RPOA_LDVC
ID RPOA_LDVC Reviewed; 3637 AA.
AC Q06502; Q06503;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
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 Lactate dehydrogenase elevating virus (strain C) (LDV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Arnidovirineae; Arteriviridae; Variarterivirinae;
OC Gammaarterivirus; Gammaarterivirus lacdeh.
OX NCBI_TaxID=300015;
OH NCBI_TaxID=10092; Mus musculus domesticus (western European house mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8389075; DOI=10.1006/viro.1993.1298;
RA Godeny E.K., Chen L., Kumar S.N., Methven S.L., Koonin E.V., Brinton M.A.;
RT "Complete genomic sequence and phylogenetic analysis of the lactate
RT dehydrogenase-elevating virus (LDV).";
RL Virology 194:585-596(1993).
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: 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 -!- 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 -!- 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=Q06502-1; Sequence=Displayed;
CC Name=Replicase polyprotein 1a; Synonyms=pp1a, ORF1a polyprotein;
CC IsoId=Q06502-2; Sequence=VSP_032888;
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA74104.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L13298; AAA74103.1; -; Genomic_RNA.
DR EMBL; L13298; AAA74104.1; ALT_INIT; Genomic_RNA.
DR SMR; Q06502; -.
DR PRIDE; Q06502; -.
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:0070008; F:serine-type exopeptidase 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; 3.30.40.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.90.70.60; -; 1.
DR Gene3D; 3.90.70.70; -; 1.
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; IPR038155; AV_PCPalpha_sf.
DR InterPro; IPR025773; AV_PCPbeta.
DR InterPro; IPR038154; AV_PCPbeta_sf.
DR InterPro; IPR023183; Chymotrypsin-like_C.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR022230; DUF3756.
DR InterPro; IPR008760; EAV_peptidase_S32.
DR InterPro; IPR037227; EndoU-like.
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; PF12581; DUF3756; 1.
DR Pfam; PF05410; Peptidase_C31; 1.
DR Pfam; PF05411; Peptidase_C32; 1.
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 3: Inferred from homology;
KW ATP-binding; Endonuclease; Helicase; Host cytoplasm; Host membrane;
KW Hydrolase; Lyase; Membrane; Metal-binding; Nuclease; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; Ribosomal frameshifting;
KW RNA-directed RNA polymerase; Serine protease; Thiol protease; Transferase;
KW Transmembrane; Transmembrane helix; Viral RNA replication; Zinc;
KW Zinc-finger.
FT CHAIN 1..3637
FT /note="Replicase polyprotein 1ab"
FT /id="PRO_0000036631"
FT CHAIN 1..?
FT /note="Nsp1-alpha papain-like cysteine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036633"
FT CHAIN ?..380
FT /note="Nsp1-beta papain-like cysteine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036634"
FT CHAIN 381..1284
FT /note="Nsp2 cysteine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036635"
FT CHAIN 1285..1510
FT /note="Non-structural protein 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036636"
FT CHAIN 1511..1712
FT /note="3C-like serine proteinase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036637"
FT CHAIN 1713..2181
