POL1_TBRVM
ID POL1_TBRVM Reviewed; 2266 AA.
AC Q8B8X3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=RNA1 polyprotein;
DE AltName: Full=P1;
DE Contains:
DE RecName: Full=P1A protein;
DE Short=1A;
DE AltName: Full=protease cofactor;
DE Contains:
DE RecName: Full=Putative ATP-dependent helicase;
DE EC=3.6.4.-;
DE AltName: Full=1B;
DE AltName: Full=NTP-binding protein;
DE Short=NTB;
DE AltName: Full=membrane-binding protein;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=1C-VPg;
DE Contains:
DE RecName: Full=Picornain 3C-like protease;
DE Short=3C-like protease;
DE EC=3.4.22.-;
DE AltName: Full=1D-PRO;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=1E-POL;
OS Tomato black ring virus (strain MJ) (TBRV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Nepovirus.
OX NCBI_TaxID=283677;
OH NCBI_TaxID=4681; Allium porrum (Leek) (Allium ampeloprasum var. porrum).
OH NCBI_TaxID=4045; Apium graveolens (Celery).
OH NCBI_TaxID=161934; Beta vulgaris (Sugar beet).
OH NCBI_TaxID=38871; Fraxinus (ash trees).
OH NCBI_TaxID=4236; Lactuca sativa (Garden lettuce).
OH NCBI_TaxID=39639; Narcissus pseudonarcissus (Daffodil).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=35938; Robinia pseudoacacia (Black locust).
OH NCBI_TaxID=23216; Rubus (bramble).
OH NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH NCBI_TaxID=4113; Solanum tuberosum (Potato).
OH NCBI_TaxID=13305; Tulipa.
OH NCBI_TaxID=3604; Vitis sp. (Grape).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15045566; DOI=10.1007/s00705-003-0261-z;
RA Jonczyk M., Le Gall O., Palucha A., Borodynko N., Pospieszny H.;
RT "Cloning and sequencing of full-length cDNAs of RNA1 and RNA2 of a Tomato
RT black ring virus isolate from Poland.";
RL Arch. Virol. 149:799-807(2004).
CC -!- FUNCTION: Picornain 3C-like protease is a thiol protease that cleaves
CC the P1 and P2 polyproteins. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: [Viral genome-linked protein]: Host endoplasmic
CC reticulum lumen {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Putative ATP-dependent helicase]: Host
CC endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages by picornain 3C-like protease in vivo
CC yield mature proteins. Picornain 3C-like protease is autocatalytically
CC processed (By similarity). {ECO:0000250}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently linked to
CC the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC peptide primer for the polymerase (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nepoviruses RNA1 polyprotein family.
CC {ECO:0000305}.
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DR EMBL; AY157993; AAN72830.1; -; Genomic_RNA.
DR RefSeq; NP_958814.1; NC_004439.1.
DR SMR; Q8B8X3; -.
DR MEROPS; C03.025; -.
DR GeneID; 956643; -.
DR KEGG; vg:956643; -.
DR GO; GO:0044166; C:host cell endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; 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:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Covalent protein-RNA linkage; Helicase;
KW Host endoplasmic reticulum; Host membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; RNA-binding;
KW RNA-directed RNA polymerase; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral RNA replication.
FT CHAIN 1..565
FT /note="P1A protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037075"
FT CHAIN 566..1205
FT /note="Putative ATP-dependent helicase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037076"
