R1AB_BYVU
ID R1AB_BYVU Reviewed; 3094 AA.
AC Q08534; Q66109;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
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 Beet yellows virus (isolate Ukraine) (BYV) (Sugar beet yellows virus).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Closteroviridae; Closterovirus.
OX NCBI_TaxID=478555;
OH NCBI_TaxID=161934; Beta vulgaris (Sugar beet).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], RIBOSOMAL FRAMESHIFT, PROCESSING OF
RP POLYPROTEIN, AND ACTIVE SITES OF LEADER PROTEASE.
RX PubMed=8259666; DOI=10.1006/viro.1994.1034;
RA Agranovsky A.A., Koonin E.V., Boyko V.P., Maiss E., Froetschl R.,
RA Lunina N.A., Atabekov J.G.;
RT "Beet yellows closterovirus: complete genome structure and identification
RT of a leader papain-like thiol protease.";
RL Virology 198:311-324(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2857-3074.
RX PubMed=1990061; DOI=10.1099/0022-1317-72-1-15;
RA Agranovsky A.A., Boyko V.P., Karasev A.V., Lunina N.A., Koonin E.V.,
RA Dolja V.V.;
RT "Nucleotide sequence of the 3'-terminal half of beet yellows closterovirus
RT RNA genome: unique arrangement of eight virus genes.";
RL J. Gen. Virol. 72:15-23(1991).
RN [3]
RP PROTEIN SEQUENCE OF 589-594, PROCESSING OF POLYPROTEIN, AND SUBCELLULAR
RP LOCATION OF THE LEADER PROTEASE.
RX PubMed=12867660; DOI=10.1099/vir.0.19151-0;
RA Zinovkin R.A., Erokhina T.N., Lesemann D.E., Jelkmann W., Agranovsky A.A.;
RT "Processing and subcellular localization of the leader papain-like
RT proteinase of Beet yellows closterovirus.";
RL J. Gen. Virol. 84:2265-2270(2003).
RN [4]
RP SUBCELLULAR LOCATION OF METHYLTRANSFERASE/HELICASE/RNA-DIRECTED RNA
RP POLYMERASE.
RX PubMed=11458006; DOI=10.1099/0022-1317-82-8-1983;
RA Erokhina T.N., Vitushkina M.V., Zinovkin R.A., Lesemann D.E., Jelkmann W.,
RA Koonin E.V., Agranovsky A.A.;
RT "Ultrastructural localization and epitope mapping of the methyltransferase-
RT like and helicase-like proteins of Beet yellows virus.";
RL J. Gen. Virol. 82:1983-1994(2001).
RN [5]
RP CHARACTERIZATION OF THE LEADER PROTEASE.
RX PubMed=11711606; DOI=10.1128/jvi.75.24.12153-12160.2001;
RA Peng C.-W., Peremyslov V.V., Mushegian A.R., Dawson W.O., Dolja V.V.;
RT "Functional specialization and evolution of leader proteinases in the
RT family Closteroviridae.";
RL J. Virol. 75:12153-12160(2001).
RN [6]
RP FUNCTION OF THE LEADER PROTEASE.
RX PubMed=12584307; DOI=10.1128/jvi.77.5.2843-2849.2003;
RA Peng C.-W., Napuli A.J., Dolja V.V.;
RT "Leader proteinase of beet yellows virus functions in long-distance
RT transport.";
RL J. Virol. 77:2843-2849(2003).
CC -!- FUNCTION: L-pro is involved in systemic transport and in RNA
CC amplification. {ECO:0000269|PubMed:12584307}.
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 -!- SUBCELLULAR LOCATION: [Leader protease]: Host cytoplasmic vesicle
CC membrane. Note=Associates with the closterovirus-induced membranous
CC vesicle aggregates.
CC -!- SUBCELLULAR LOCATION: [Methyltransferase/helicase/RNA-directed RNA
CC polymerase]: Host cytoplasmic vesicle membrane. Note=Associates with
CC the closterovirus-induced membranous vesicle aggregates.
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 {ECO:0000269|PubMed:8259666};
CC Name=Replicase 1ab;
CC IsoId=Q08534-1; Sequence=Displayed;
CC Name=Replicase 1a;
CC IsoId=Q08534-2; Sequence=VSP_029860;
CC -!- DOMAIN: The C-terminal domain is required for autoproteolysis.
CC -!- PTM: The leader protease is released by autoproteolysis.
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DR EMBL; X73476; CAA51871.1; -; Genomic_RNA.
DR EMBL; X53462; CAA37549.1; -; Genomic_RNA.
DR RefSeq; NP_041870.2; NC_001598.1.
DR MEROPS; C42.001; -.
DR PRIDE; Q08534; -.
DR GeneID; 1493976; -.
DR KEGG; vg:1493976; -.
