R1AB_GLRV3
ID R1AB_GLRV3 Reviewed; 2772 AA.
AC O71189;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Replicase polyprotein 1ab;
DE Contains:
DE RecName: Full=Leader protease;
DE Short=L-Pro;
DE EC=3.4.22.-;
DE AltName: Full=Papain-like cysteine proteinase;
DE Short=PCP;
DE Contains:
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;
GN ORFNames=1a-1b;
OS Grapevine leafroll-associated virus 3 (isolate United States/NY1) (GLRaV-3)
OS (Grapevine leafroll-associated closterovirus (isolate 109)).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Closteroviridae; Ampelovirus.
OX NCBI_TaxID=651354;
OH NCBI_TaxID=29760; Vitis vinifera (Grape).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9603346; DOI=10.1099/0022-1317-79-5-1299;
RA Ling K.S., Zhu H.Y., Drong R.F., Slightom J.L., McFerson J.R.,
RA Gonsalves D.;
RT "Nucleotide sequence of the 3'-terminal two-thirds of the grapevine
RT leafroll-associated virus-3 genome reveals a typical monopartite
RT closterovirus.";
RL J. Gen. Virol. 79:1299-1307(1998).
CC -!- FUNCTION: RNA-dependent RNA polymerase replicates the viral genome.
CC {ECO:0000305}.
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 -!- 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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Comment=The replicase 1a is produced from conventional translation of
CC the 1a ORF. The replicase 1ab is generated probably by a +1 ribosomal
CC frameshifting mechanism occurring at the 1a-1b genes boundary.;
CC Name=Replicase 1ab;
CC IsoId=O71189-1; Sequence=Displayed;
CC Name=Replicase 1a;
CC IsoId=O71188-1; Sequence=External;
CC -!- DOMAIN: The C-terminal domain is required for autoproteolysis.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ssRNA positive-strand viruses RNA-directed
CC RNA polymerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC40705.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF037268; AAC40705.3; ALT_SEQ; Genomic_RNA.
DR SMR; O71189; -.
DR Proteomes; UP000006707; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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: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; 2.60.120.590; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR002588; Alphavirus-like_MT_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR Pfam; PF01660; Vmethyltransf; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Dioxygenase; Helicase; Hydrolase; Iron; Metal-binding;
KW Methyltransferase; Nucleotide-binding; Nucleotidyltransferase;
KW Oxidoreductase; Protease; Reference proteome; Ribosomal frameshifting;
KW RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Viral RNA replication.
FT CHAIN 1..2772
FT /note="Replicase polyprotein 1ab"
FT /id="PRO_0000402528"
FT CHAIN 1..393
FT /note="Leader protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402529"
FT CHAIN 394..2772
FT /note="Methyltransferase/helicase/RNA-directed RNA
FT polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000402530"
FT DOMAIN 478..669
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 1601..1694
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT DOMAIN 1902..2066
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 2067..2233
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 2502..2615
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 143..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1708..1746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1714..1737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 311