FT CHAIN 1206..1232
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037077"
FT CHAIN 1233..1442
FT /note="Picornain 3C-like protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037078"
FT CHAIN 1443..2266
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037079"
FT TOPO_DOM 566..1158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1159..1179
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1180..1205
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT DOMAIN 751..917
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1229..1438
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1715..1843
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 1272
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1310
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1402
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 781..788
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
SQ SEQUENCE 2266 AA; 254131 MW; FF27C55CBE738377 CRC64;
MSVTLSPPGD CFTFNHVKYN NSLNKYLFYN NNLDIVLDDF DFYFNFYAKK YNVLSSFFSD
RVLSALYTPM SVSEAASLAL EDFCELALDK LKINPFHQLW EETLANWPVY PGTSLLDFFR
TQYEIRREVA EASAEALRLK KATRADAFAD EVKFLIKNGV LPHLAGDFAR KIWSTGKDQK
KTRTAFLVKI KKANQLKQQW NSARSLAAAR AEVLREFEPS PQQIQKAIEA QLFAEKLGRK
YATLTARVRA KRAAARELRE KQLYQETVDL LNASLLPPME KVEIERKYRK VRPTGANVVH
QVVANPLGSL CPYMGLGAKT ADVRCQATLM AGKIHAQYPR LATAIYAWVI GPAAHFECIT
PVRNFVKGLT FMVDFFPEEA LIHELNEITT EAVCIGASMV LDEERAKLEA HAQSANCRAN
VFMKAMAGVK NMAKCAYTGF KTGCEEAGRS LAEGICSVMM RSFRECIAQI KTELGCAIEM
VEVMIKKVKD WFYSMLEKLQ CGLETLGSYA MYALAILLGC GLTSLLERCI GGQGILTKLF
ITGVLAAIGL QAAGGFDNLQ REMVQLCTAL AAGIFDIQHA GNGKYKPSWD ITAEHAREDA
RDSNVRSIPI ISGVIEALAQ FGTGLCSMQS ATLIEIGKIG AACHSMRMGK EALKEFCATL
MYYLGRIADK VTGRETIFFD ELSTLVHVDV RGWIKRAQSC MRESFHTEIG NQFFRDMVAQ
LVDEGQKLQI GVNGIPRKIS ADYSQLIGQI MKDLVELHKR TIRAGISEGR RCEPVWIYLF
GQRHCGKSNF MSTLDNALAK HFNLPNTTAY RNCKDAFYSG YSGQTFFHMD DLSSVKLEPP
LEAELINLVS CQEVPLNMAD LADKPIYFRS PFIISSSNFE DVPAGCGVRD IEAYRARKAC
LVEMRRKPGV IYDPENPLLA SQARFKDPMY QTLINGQTEE TSWMEMDDVV TEIINISARH
RSAQEKLQAR YMREKALLDP LALASESFLV KEAQKVFLDF DGVELEKAGV PRPEGGHGLY
VDGVLYLVNA SFEFDEIPIK DGGYQRLWDS RMRKKFLPAI QRDEHLNTKS MVVTGFLRSL
VNGECAVLSK DTLTASATTA QLSIFKALRL EERVYLRTLQ HQLDLYSQDI PENPYCNSAW
VKVLGAIGAG RDYLVQNGCG ILMIAAALIL ILVSGWGFWK LFVGLFSGTM SLGAAITGMS
AVDIKAQQSS ASQEKGYRAR NIPIHHRYAY ARSQAGDGLL PAARLCVAIY QPGGGFVSAM
QYKNKSVRMT RHQALRFKEG EQLTVIFAST GESQLIRWHK YHMREEHGSE IVTWLAPSLP
ALSPDLKDLF LEDKEVDLPN HFKTIGYVLR VDSTAFHYDT LDTYGAVDKT PLPLKGVVGN
ELYLHEIPEK IVFHYESRND DCGMIMLCQI RGKMRVVGML VAGKDKTSWA DIMPPNSLAE
LKSQIDYIPE FGEACDGYFK AGYVHKSEAP TLPKKTNMVP VPESLRVPCD VPVKEPAVLT
KDDPRCPIGV DPPRAALKKK FTQPMMELEQ EILDEVATDI LETWYDCEDH VLSDISLSVA
INGIPADSEE AELENFVMKT SPGYPYFKNN RAEKLKGKHA YFEEAEDGSL QLKKGGMAAE
LHENLVEFTK NEVPELVVIE CTKDELLPER KIKVGACRLF EIMPLHYNLF LRQKTCAFTQ
FLQHNRHRLP CQVGTNPYSR EWGHMLNRLM RPKTNEAINC DYSGFDGLLN PQLIECIARM
INRLYALSGE SDVQQAQRYN MLMALVGRYA FVGQQVYKVN CGLPSGFALT VVVNSVFNEI
LIRYAYKKLA PAPERNRFGS TVCLLVYGDD NLISVSPSIA SWFTGEAIRI TLAEKKVKIT
DGSDKDAPTI EAKSFWELDF LKRKFLKLDN GIVQAPLDRS AIFSSLYWLT PDKSKFHESQ
KPSDFQGEVD VIEELLLNVN VALMELYLHN DVAEFQRVRG FYAQRLPLMV SQLRTWAFCE
AFHSAQQTGM QKYDPAVVLD HMSGVDFKRF MHMSEQGNKA HFYTEMLGVS GPHYKPQEGD
FIVSNQPLKP GVQGEYVPIV FGEGIGGLPT KKWVGDFGKP SQLKNSKGYL ITGLLREQIE
AGKRLIFMGP APYVANNAAL ISFGSAHKML IQKDALAHYR NVIPESTSGL EQYFDAPIPQ
ASVGTFYFGD GETYTALCEY KDGKVLQYEG LPTAILNQAA KDRKVPCMVA RQWKSKFTVR
MACDSNMCPH HSATCANFEL AFKQCWLSKC KCAGNNVSKW YGTKFS