FT /note="Non-structural protein 5-6-7"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036638"
FT CHAIN 1713..1898
FT /note="Non-structural protein 5"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423110"
FT CHAIN 1899..1914
FT /note="Non-structural protein 6"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423111"
FT CHAIN 1915..2046
FT /note="Non-structural protein 7-alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423112"
FT CHAIN 2047..2181
FT /note="Non-structural protein 7-beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000423113"
FT CHAIN 2182..2864
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036639"
FT CHAIN 2182..2226
FT /note="Non-structural protein 8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036640"
FT CHAIN 2865..3293
FT /note="Helicase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036641"
FT CHAIN 3294..3515
FT /note="Uridylate-specific endoribonuclease nsp11"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036642"
FT CHAIN 3516..3637
FT /note="Non-structural protein 12"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036643"
FT TRANSMEM 940..960
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 981..1001
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1083..1103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1287..1307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1362..1382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1390..1410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1423..1443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1735..1755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1761..1781
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1801..1821
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1824..1844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1853..1873
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 69..181
FT /note="Peptidase C31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT DOMAIN 262..381
FT /note="Peptidase C32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT DOMAIN 381..486
FT /note="Peptidase C33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT DOMAIN 1511..1712
FT /note="Peptidase S32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT DOMAIN 2214..2372
FT /note="NiRAN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01292"
FT DOMAIN 2611..2745
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT DOMAIN 2865..2928
FT /note="AV ZBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT DOMAIN 2985..3137
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 3138..3269
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 3293..3389
FT /note="AV-Nsp11N/CoV-Nsp15M"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01306"
FT DOMAIN 3391..3513
FT /note="NendoU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ZN_FING 8..28
FT /note="C4-type; atypical"
FT REGION 69..183
FT /note="PCP1-alpha"
FT REGION 262..380
FT /note="PCP1-beta"
FT REGION 676..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1103
FT /note="HD1"
FT REGION 1287..1446
FT /note="HD2"
FT REGION 1735..1872
FT /note="HD3"
FT COMPBIAS 690..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 76
