT PALSGPTLQL LSAGYVPGAK HYLDEACYAN PFDVFKLLSK TPITAIGDPA
QLTPVGFDTP LYVFELMKKN ALHAIYRFGQ NICNAIQPCY STKLVSQRQG DTEVIFQTKF
APRGKVLTPY HRDRVGAAVT IDSSQGSTYD VVTLYLPTKG SLTLARGLVG ITRARERLYV
YDPHHQLAKY FNLQPSSTTI RPHAVVIDGK ARVMLSDKCY AAPEDFPGML CTARPATAAD
RKILEETCLK LDFLESGSLS PLPRVCYNLG FYYSPDITKL LPIPSELAKH WPVATNRNNP
EWPNRLVVSA TRLSPLSHPA VCAGYYVGDS LFVGTPNVTS YWLTKFLDGR AVPMEDSVYS
TGRFEMDIRD YLDSAERDFA AKHPHAFIGD TKGTTVGGCH HITSQYLPHV LPADSVVKVG
VSKPGVAHKA LCTVTDIYLP MLGSYTSPPT QSKVYKVNVD HKACKLMVWR DQTMYFQEGF
DYHTLVDALR FVRLSSDGVY RVAPELTPMI GNRRLDLGAK PLRPVDLAIT PWDDPKCEFL
VTHASPFDMS DEFLLVNAFD FIKEDLLGKS VTPVYFYKRL SEPLHFDQNL PPHVGAILSK
APRFISLAKV FNFCFTPTAC HCKVSVKTAT GDHMCKCSLS SDEFLSRFNP TVGTP
