ID   1A_PZSVT                Reviewed;         962 AA.
AC   Q9DUT3;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   29-SEP-2021, entry version 68.
DE   RecName: Full=Replication protein 1a;
DE   Includes:
DE     RecName: Full=ATP-dependent helicase;
DE              EC=3.6.4.-;
DE   Includes:
DE     RecName: Full=Methyltransferase;
DE              EC=2.1.1.-;
GN   ORFNames=ORF1a;
OS   Pelargonium zonate spot virus (isolate Tomato/Italy/1982) (PZSV)
OS   (Pelargonium zonate spot virus (isolate Tomato)).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Martellivirales; Bromoviridae; Anulavirus.
OX   NCBI_TaxID=650488;
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=tomato;
RX   PubMed=14573820; DOI=10.1099/vir.0.19391-0;
RA   Finetti-Sialer M., Gallitelli D.;
RT   "Complete nucleotide sequence of Pelargonium zonate spot virus and its
RT   relationship with the family Bromoviridae.";
RL   J. Gen. Virol. 84:3143-3151(2003).
CC   -!- FUNCTION: Involved in the virus replication. Contains a helicase domain
CC       and a methyltransferase domain. The methyltransferase domain is
CC       probably involved in viral RNA capping. Involved in the formation of ER
CC       membrane spherular invaginations in which RNA replication complexes
CC       form (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RNA-directed RNA polymerase 2a. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bromoviridae replication protein 1a family.
CC       {ECO:0000305}.
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DR   EMBL; AJ272327; CAC08526.1; -; Genomic_RNA.
DR   RefSeq; NP_619770.1; NC_003649.1.
DR   PRIDE; Q9DUT3; -.
DR   GeneID; 956568; -.
DR   KEGG; vg:956568; -.
DR   Proteomes; UP000000411; Genome.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR   GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR021002; 1a_necrotic_phenotyp-det_dom.
DR   InterPro; IPR002588; Alphavirus-like_MT_dom.
DR   InterPro; IPR022184; CMV_1a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF12467; CMV_1a; 1.
DR   Pfam; PF12503; CMV_1a_C; 1.
DR   Pfam; PF01443; Viral_helicase1; 1.
DR   Pfam; PF01660; Vmethyltransf; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Host endoplasmic reticulum; Host membrane;
KW   Hydrolase; Membrane; Methyltransferase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..962
FT                   /note="Replication protein 1a"
FT                   /id="PRO_0000402415"
FT   DOMAIN          71..270
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          667..820
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          821..962
FT                   /note="(+)RNA virus helicase C-terminal"
FT   REGION          79..356
FT                   /note="Methyltransferase"
FT   REGION          536..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..941
FT                   /note="ATP-dependent helicase"
FT   COMPBIAS        547..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   962 AA;  108490 MW;  B545F0F84858A891 CRC64;
     MAATSFNVRD LINSNGADAM GVRGLVDAHA TKAAEEQFEY IKRSKKVWVR QILSASDGEK
     MQKRFGGTFD LQLSKNLCPH SFAGAMRQCE TLECLSSFPE DSLILDFGGS WLFHWQRQHN
     VHSCCPVLDA RDMARHQERM ISMQKCVAHR PGKFESFESP DFCLLKAEDC EVQSPYAISI
     HGAYDMGFEG LCKAMHSHGT IMLRGTMMFD ANMLVFNEGV MEDLNCRWTK EKGDPYGLRG
     APCEDMVHFD FIDESTLSYS HSWKNIKSFL TEGGYQIGNV QYVLERCVIS YGIMSFKIFA
     VSGKIPHTRL RHCVWFPKVR DYVNINPSDP RIWSKVRVKL DTVREVEEIC FRCPKDVSKI
     EVMGGESETC GIMSVLYSST IIVNGMTMMA GERLDVLDYH HVAFSLMLSA RRKFDMFGKA
     MNSLEWKGWV SHFFKSLWPS GDLRDLFGRY FPSLIRYYDK IEFVEKLTHC EVFVNELGMT
     DDKEQRDVVA EAADVLKNTL LKVAIKMSLD KTFRPAEEKK EERTTTTTVT SSAVGDVDER
     PAGTVSGPTI QAPSVTQENT VTSLSEPLDG RLAVRLEAMK EYKRYLLKLQ KNTESNLAGL
     WSLCGGTSDS NNLISTEVLR IMRQSDSLVN LHKADGGWLF PNDFEYMVGY NSSGLGEKRP
     NEVFLVNKDC VLNNNVLLAN GVPAQPPKGN INLMDGVAGC GKTTAIKRAF VFESDLIVTA
     NKKSSEDILK AMFRDTPDIG RNKVRTADSV LMHGVAHKVK RVLFDEVSLV HFGQLCAILT
     ISGAEELIGF GDSEQISFVS RDRLFDMKYH KLSPDSSDQQ IRTFRCPKDV VECVKIMARK
     VGARGSKYNN WFTTSAVRKS LGYHKVSSIN ESPLRPDVHY LTMTQADKAS LLSKARETRF
     RPSVSTIDEV IKTTHESQGI SVPKVILWRG KSTKCDLFTD KMELRFGCCH QASRKFRLLF
     GC