FT /note="For Nsp1-alpha papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT ACT_SITE 147
FT /note="For Nsp1-alpha papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00872"
FT ACT_SITE 269
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT ACT_SITE 340
FT /note="For Nsp1-beta papain-like cysteine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00873"
FT ACT_SITE 390
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT ACT_SITE 456
FT /note="For Nsp2 cysteine proteinase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00871"
FT ACT_SITE 1549
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 1574
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 1626
FT /note="Charge relay system; for 3C-like serine proteinase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00826"
FT ACT_SITE 3422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 3437
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT ACT_SITE 3466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01303"
FT BINDING 2871
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2874
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2892
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2905
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2914
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 2917
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00985"
FT BINDING 3013..3020
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 181..182
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255"
FT SITE 381..382
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255"
FT SITE 1284..1285
FT /note="Cleavage; by CP2"
FT /evidence="ECO:0000250"
FT SITE 1510..1511
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 1712..1713
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 1898..1899
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 1914..1915
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 2046..2047
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 2181..2182
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 2864..2865
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 3293..3294
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT SITE 3515..3516
FT /note="Cleavage; by 3CLSP"
FT /evidence="ECO:0000250"
FT VAR_SEQ 2227..3637
FT /note="Missing (in isoform Replicase polyprotein 1a)"
FT /evidence="ECO:0000305"
FT /id="VSP_032888"
FT UNSURE 1698
FT /note="S or P"
FT UNSURE 2243
FT /note="S or F"
SQ SEQUENCE 3637 AA; 398663 MW; 186FAFAFA5BCA311 CRC64;
MQSGFDRCLC TPNARVFWER GQVYCTRCLA ARPLLPLSQQ HPRLGALGLF YRPASPLSWE
APVTYPTKEC RPGGMCWLSS IYPIARMTSG NHNFQARLNF IASVVYRDGK LTSKHLEEDF
EVYSRGCRWY PITGPVPGIA LYANAVHVSD ESFPGATHVL SNLPLPQQPL RKGLCPFADA
RANVWRYKGN TVFVSPQGYL WTTGSNDSVP EPWGEDRRLC EKIISSLPAD HLVKINFSNY
PFDYSFTGGD GAGFVVFPCK ERDTKFSKCW EKIFEDHSGW MAACEEADLA DRMGYRTPAG
VAGPYLARRL QVRGLRAVVK PENNDYIVWA LGVPESYIRH VSRAGEPVEE FFVKVGEFSI
VSNCVVTPHP KFRFQTRKYY GYSPPGDGAC GLHCISAMLN DIFGDSFTTR LGKCSRDSSE
WLSDQDLYQL VMTANLPATI GHCPSAIYKL DCVNQHWTVT KRKGDRAVGR LAPDCLRGVC
GECEMGIHIG ADTDLSPIVE LQLAQDVSPR PGALLWFLEL HELCVVDDDF AHAIARAGEE
YRRAMGIPRD DWVILAELMT ENCRTRHQVL EKLQRGLQLQ ASSRPSSPAS VSPASSVDLS
AAGLLLSGTE SDKEAVVAVN DGCYTVLGFD KNEATKSEQD LATDLFCDLV KPMETSTTKL
ESRKILEAAA KALESCKPKR KRSRKKKTRT PSPTCSVDAA VAEPTSVNSL GNQDTRETCA