DR Proteomes; UP000000359; Genome.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008234; F:cysteine-type peptidase activity; 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; 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; IPR008749; Peptidase_C42.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR InterPro; IPR040910; Zemlya.
DR Pfam; PF05533; Peptidase_C42; 1.
DR Pfam; PF00978; RdRP_2; 1.
DR Pfam; PF01443; Viral_helicase1; 1.
DR Pfam; PF01660; Vmethyltransf; 1.
DR Pfam; PF17646; Zemlya; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR PROSITE; PS51657; PSRV_HELICASE; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Direct protein sequencing; Helicase;
KW Host cytoplasmic vesicle; Host membrane; Hydrolase; Membrane;
KW Methyltransferase; Nucleotide-binding; Nucleotidyltransferase; Protease;
KW Reference proteome; Ribosomal frameshifting; RNA-directed RNA polymerase;
KW Thiol protease; Transferase; Viral RNA replication.
FT CHAIN 1..3094
FT /note="Replicase polyprotein 1ab"
FT /id="PRO_0000312562"
FT CHAIN 1..588
FT /note="Leader protease"
FT /id="PRO_0000312563"
FT CHAIN 589..3094
FT /note="Methyltransferase/helicase/RNA-directed RNA
FT polymerase"
FT /id="PRO_0000312564"
FT DOMAIN 670..857
FT /note="Alphavirus-like MT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT DOMAIN 2215..2387
FT /note="(+)RNA virus helicase ATP-binding"
FT DOMAIN 2388..2548
FT /note="(+)RNA virus helicase C-terminal"
FT DOMAIN 2817..2930
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1807..1828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 622..647
FT /evidence="ECO:0000255"
FT ACT_SITE 509
FT /note="For leader protease activity"
FT /evidence="ECO:0000269|PubMed:8259666"
FT ACT_SITE 569
FT /note="For leader protease activity"
FT /evidence="ECO:0000269|PubMed:8259666"
FT SITE 588..589
FT /note="Cleavage; by the leader protease"
FT VAR_SEQ 2631..3094
FT /note="Missing (in isoform Replicase 1a)"
FT /evidence="ECO:0000305"
FT /id="VSP_029860"
SQ SEQUENCE 3094 AA; 348277 MW; 83078999DA9D64C7 CRC64;
MAFLNVSAVP SCAFAPAFAP HAGASPIVPD SFPCVPRYSD DISHFRLTLS LDFSVPRPLS
LNARVHLSAS TDNPLPSLPL GFHAETFVLE LNGSSAPFSI PSRHIDFVVN RPFSVFPTEV
LSVSSLRTPS RLFALLCDFF LYCSKPGPCV EIASFSTPPP CLVSNCVAQI PTHAEMESIR
FPTKTLPAGR FLQFHKRKYT KRPETLIIHE SGLALKTSAL GVTSKPNSRP ITVKSASGEK
YEAYEISRKD FERSRRRQQT PRVRSHKPRK INKAVEPFFF PEEPKKDKRK RASLPTEDEG
FITFGTLRFP LSETPKEEPR LPKFREVEIP VVKKHAVPAV VSKPVRTFRP VATTGAEYVN
ARNQCSRRPR NHPILRSASY TFGFKKMPLQ RFMKEKKEYY VKRSKVVSSC SVTKSPLEAL
ASILKNLPQY SYNSERLKFY DHFIGDDFEI EVHPLRGGKL SVLLILPKGE AYCVVTAATP
QYHAALTIAR GDRPRVGELL QYRPGEGLCY LAHAALCCAL QKRTFREEDF FVGMYPTKFV
FAKRLTEKLG PSALKHPVRG RQVSRSLFHC DVASAFSSPF YSLPRFIGGV EEEAPEITSS
