ID   POL1_APMV               Reviewed;         729 AA.
AC   Q02941;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=RNA1 polyprotein;
DE   AltName: Full=Genome polyprotein B;
DE   AltName: Full=P1;
DE   Contains:
DE     RecName: Full=Picornain 3C-like protease;
DE              Short=3C-like protease;
DE              EC=3.4.22.-;
DE     AltName: Full=24 kDa protein;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase {ECO:0000255|PROSITE-ProRule:PRU00539};
DE              EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE     AltName: Full=87 kDa protein;
DE   Flags: Fragment;
OS   Andean potato mottle virus (APMV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Secoviridae; Comovirinae; Comovirus.
OX   NCBI_TaxID=12259;
OH   NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=C;
RX   PubMed=8429307; DOI=10.1099/0022-1317-74-2-315;
RA   Krengiel R., Vicente A.C.P., Weyne M., Shindo N., Brioso P.S.T.,
RA   Felix D.B., Villaroel R., de Oliveira D.E., Timmerman B.;
RT   "Molecular cloning and sequence analysis of a segment from Andean potato
RT   mottle virus B RNA encoding the putative RNA polymerase.";
RL   J. Gen. Virol. 74:315-318(1993).
CC   -!- FUNCTION: [Picornain 3C-like protease]: Thiol protease that cleaves the
CC       RNA1 and RNA2 polyproteins. {ECO:0000250|UniProtKB:P03600}.
CC   -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genome.
CC       {ECO:0000250|UniProtKB:P03600}.
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   -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host endoplasmic
CC       reticulum {ECO:0000250|UniProtKB:P03600}.
CC   -!- PTM: [RNA1 polyprotein]: Specific enzymatic cleavages by picornain 3C-
CC       like protease in vivo yield mature proteins. Picornain 3C-like protease
CC       is autocatalytically processed. {ECO:0000250|UniProtKB:P03600}.
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DR   EMBL; M84806; AAA42422.1; -; Genomic_RNA.
DR   PIR; JQ1898; JQ1898.
DR   SMR; Q02941; -.
DR   GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 3.30.70.270; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR044067; PCV_3C_PRO.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF00680; RdRP_1; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51874; PCV_3C_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   Covalent protein-RNA linkage; Host endoplasmic reticulum; Hydrolase;
KW   Nucleotide-binding; Nucleotidyltransferase; Protease;
KW   RNA-directed RNA polymerase; Thiol protease; Transferase;
KW   Viral RNA replication.
FT   CHAIN           <1..729
FT                   /note="RNA1 polyprotein"
FT                   /id="PRO_0000445833"
FT   CHAIN           <1..26
FT                   /note="Picornain 3C-like protease"
FT                   /id="PRO_0000036999"
FT   CHAIN           27..729
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000037000"
FT   DOMAIN          <1..21
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          299..429
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   SITE            26..27
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000250|UniProtKB:P03600"
FT   NON_TER         1
SQ   SEQUENCE   729 AA;  82621 MW;  AAC3E05AB2218D7B CRC64;
     GIHVAGGRGK GYACLMPPLR PKAQAQSAQE HFEIFPYEQE TNAGLALVGE LKQGVYVSCP
     TKTSFERTPE SYHLGLPCEK EPSILSSHDP RIPEHVEGYC PFRAGIQKYA NPMGHLDHDL
     MYEVAHDMQE SWHDCVQDFT FPEVDLETAI NGIDMVEYME CIPKSTSEGF PHVLSRAPGE
     KGKMRFLEGD GEKFSLREGT SVKKAYDLLQ EEIDRSVPTL VAIECPKDEK LPLRKIYTSP
     KTRCFSILPM EYNLLVRQKF LHFVRFMMKR RDVLPSQVGV NPYSLEWGAI ARRLQEVGNS
     ILCCDYSSFD GLMSSQVMSC IADTMNDFMG GDVSLKRQRK NLLMACCSRF SVVKGNVWRV
     EGGIPSGFPL TVVMNGIFNE LLVRYCFKKI MREGGATPLE CSAFDSYIRF VVYGDDNLIS
     VSPVIHDKFN GKLLKECMAR FGVTITDGKD KTLPTLEFRP LEDCDFLKRG FIQRSELVWD
     APEERSSLYT QLHYVSTKMQ SLEDAYTGNL VNVIRELYMH SPKEASDLRR KALRDLPWLS
     RSKIGTMENV QAFYAMQRAG YRMDESIDVI CDLAKLGKYV KGEACKEIVW LTPTVGACDL
     RYFDWQNAKV DEFWVLCQTN YHEFDENRVM QLCWTPGSGR GGLPTAHWLR TCMLLEKGNV
     RKKLHWAMAE KKKIIFCAKG GVLIPTVMAG IFLSKEDPML NLAGVSTLTC AMESVKTLGF
     LKEGNLNLF