FT /note="For leader protease activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 357
FT /note="For leader protease activity"
FT /evidence="ECO:0000250"
FT BINDING 1619
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 1621
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 1676
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 1685
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT SITE 393..394
FT /note="Cleavage; by the leader protease"
FT /evidence="ECO:0000250"
SQ SEQUENCE 2772 AA; 306516 MW; F34DA9FA12B7760F CRC64;
MDYIRPLRVF SFPHVNNTLE YVRYNKANGD VGAFLTTMKF IGNVKLSDFT PRCAAMIYIG
KLTKGVKRTF VPPPVKGFAR QYAVVSGSVS ALRGDGKKVL MEARTSTSAT SDVSDFDVVF
EAVSNALLVV HYHRVVPYAP VKREQPKPAV KQDEQKPKRQ ASHWAVKPTA VGVHVPLPKK
QEALEPAQSV PQQSLEEKAA LTFGLFFSKG GGDESDAVIL RKGKLFNRAL NVPIDVKNTF
VWAKIWDEAS RRRGYFYVKD RAVKFFPIVR GRATIEDFIV NTAPGCDVAL PRIELWSMRE
RAFVCTTKGW CWFNNERLRG EIYRRRCFSS SFSIGFLMHL GFRSLKVIRF AGTNILHMPS
LNEERTFGWK GGDVYLPNVP KTAIVAGDRT RLGGEILASV ANALNQEEVY SSVVSSITNR
LVLRDQSALL SHLDTKLCDM FSQRDAMIRE KPSHRCDVFL KPREREKLRE LFPELSIQFS
DSVRSSHPFA NAMRSCFNGI FSRRCGNVCF FDIGGSFTYH VKAGHVNCHV CNPVLDVKDV
KRRINEILFL STAGGDSYVS SDLLTEAASK SVSYCSRESQ NCDSRADAGF MVDVYDISPQ
QVAEAMDKKG ALVFDIALMF PVELLYGNGE VYLEELDTLV KREGDYLAYN VGQCGEMYEH
SFSNVSGFFT FSYVRTSSGN VFKLEYEGYR CGYHHLTMCR AQKSPGTEVT YRSLVPSFVG
KSLVFIPVVA GSSVSFKTIV LDSDFVDRIY SYALNTIGTF ENRTFEYAVG AVRSQKTHVI
TGSRVVHSKV DISPDDMWGL VVAVMAQAIK DRAKSIRSYN FIKASEGSLA GVFKLFFQTV
GDCFSNAVSV YAKAMVHDNF NVLETLMSMP RAFIRKVPGS VVVTICTSGA SDRLELRGAF
DISKETFGRK LKNSRLRVFS RAIVEDSIKV MKAMKTEDGK PLPITEDSVY AFIMGNVSNV
HCTRAGLLGG SKATVVSSVS KGLVARGAAT KAFSGITSFF STGSLFYDRG LTEDERLDAL
VRTENAINSP VGILETSRVA VSKVVAGTKE FWSEVSLNDF TTFVLRNKVL IGIFVASLGA
APIAWKYRRG IAANARRYAG SSYETLSSLS SQAAGGLRGL TSSTVSGGSL VVRRGFSSAV
TVTRATVAKR QVPLALLSFS TSYAISGCSM LGIWAHALPR HLMFFFGLGT LLGARASANT
WKFGGFSNNW CAVPEVVWRG KSVSSLLLPI TLGVSLIIRG LLNDTIPQLA YVPPVEGRNV
YDETLRYYRD FDYDEGAGPS GTQHEAVPGD DNDGSTSSVS SYDVVTNVRD VGISTNGEVT
GEEETHSPRS VQYTYVEEEV APSAAVAERQ GDPSGSGTAD AMAFVESVKK GVDDVFHQQS
SGETAREVEV DGKGLLPESV VGEAPTQERG RAADGNTAQT AVNEGDREPV QSSLVSSPQA
DIPKVTQSEV HAQKEVKQEV PLATVSGATP IVDEKPAPSV TTRGVKIIDK GKAVAHVAEK
KQVQVEQPKQ RSLTINEGKA GKQLCMFRTC SCGVQLDVYN EATIATRFSN AFTFVDNLKG
RSAVFFSKLG EGYTYNGGSH VSSGWPRALE DILTAIKYPS VFDHCLVQKY KMGGGVPFHA
DDEECYPSDN PILTVNLVGK ANFSTKCRKG GKVMVINVAS GDYFLMPCGF QRTHLHSVNS
IDEGRISLTF RATRRVFGVG RMLQLAGGVS DEKSPGVPNQ QPQSQGATRT ITPKSGGKAL
SEGSGREVKG RSTYSIWCEQ DYVRKCEWLR ADNPVMALEP DYTPMTFEVV KTGTSEDAVV
EYLKYLAIGI ERTYRALLMA RNIAVTTAEG VLKVPNQVYE SLPGFHVYKS GTDLIFHSTQ
DGLRVRDLPY VLIAEKGIFT KGKDVDAVVA LGDNLFVCDD ILVFHDAINL IGALKVARCG
MVGESFKSFE YKCYNAPPGG GKTTTLVDEF VKSPNSTATI TANVGSSEDI NMAVKKRDPN
LEGLNSATTV NSRVVNFIVR GMYKRVLVDE VHMMHQGLLQ LGVFATGASE GLFFGDINQI
PFINREKVFR MDCAVFVPKK ESVVYTSKSY RCPLDVCYLL SSMTVRGTEK CYPEKVVSGK
DKPVVRSLSK RPIGTTDDVA EINADVYLCM TQLEKSDMKR SLKGKGKETP VMTVHEAQGK
TFSDVVLFRT KKADDSLFTK QPHILVGLSR HTRSLVYAAL SSKLDDKVGT YISDASPQSV
SDALLTRSPR LVAFEVYERM NFGPTFEGEL VRKIPTSHFV AVNGFLEDLL DGCPAFDYDF
FEDDFETSDQ SFLIEDVRIS ESFSHFTSKI EDRFYSFIRS SVGLPKRNTL KCNLVTFENR
NFNADRGCNV GCDDSVAHEL KEIFFEEVVN KARLAEVTES HLSSNTMLLS DWLDKRAPNA
YKSLKRALGS FVFHPSMLTS YTLMVKADVK PKLDNTPLSK YVTGQNIVYH DRCVTALFSC
IFTACVERLK YVVDERWLFY HGMDTAELAA ALRNNLGDIR QYYTYELDIS KYDKSQSALM
KQVEELILLT LGVDREVLST FFCGEYDSVV RTMTKELVLS VGSQRRSGGA NTWLGNSLVL
CTLLSVVLRG LDYSYIVVSG DDSLIFSRQP LDIDTSVLSD NFGFDVKIFN QAAPYFCSKF
LVQVEDSLFF VPDPLKLFVK FGASKTSDID LLHEIFQSFV DLSKGFNRED VIQELAKLVT
RKYKHSGWTY SALCVLHVLS ANFSQFCRLY YHNSVNLDVR PIQRTESLSL LALKARILRW
KASRFAFSIK RG