SEKKAEKCPT PTPPPRPKRA ALKNSNSGCV LKDIIWNQTG PGVKCLTIVE DVRAFLKGIT
PPGGVLSTRS RITKHIVDHF HSICEQTPEL VLAHAEHQAK NLHELLASET AKLILGIGED
PLKKLVGSQR SLPRRLGFGA WLGGQQKTSG GCGEREFKDV GRKSGAERTP SKRDLGVSLG
DQLSQDGARR LSSSTACEIK ESVPPIIDSG GGLSQKFMAW LNHQVFVLSS HLLAVWSFIF
GSRQVLGVFD YVYTLFCLCC VLLCFYLPAI GFMTLVGCVF GSPWRVRLSV FSVWLCVAVV
VFQEVLPEPG AVCTSASAER AAALERYTSN GVHRPVNHLS VGLVGTVAGF VARSVGGPRR
YWFYFLRLMV LLDLGLVFLA VALRGSCKKC FCKCVRTASH EVQLRVFPST KVARTTLEAI
CDMYSAPRVD PIFIATGVRG CWTGSVSPHQ VTEKPVSYSN LDDKKISNKT VVPPPTDPQQ
AVRCLKVLQC GGSIQDVSVP EVKKVTKVPF KAPFFPNVTI DPECYIVVDP VTYSAAMRGG
YGVSHLIVGL GDFAEVNGLR FVSGGQIADF VCLGLYVLLN FLLSAWLSSP VSCGRGTNDP
WCRNPFSYPV VGQGVMCNSH LCVAEDGLTS PMTLSYSLID WALMVAIMAT VAIFFAKISL
LVDVVCVFCC LLMYAFPSLS IAAFGFPFVL CKVSLHPITL VWVQFFLLAV NVWAGVASVV
VLISSWFLAR ATSSLGLITP YDVHMITATP RGASSLASAP EGTYLAAVRR SALTGRCCMF
VPTNFGSVLE GSLRTRGCAK NVVSVFGSAS GSGGVFTING NPVVVTASHL LSDGKARVSC
VGFSQCLDFK CAGDYAFARV ANWKGDAPKA ELSHRRGRAY CSPLVGLSLD LLGKNSAFCF
TKCGDSGSPV VDEDGNLLGI HTGSNKRGSG MVTTHGGKTL GMANVKLSEM CPHYSGPGVP
VSTVKLPKHL VVDVETVSSD LVAVVESLPA LEGALSSMQL LCVFFFLWRL IHVPDVPVIR
IAFFFLNEIL PVMLARLMFS FALSLFFCVH WLFCSSVAVA FGDCCSKSVT GYSVQVLLLR
LVIAALNRPC GPFGFSLLGQ LSQCCLMLCL LDIELQLLGC LYLGQLLMWP PKEIFFHPTG
QFMFLPLFLS LFKRNALADM LVGNGCFDAA FFLKYFAEGN LRDGVSDSCN MTPEGLTAAL
AITLSDDDLE FLQRHSEFKC FVSASNMRNG AKEFIESAYA RALRAQLAAT DKIKASKSIL
AKLESFAGGV VTQVEPGDVV VVLGKKVIGD LVEVVINDAK HVIRVIETRT MAGTQFSVGT
ICGDLENACE DPSGLVKTSK KQARRQKRTG LGTEVVGTVV IDGVSYNKVW HIATGDVTYE
GCLVTENPQL RPLGMTTIGR FQEFIRKHGE KVKTSVEKYP VGKKKSVEFN ITTYLLDGEE
YDVPDHEPLE WTITIGESDL EAERLTVDQA LRHMGHDSLL TAKEKEKLAR IIESLNGLQQ
ASALNCLATS GLDRCTRGGL TVSGDAVKLV RYHSRTFSIG DVNLKVMGRE EYGRTVGKQG
HCLVANLVDG VVVMRKHEPS LVDVLLTGED ADLISPTHGP GNTGVHGFTW DFEAPPTDLE
LELSEQIITA CSIRRGDAPS LDLPYKLHPV RGNPYRDRGV LYNTRFGDIK YLTPQKTKEP
LHAAACFNPK GVPVSDSETL VATTLPHGFE LYVPTIPQSV LEYLDSRPMH RKCCVRAVVR
GLAECDLQKF DLSRQGFVLP GVLYMVRRYL CRLVGIRRRL FLPSTYPAKN SMAGINGNRF
PTHVVQSHPD IDALCERACK EHWQTVTPCT LKKQYCSKAK TRTILGTNNF VALGLRSALS
GVTQGFMRKG IGSPICLGKN KFTPLPTKVS GRCLEADLAS CDRSTPAIIR WFTTNLLFEL
AGPEEWIPSY VLNCCHDAVS TMSGCFDKRG GLSSGDPVTS VSNTVYSLVI YAQHMVLSAF
RCGHKVGGLF LRDSLEMEQL FELQPLLVYS DDVVLYDESS ELPNYHFFVD HLDLMLGFKT
DRSKTVITSD PQFPGCRIAA GRVLVPQRDR ILAALAYHMK ASCVSDYFAS AAAILMDACA
CCDYDEDWYF DLVCGIADCA RKEGFRFPGP SFYVDMWKRL SVEEKKKCRT CAHCGAPSTL
VSSCGLNLCD YHGHGHPHCP VVLPCGHAVG SGVCDGCSSP VMSLNTELDK LLACVPYHPP
KVELLSVNDG VSSLPPGRYQ ARGGVVSVRR DILGNVVDLP DGDYQVMKVA QTCADICMVS
INSHILRSQF ITGAPGTGKT TYLLSVVRDD DVIYTPTHRT MLDVVKALGT CRFDPPKDTP
LEFPVPSRTG PCVRLIRAGF IPGRVSYLDE AAYCNPLDVL KILSKTPLVC VGDLNQLPPV
DFIGPCYAFA LMLGRQLIEV FRFGPSIVNP IKKFYREELV SRGPDTGVKF LKSYQPYGQV
LTPYHRDRVD GAITIDSSQG CTYDVITVYL PTPKSLNSAR ALVAITRARF YVFVYDPHNQ
LEQYLNMSEH EPAGAVAFWC GEQPMMISEG RVQRLSGPAQ TTDPKLQQLM GLEGTASPLP
QVAHNLGFYY SPDLVQFARI PSELCKHWPV VTAQNRTDWP DRLVCSMSKI DKCSRAIFCA
GYHVGPSVFL GVPGVVSYYL TKFLKGKPVP LPDSLMSTGR IALNVREYLD EKEMEFSSRC
PHAFIGEVKG SNVGGCHHVT SRYLPPVLVP GSVVKIGVSC PGKAAKELCT VTDVYLPELD
PYLNPPTKSM DYKLLVDFQP VKLMVWKDAT AYFHEGIRPM ESMSRFLKVP QEEGVFFDLD
EFVTNAKVSK LPCKYSVSAN QFLTDVVLSM THPSLAPPDY ELLFARAYCV PGLDVGTLNA
YIYRRGPSTY TTSNIARLVK DICCPVGCKG SGYMFPK
