ID   POL1_CRLVP              Reviewed;        2250 AA.
AC   Q6EWG9;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=RNA1 polyprotein;
DE   AltName: Full=Genome polyprotein B;
DE   AltName: Full=P1;
DE   Contains:
DE     RecName: Full=Protease cofactor;
DE   Contains:
DE     RecName: Full=Putative helicase;
DE              EC=3.6.4.-;
DE     AltName: Full=Membrane-binding protein;
DE     AltName: Full=NTP-binding protein;
DE              Short=NTB;
DE   Contains:
DE     RecName: Full=Viral genome-linked protein;
DE     AltName: Full=VPg;
DE   Contains:
DE     RecName: Full=Picornain 3C-like protease;
DE              Short=3C-like protease;
DE              EC=3.4.22.-;
DE   Contains:
DE     RecName: Full=RNA-directed RNA polymerase;
DE              EC=2.7.7.48;
OS   Cherry rasp leaf virus (isolate Potato/United States) (CRLV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Secoviridae; Cheravirus.
OX   NCBI_TaxID=650137;
OH   NCBI_TaxID=230209; Balsamorhiza sagittata.
OH   NCBI_TaxID=3750; Malus domestica (Apple) (Pyrus malus).
OH   NCBI_TaxID=29818; Plantago major (Common plantain).
OH   NCBI_TaxID=42229; Prunus avium (Cherry) (Cerasus avium).
OH   NCBI_TaxID=3760; Prunus persica (Peach) (Amygdalus persica).
OH   NCBI_TaxID=50225; Taraxacum officinale (Common dandelion) (Leontodon taraxacum).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15503203; DOI=10.1007/s00705-004-0362-3;
RA   Thompson J.R., Perry K.L., De Jong W.;
RT   "A new potato virus in a new lineage of picorna-like viruses.";
RL   Arch. Virol. 149:2141-2154(2004).
CC   -!- FUNCTION: Picornain 3C-like protease is a thiol protease that probably
CC       cleaves the B and M polyproteins.
CC   -!- FUNCTION: Viral genome-linked protein (VPg) plays a role in RNA
CC       replication. {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   -!- SUBCELLULAR LOCATION: [Putative helicase]: Host membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- PTM: Specific enzymatic cleavages by picornain 3C-like protease in vivo
CC       yield mature proteins. Picornain 3C-like protease is autocatalytically
CC       processed (By similarity). {ECO:0000250}.
CC   -!- PTM: Viral genome-linked protein (VPg) is uridylylated by the
CC       polymerase and is covalently linked to the 5'-end of genomic RNA. This
CC       uridylylated form acts as a nucleotide-peptide primer for the
CC       polymerase (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the comoviridae genome polyprotein B family.
CC       {ECO:0000305}.
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DR   EMBL; AJ621357; CAF21713.1; -; Genomic_RNA.
DR   RefSeq; YP_081444.1; NC_006271.1.
DR   SMR; Q6EWG9; -.
DR   GeneID; 3021844; -.
DR   KEGG; vg:3021844; -.
DR   Proteomes; UP000006923; Genome.
DR   GO; GO:0033644; C:host cell membrane; 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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; 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; 2.40.10.10; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR   InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR   InterPro; IPR044067; PCV_3C_PRO.
DR   InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF00548; Peptidase_C3; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   Pfam; PF00910; RNA_helicase; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51874; PCV_3C_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR   PROSITE; PS51218; SF3_HELICASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Covalent protein-RNA linkage; Helicase; Host membrane;
KW   Hydrolase; Membrane; Nucleotide-binding; Nucleotidyltransferase;
KW   Phosphoprotein; Protease; Reference proteome; RNA-directed RNA polymerase;
KW   Thiol protease; Transferase; Transmembrane; Transmembrane helix;
KW   Viral RNA replication.
