ID   POLR_KYMVJ              Reviewed;        1874 AA.
AC   P36304;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=RNA replicase polyprotein;
DE            EC=2.7.7.48;
OS   Kennedya yellow mosaic virus (strain Jervis bay) (KYMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Tymoviridae; Tymovirus.
OX   NCBI_TaxID=36392;
OH   NCBI_TaxID=53866; Desmodium.
OH   NCBI_TaxID=53889; Indigofera australis.
OH   NCBI_TaxID=76709; Kennedia rubicunda.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2324710; DOI=10.1099/0022-1317-71-4-925;
RA   Ding S., Keese P., Gibbs A.;
RT   "The nucleotide sequence of the genomic RNA of kennedya yellow mosaic
RT   tymovirus-Jervis Bay isolate: relationships with potex- and carlaviruses.";
RL   J. Gen. Virol. 71:925-931(1990).
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   -!- SIMILARITY: Belongs to the tymovirus NS35 RNA replicase polyprotein
CC       family. {ECO:0000305}.
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DR   EMBL; D00637; BAA00532.1; -; Genomic_RNA.
DR   PIR; JQ0533; JQ0533.
DR   RefSeq; NP_044328.1; NC_001746.1.
DR   MEROPS; C21.001; -.
DR   GeneID; 1493972; -.
DR   KEGG; vg:1493972; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
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:0006396; P:RNA processing; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.90.70.100; -; 1.
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; IPR008043; Peptidase_C21.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR   InterPro; IPR043181; TYMV_endopept_dom.
DR   Pfam; PF05381; Peptidase_C21; 1.
DR   Pfam; PF00978; RdRP_2; 1.
DR   Pfam; PF01443; Viral_helicase1; 1.
DR   Pfam; PF01660; Vmethyltransf; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR   PROSITE; PS51738; PEPTIDASE_C21; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Nucleotide-binding; Nucleotidyltransferase;
KW   Protease; RNA-directed RNA polymerase; Thiol protease; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..1874
FT                   /note="RNA replicase polyprotein"
FT                   /id="PRO_0000222935"
FT   DOMAIN          58..219
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          757..912
FT                   /note="Peptidase C21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT   DOMAIN          972..1129
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          1130..1266
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1601..1707
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          619..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..639
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..709
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..751
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        810
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT   ACT_SITE        896
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT   BINDING         1002..1009
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1874 AA;  210030 MW;  72B6DDE57732A2AD CRC64;
     MAFQLALDAL ASTSHKDPSL HPVLESVHDS LTDSLQTYPW MVPQDLQPFL LKSGIPINSF
     GSSPHPHPAH KTLETHLLFT HWMHLCTQPS SVLFMKPQKF MKLQRKNKFF QHLHNYRLTP
     TDSVRFPSTS PHLPNTPFVF MHDALMYYQP EQILHLFHQV PQLTNLFCSL VTPPESHFTH
     LSLMPDLYTF TLKGQTLHYT PEGHSAGSYN QPITALSWLK INSILSPNLN LSITILESWG
     PLHSILIQRG LPLPDPKLLV RSLPPFSRSP DPETDLVSFQ VPKSVELPQA TFLSQPLRHR
     LVPESVYNAL FTYTRAVRTL RVSDPAGFVR TQSNKPEHKW VTPSAWDNLQ TFALLNCPLR
     PNVVYHVLLN PLQKMKLYFS QHWRRLGVIA APGLFCLSLL LRSQKWSLPL PKAKSISVFR
     RNLLLPPKPH RPPLLPHPEQ MLQEFKLPWH RPPPKGKRNP FLTLLINLLH IPREICAGIR
     RYPSYYQSIQ PKPLNPIQQF RNQLLAQLHT LPLPKKFLSI LPRARKDIPL LPRMSFTTVN
     LPLQPPMWLA IGASLVPELA FLLSWLSGDV DLQTQHDIYH HHLHPENFTL SWTRTPYLAL
     APSPFLPYAH SPLPPLPVNS SPLFPPPPPL PPSQPPLSQG PATQAPSAQP TPGEPLLAPP
     TTELKPESSN PNNPNPSSSA GSNPPPKSSS SDNPPAPNKP TPTSSSTTPP SPNLPLQFGS
     IHSPFLSDGQ LNYSALPPPQ DPTNTTLSLL PEPKPPTEVQ SPLMADPTCV GPAVSFSSLY
     PRDFFPNTAS FLTRLRLSPP TPLPMPKNNC LLTAVAPSLH INPHRLWTSL QEVLPDSLLS
     NSEIDSVGMS TDLLTALSHL FNFQAVVHSE RGDILFGLQS AKTVIHIYHT NGPPAHYSPP
     PKIIGSNSPP SSQQHPLEQA ALRFKYQGSH LPFSSFHSFT TSVQHAKNLI SNMKNGFDGV
     MSTIEPSIRH QPGHSPREKF IALDAMIDLA RPKTVSMFHL AGFAGCGKTK PLQSLLSTRP
     FHSFRVSTPT TELRNEWKKD MNLPASQAFR FCTWESSLLK QTKILVIDEI YKLPRGYLDL
     CILADPCLEL VIILGDPLQG EYHSTSPHSS NHQLQSETTR LLPFIDHYCW WTYRVPSHIA
     DLFSVPSFNR SEGHYQMAVR TADSYTPGHF NLVNSVATAN AVIQLGFPAT TISASQGVTH
     HNRVTILLDK HSRLLSPSNT LVALTRSTVG VEFLGDIGSL SGTNNSSDMF SRAIYRQPIN
     LSSSFPRIFH LLPLLNKPIS RRSTRLIGSH SPIFHNPRLT NIHLPPHIPT SYSQDFVVSN
     PIFQGQADPR LDTHFLPPTR LPLQSELLPA QLSQTTKPTD SFTNNTPFTP VYPGENFENL
     AAFFLPAHDP ELKEVTRRDQ TSAQFPWFDR PFSLSCQPSS LIAAKHSPSQ DPTLLPFSIP
     KRLRFRKSDN PHVLSAIDVL LGNQLFFNLC KAYRRNPTHV GPFNPALFAE CIALNDYAQL
     SSKTQATLVA NHSRSDPDWR HTAVKIFAKS QHKVNDASIF GNWKACQTLA LMHDFVILSL
     GPVKKYQRIF DALDRPPHLY THCGKSPADL SAWCQTHLTG QIKLTNDYTA FDQSQHGESV
     ILEALKMKRL SIPSHLIQLH VHLKTNVATQ FGPLTCMRLT GEPGTYDDNS DYNLAVIHSQ
     FDMKDIPVMV SGDDSLIDRQ PPLAQSWEAT KRLLHLRFKT EKTTHPLFCG YYTGSAGAIR
     NPLALFSKLM IAIDDEAIHD RRLSYLTEFS TGHQLGDALW TLLPESTQIY QSACFDYFCR
     HSPPHEKALL SSFELPDSVI SKISSSTKWL SKNAFYALPS KIRKAVIASR HSSSFPENPD
     VSQLEFELLQ SFQF