ID   RDRP_HASV               Reviewed;        1704 AA.
AC   Q67724;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 92.
DE   RecName: Full=Methyltransferase/helicase/RNA-directed RNA polymerase;
DE            EC=2.1.1.-;
DE            EC=2.7.7.48;
DE            EC=3.6.4.13;
OS   Helicoverpa armigera stunt virus (HaSV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Hepelivirales; Alphatetraviridae; Omegatetravirus.
OX   NCBI_TaxID=37206;
OH   NCBI_TaxID=29058; Helicoverpa armigera (Cotton bollworm) (Heliothis armigera).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND FUNCTION.
RX   PubMed=11831734; DOI=10.1006/viro.1995.1132;
RA   Gordon K.H., Johnson K.N., Hanzlik T.N.;
RT   "The larger genomic RNA of Helicoverpa armigera stunt tetravirus encodes
RT   the viral RNA polymerase and has a novel 3'-terminal tRNA-like structure.";
RL   Virology 208:84-98(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   PubMed=20107015; DOI=10.1099/vir.0.020156-0;
RA   Short J.R., Knox C., Dorrington R.A.;
RT   "Subcellular localization and live-cell imaging of the Helicoverpa armigera
RT   stunt virus replicase in mammalian and Spodoptera frugiperda cells.";
RL   J. Gen. Virol. 91:1514-1523(2010).
CC   -!- FUNCTION: RNA-dependent RNA polymerase replicates the viral genome
CC       composed of 2 RNA segments, RNA1 and RNA2.
CC       {ECO:0000269|PubMed:11831734}.
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;
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   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:20107015}.
CC       Note=Localizes to punctate structures partially overlapping late
CC       endosomes.
CC   -!- SIMILARITY: Belongs to the ssRNA positive-strand viruses RNA-directed
CC       RNA polymerase family. {ECO:0000305}.
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DR   EMBL; U18246; AAC98529.1; -; Genomic_RNA.
DR   EMBL; EU345431; ACA50473.1; -; mRNA.
DR   RefSeq; NP_049235.1; NC_001981.1.
DR   SMR; Q67724; -.
DR   PRIDE; Q67724; -.
DR   GeneID; 991180; -.
DR   KEGG; vg:991180; -.
DR   Proteomes; UP000006711; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
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:0006396; P:RNA processing; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR002588; Alphavirus-like_MT_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR   Pfam; PF00978; RdRP_2; 1.
DR   Pfam; PF01443; Viral_helicase1; 1.
DR   Pfam; PF01660; Vmethyltransf; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Host cytoplasm; Hydrolase; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; RNA-directed RNA polymerase;
KW   Transferase.
FT   CHAIN           1..1704
FT                   /note="Methyltransferase/helicase/RNA-directed RNA
FT                   polymerase"
FT                   /id="PRO_0000402490"
FT   DOMAIN          52..295
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          575..737
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          738..880
FT                   /note="(+)RNA virus helicase C-terminal"
FT   REGION          1475..1518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1621..1649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1678..1704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1475..1498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1499..1518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1621..1647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1684..1704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1704 AA;  187842 MW;  D7CFE0B6FE065997 CRC64;
     MYAKATDVAR VYAAADVAYA NVLQQRAVKL DFAPPLKALE TLHRLYYPLR FKGGTLPPTQ
     HPILAGHQRV AEEVLHNFAR GRSTVLEIGP SLHSALKLHG APNAPVADYH GCTKYGTRDG
     SRHITALESR SVATGRPEFK ADASLLANGI ASRTFCVDGV GSCAFKSRVG IANHSLYDVT
     LEELANAFEN HGLHMVRAFM HMPEELLYMD NVVNAELGYR FHVIEEPMAV KDCAFQGGDL
     RLHFPELDFI NESQERRIER LAARGSYSRR AVIFSGDDDW GDAYLHDFHT WLAYLLVRNY
     PTPFGFSLHI EVQRRHGSSI ELRITRAPPG DRMLAVVPRT SQGLCRIPNI FYYADASGTE
     HKTILTSQHK VNMLLNFMQT RPEKELVDMT VLMSFARARL RAIVVASEVT ESSWNISPAD
     LVRTVVSLYV LHIIERRRAA VAVKTAKDDV FGETSFWESL KHVLGSCCGL RNLKGTDVVF
     TKRVVDKYRV HSLGDIICDV RLSPEQVGFL PSRVPPARVF HDREELEVLR EAGCYNERPV
     PSTPPVEEPQ GFDADLWHAT AASLPEYRAT LQAGLNTDVK QLKITLENAL KTIDGLTLSP
     VRGLEMYEGP PGSGKTGTLI AALEAAGGKA LYVAPTRELR EAMDRRIKPP SASRTQHVAL
     AILRRATAEG APFATVVIDE CFMFPLVYVA IVHALSPSSR IVLVGDVHQI GFIDFQGTSA
     NMPLVRDVVK QCRRRTFNQT KRCPADVVAT TFFQSLYPGC TTTSGCVASI SHVAPDYRNS
     QAQTLCFTQE EKSRHGAEGA MTVHEAQGRT FASVILHYNG STAEQKLLAE KSHLLVGITR
     HTNHLYIRDP TGDIERQLNH SAKAEVFTDI PAPLEITTVK PSEEVQRNEV MATIPPQSPT
     PHGAIHLLRK NFGDQPDCGC VALAKTGYEV FGGRAKINVE LAEPDATPKP HRAFQEGVQW
     VKVTNASNKH QALQTLLSRY TKRSADLPLH EAKEDVKRML NSLDRHWDWT VTEDARDRAV
     FETQLKFTQR GGTVEDLLEP DDPYIRDIDF LMKTQQKVSP KPINTGKVGQ GIAAHSKSLN
     FVLAAWIRIL EEILRTGSRT VRYSNGLPDE EEAMLLEAKI NQVPHATFVS ADWTEFDTAH
     NNTSELLFAA LLERIGTPAA AVNLFRERCG KRTLRAKGLG SVEVDGLLDS GAAWTPCRNT
     IFSAAVMLTL FRGVKFAAFK GDDSLLCGSH YLRFDASRLH MGERYKTKHL KVEVQKIVPY
     IGLLVSAEQV VLDPVRSALK IFGRCYTSEL LYSKYVEAVR DITKGWSDAR YHSLLCHMSA
     CYYNYAPESA AYIIDAVVRF GRGDFPFEQL RVVRAHVQAP DAYSSTYPAN VRASCLDHVF
     EPRQAAAPAG FVATCAKPET PSSLTAKAGV SATTSHVATG TAPPESPWDA PAANSFSELL
     TPETPSTSSS AVIVFIGLLY IVWKVAQWWR HRKRTEDLNS RKPPSQDRQS RSSECLDRSG
     ERTGSSLTAP TAPSPSFSFS ERARLATGPT VAAATSPSAT PSCATDQVAA RTTPDFAPFL
     GSQSARAVSK PYRPPTTARW KEVTPLHAWK GVTGDRPEVR EDPETAAVVQ ALISGRYPQK
     TKLSSDASKG YSRTKGCSQS TSFPAPSADY QARDCQTVRV CRAAAEMARS CIHEPLASSA
     ASADLKRIRS TSDSVPDVKI SKSA