FT   CHAIN           1..697
FT                   /note="Protease cofactor"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000072352"
FT   CHAIN           698..1263
FT                   /note="Putative helicase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000072353"
FT   CHAIN           1264..1318
FT                   /note="Viral genome-linked protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000072354"
FT   CHAIN           1319..1543
FT                   /note="Picornain 3C-like protease"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000072355"
FT   CHAIN           1544..2250
FT                   /note="RNA-directed RNA polymerase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000072356"
FT   TRANSMEM        1225..1245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          849..1020
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1319..1532
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          1814..1956
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          346..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1362
FT                   /note="For picornain 3C-like protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1400
FT                   /note="For picornain 3C-like protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1495
FT                   /note="For picornain 3C-like protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   SITE            697..698
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            1263..1264
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            1318..1319
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   SITE            1543..1544
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1299
FT                   /note="O-(5'-phospho-RNA)-serine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   2250 AA;  251009 MW;  BF1F195785D6B2C2 CRC64;
     MGIFTLCSCG VPCPTRSFYR RHMASGCDLL PTRQQLADVG YTEPTVIAEV VTPPTQAPLE
     LFVEISPPVL APFEPSVEIS LPIQAPAEPI VEASPPAATQ FVGIEALIAS GPCFFGSFGP
     FEEYYSSPVG PLTRFDTLRR EGHCAARARV AAVAAKAVIV QQTLSETAAA MRATLPLWMK
     GQVAPPVKSK RALKREAKAK AKADYLASDE AYYKATDGLT ALPPGVSRDV HMRQLDAMEV
     AYLAHVGDVA ARGFQRRQVL RAAYKARCEK RAFKRFLEEV DFLCLPVHIV DKIQTPFDGE
     QAAAPEMQKG MVYATSRRQV KTRRSFSSFL PKEDFSFTLG VCPARSPTVT PSSTPSTSRS
     SSPEPRVSSP SGVLPEKAAC IGFCSHGSEC TEHFCFGYLN LKSEALASQY LAWLLQTKLP
     GGISCFELEV SSYLEQCQDT MEAIDLWWHA MDRYCFNFKS SKYVILDNFL CKHSIAKDQT
     PREFLAKHRI AKAKALHRVP SRKEKMQALC EQRADKAWDA YIELNKNCKV GEGPLEYLKA
     AKDRCVEFFS PFTKYCNEAI RSLNPLVAIL GPFKDGFWTC FNNLREKCLK MVNDHWLAFA
     AGTTLVLSLI FLLCIICLVK IFSILIANLG LGVVAITTLV TALVVGFFLF NGMLEQAADL
     QLCSLVASDF LNFLAQNQGS ALVAGTMASV QDDLRGQGVS WCFSALYKLI SRVVPVGIKE
     TSILFNSIGN VSRSANHSKD FFLNMKEMAC SWMDALSDAM ALISDDSVSA MQVLKHLCEH
     DFLDWAKKVE RYAGETYDSL IISPAERLKI LRILADQQES FQKAFYNPRI ASKAPRLMLT
     EFNRLSTLLR DAHNALSRAS LFDRQRTPPF WVHLYSENGG TGKSMAMMPL GNHMLDAIGE
     PKTCRFVTRN VASKFLNGYQ HQPCFLMDEF GAAPKQDYSD EVTMLDLVSP NALTLNMAAI
     GEKNTMFTSK LIISTANRRL AHPDVKLGAN LDGFLRRRNI LAEVVLVSGK PHFHEFNLLA
     PRTEQKVYLN RAMQESQVPD PLTPQEFYSL CTENFVNFLN QQSSTVAMSA GLNYVRSSDF
     SHLKDFLLFK IGLDFEENEV ERIVTDYGNS LKNETIFPPE HEQIFQKWKD ALDSLTLPEL
     VSLLDKSVSE TFVYTLISEN HPNVVMSSLT PYECMIYAIC KKKYREGTEA KLPFPEGETT
     SYGASFLSFV AQVALCIPKW ALFCVALCAV LLVGYLIIKF AIFLFSGVVT LLGALAFSNL
     SGDGAEDSPS FDTNRKRGGV KFEYSTKWDA SSTNRFAESY SENGTIPAGT SWADFFGEGP
     EEEPSQSLLN LLKHQVVLIA EPTKVVYNCI ALGGRNFLIT KHVWDLMPAC NYGLYGYAVA
     KDRIFISPRI RPCAQLKGRD LVIVQLPDSV PPFTSLPRDI FLENMAKAPK TANACLVVAK
     PLFERRSVAK LEQTIYPFKQ LPQVHSKDTY SCGSLGSKQM PACYSYVFET YAGLCTSPLI
     AQEGGRCIIL GLHVVGDRSK MGYAQIVTLD DFSDVALSDK VGQGPEEMYI PTKNSECFGS
     VTKLGAWTGP KPYFLEKTSL IPSLISTSID VERTTEPAIL SQRDKRLKDS INPEFDVFLE
     GMKKYAVEAH SLDEDLEVFE DALDRVFLEI PEHACEDLTN DQVCNGIEDD PYAEGIVMQT
     AEGFPFCTQR PAGASGKSWL FAGAPGDWHI VPGSLLANEM HKKEVAPSRG LFEPLIGIDF
     PKDEKVDSSK VYIKPKTRLF TILPVDYNIL VRKYFLSSVS HIMTQHNTIP VKVGIDCLSN
     EWSILYHQLR SKGTNWFNGD YSRFDGITPR NVLQGIVKRI NKFYNNKNSL AITDSNLSIN
     SDLARSLLTD MASTRYGLTN GDLWYVTSGI PSGFPLTVIV NSLVNNFFIH FSYIKLMKRE
     ELNSLYPLHS FRQMVAYATY GDDNLVSVND VITEKFNLVK IADLLAEHGV TLKNGADKNE
     EILSPFYPLE KVDFLKRKFV HYQGHVVAPL NPVNITERLH WIRKGLGEAD ATLENCSSAA
     FEALFHGRCY YDTLVAKIYK ACAASKLSIQ LPTYNDALAI FLSNDSFAKA IQTISLDLPK
     AIFVNKSNYF VSEIFPDVFF CSNERNVTLH KLLEITTTRN ICYISRNYES RNSSRGLFSL
     KGEGWALAPV SARLVVYKNM QKPVYFVDEA NDGLALAYCL DYMLRIKGVS RSRLAQVLYN
     IFGHDETLCS RIASNFSLLD SNKYMPPHKK