LKHKAIESVY ERVSIHKDNL LARSVEKDLI DFKDEIKSLS KEKRSVTVPF YMGEAVQSGL
TRAYPQFNLS FTHSVYSDHP AAAGSRLLEN ETLASMAKSS FSDIGGCPLF HIKRGSTDYH
VCRPIYDMKD AQRRVSRELQ ARGLVENLSR EQLVEAQARV SVCPHTLGNC NVKSDVLIMV
QVYDASLNEI ASAMVLKESK VAYLTMVTPG ELLDEREAFA IDALGCDVVV DTRRDMVQYK
FGSSCYCHKL SNIKSIMLTP AFTFSGNLFS VEMYENRMGV NYYKITRSAY SPEIRGVKTL
RYRRACTEVV QVKLPRFDKT LKTFLSGYDY IYLDAKFVSR VFDYVVSNCS VVNSKTFEWV
WSYIKSSKSR VVISGKVIHR DVHIDLKHSE CFAAVMLAVG VRSRTTTEFL AKNLNYYTGD
ASCFETIRFL FREWSRRAYA EINRSFRKLM KSILSAGLDY EFLDLDNSLQ HLLEYSEVEV
RVSIAQNGEV DCNEENRVLT EIIAEAADRK SIAQGLSGAL SSVPTQPRGG LRGGSRRSGV
SFLYNLVEEV GNLFFSVGDA VRFLVKVFKT FSDSPIFRVV RMFLDLAEAA SPFVSVVSLC
AWLREAVSAF SSWVADRTVS ESVKTFVNRT VKRFLNFMSA KTLTKKFFRF FLSASALAKT
VVRKAKVILE AYWEVWFESI LSDSGEYSAV EFCSSVVITL LTNSGRLLPG FSPSAIITEV
LLDLATKISI EVLLKQISPA DSTASSALYR RVLSEILSNF RTMGEHGIFT KVFLLCGFLP
VFVRKCVALC VPGDMATYAR FLEYGVDDLF FLGRSVNSIK NYLCVVAAGL VDSIVDSVVL
KLSGVAKERV LGFKSKIIKN FLNVFRKAKV VTRTSSSTDL SEDEYFSCDE SKPGLRGGSS
RFTLSRLLDI FFNFLKSSKL VIENACFSAY ERIERNMKLY FFPLNSSEEE ARRLIRCAGD
FDYLSDSAFD EDEMLRQAFE QYYSSDDESV TYDGKPTVLR SYLNVSRRFL ETFCNGPKFF
VKVSNYFKAL YSRLLRVLPW VDRNLSDSPG LKGGNEKALL AKFFKTCVIT ACECVSQICC
LRLIRLCWGT PACGLVRLFY ITYSSTRVLS RVVVAVAVCP LLVRNELDGL SDGLTNMGVS
VFRRLFVALR RALSAYSNSA LRRKIIEFIF GNIHHPFDVA VIETNEVAPE PLSPEVDIDV
DCDFGSDSES VSSDEVASNP RPGLHGGSRR SSNFLTSLVK VVFKLARRIP RLLFRLRNFV
AYFVERRLAS KRLKTFIGLA RLFDNFSLTS VVYLLQEYDS VLNAFIDVEL ILLNSGSVNV
LPLVSWVRGS LTKLAEAIVG SGFASFLGRM CCRVSDWCSS SSNAGCNFMS PVRTKGKFVP
PSSSGSTASM YERLEALESD IREHVLSTCR VGSDEEEERP KEVTEPGIEH TSEDVVPIRS
HSQPLSGGEC SYSEDREENE RANLLPHVSK IVSERRGLET ARRNKRTLHG VSEFLNAINT
SNEQPRPIIV DHSPESRALT NSVREFYYLQ ELALFELSCK LREYYDQLKV ANFNRQECLC
DKDEDMFVLR AGQGVVSGRN SRLPLKHFKG HEFCFRSGGL VPYDGTSRVD TIFHTQTNFV
SANALLSGYL SYRTFTFTNL SANVLLYEAP PGGGKTTTLI KVFCETFSKV NSLILTANKS
SREEILAKVN RIVLDEGDTP LQTRDRILTI DSYLMNNRGL TCKVLYLDEC FMVHAGAAVA
CIEFTKCDSA ILFGDSRQIR YGRCSELDTA VLSDLNRFVD DESRVYGEVS YRCPWDVCAW
LSTFYPKTVA TTNLVSAGQS SMQVREIESV DDVEYSSEFV YLTMLQSEKK DLLKSFGKRS
RSSVEKPTVL TVHEAQGETY RKVNLVRTKF QEDDPFRSEN HITVALSRHV ESLTYSVLSS
KRDDAIAQAI VKAKQLVDAY RVYPTSFGGS TLDVSVNPST SDRSKCKASS APYEVINSFL
ESVVPGTTSV DFGDVSEEMG TQVFESGADN VVIRDSAPVN KSTDHDPQRV SSIRSQAIPK
RKPSLQENLY SYESRNYNFT VCERFSGPQE FGQAMAMVML ERSFDLEKVA KVRSDVIAIT
EKGVRTWMSK REPSQLRALS SDLQKPLNLE EEITTFKLMV KRDAKVKLDS SCLVKHPPAQ
NIMFHRKAVN AIFSPCFDEF KNRVITCTNS NIVFFTEMTN STLASIAKEM LGSEHVYNVG
EIDFSKFDKS QDAFIKSFER TLYSAFGFDE DLLDVWMQGE YTSNATTLDG QLSFSVDNQR
KSGASNTWIG NSIETLGILS MFYYTNRFKA LFVSGDDSLI FSESPIRNSA DAMCTELGFE
TKFLTPSVPY FCSKFFVMTG HDVFFVPDPY KLLVKLGASK DEVDDEFLFE VFTSFRDLTK
DLVDERVIEL LTHLVHSKYG YESGDTYAAL CAIHCIRSNF SSFKKLYPKV KGWVVHYGKL
KFVLRKFANC FREKFDTAFG ERTFLLTTKL ETVL
