POL1_TRSVB
ID POL1_TRSVB Reviewed; 2304 AA.
AC Q88893;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=Membrane-binding protein;
DE AltName: Full=NTP-binding protein;
DE Short=NTB;
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 Tobacco ringspot virus (strain Bud Blight) (TobRV) (TRSV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Nepovirus.
OX NCBI_TaxID=282064;
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8623518; DOI=10.1006/viro.1996.0216;
RA Zalloua P.A., Buzayan J.M., Bruening G.;
RT "Chemical cleavage of 5'-linked protein from tobacco ringspot virus genomic
RT RNAs and characterization of the protein-RNA linkage.";
RL Virology 219:1-8(1996).
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; U50869; AAB03785.1; -; Genomic_RNA.
DR RefSeq; NP_919040.1; NC_005097.1.
DR SMR; Q88893; -.
DR PRIDE; Q88893; -.
DR GeneID; 2943107; -.
DR KEGG; vg:2943107; -.
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..587
FT /note="P1A protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037055"
FT CHAIN 588..1243
FT /note="Putative ATP-dependent helicase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037056"
FT CHAIN 1244..1267
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037057"
FT CHAIN 1268..1484
FT /note="Picornain 3C-like protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037058"
FT CHAIN 1485..2304
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037059"
FT TOPO_DOM 588..1195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1196..1216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1217..1243
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 786..950
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1269..1482
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1762..1900
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 1309
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1348
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1444
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 813..820
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
SQ SEQUENCE 2304 AA; 256618 MW; 133C5E6441DC4186 CRC64;
MGFTCPNSDC LYSRSEWSNR ALREEGLSFS MRCPGACCGA MLVRKQQEPE AVDQRHSPER
VRIAPHQNVC AGLPGVGPSK CPKHSQVPLA PKSKSVPARA TVSASPLKKQ HCDVVVTVGP
PADLELVYPA LVSKGSANPP KVGKKSFNEA LLEKRAAYQV RTAVPPPGPI RVVKTAATPV
KVEKVRFPKG AVAFNGANFI DAKGYVVLSA GALKILRGVQ KLRRQQARSA RRMAACRRVR
LAVFAARLPS LLRKADEATS GGFKYVDLNA PRVVRKAEKR PKKKPAKKAV RPASPVEEEI
NWDDFIIPES ERTASPMKEE KPKRSLVPNS LGFGWWRPAS GNLWDVVSQC QRACEGTFLE
ASAEACLVRA GVDDVALSVW ARISKSVVQL SAYYDVNTLL ENYTALSECT MDELQSVAVQ
LDSEYQELGP PTHFTCGLSN WARGAGKILY NFVAPTVEGI AGAGCRIVER AYELSKTVID
EIFSKMKSLF YDCFGNLFGH LNVLLSTIDS FWARASTWIM NILEKTHDCL KVLRDSAVWS
LLLILVGGLI LLSERFLQSI GIISKPGTIL GIFLATFLGI FGYTFFRKDD TLVSDLLCAF
KIAITNLFRT KPGPPGSPII VDGDVVIPES AVAMSTCSFM GGLDIAIAAI GNVGASILGF
KVGALQYAAK IATCLDQLRK GKDVLKEMTC WIIETLGALW NKMTGREATF FDEVSAIVAV
DIREWLEESQ NLCLAAQTFS IGDKIVLEQC ERLIADGHKL LRGMGDADRK LSSSFLSTVQ
RKVSDLEKIH TQSVRAGYFE GRRMEPFWVY IHGPSHCGKS LLMEPMSREL LRAGGFSESS
IYTKNSCDKY WSRYRRQACV QIDDLSAGKT DPSLESQLIN LVASKEVPLD MAEVEDKGIL
FDSAILVTSS NTAHVPTNAN VNHAEAYKNR MNVVIQCRRK PEYSPMGMEL EGTFQPFDPR
NPQASIECML QHRETHAPIT GWISAGAAMA EAVNQFRLHR EKEMILQSNH LSSFRPAHPI
YTECATFLSM YARDASFVPP VDLGCKWEIP SGYMTIAAVD GRVFGFSQLG VCTEISKQMK
FTEEMEQYTL DKFAPDITKT MASQSRFKLV GAFLKGMIRE EDNVVSLTSL GPKSTATQRE
FFETLGLAER VYLRAVQKKV NKIRTDPAFD VEALHARLLS TIATSYEYVR TYGPKIFPIL
MGFVCVVFAC YGFIMPLLSF ASGGSAVGGM VAMEQIAAAS VVSSGSSPVA HRNRAPPVQP
RYARHRLAGA SAEDAYAYEE MMVVLYVDST VAPVVNAVRG PGRQFFNSHQ ALMIPNNSTV
VAHFSTRDVV EIHWEHDVVR KGEKKDTEII QYRCPSIPEL PSRCKKYFEY DLERDFPGPF
TLDASCYRMQ SPGKIDIELV SWTDHDRELR TRPLVIADPF GEDRYRREIP QYIQYGRPDQ
LHDCGAICVA KIGGQHRIVG LVISTDKHNT GVGLLPSALH MTTCSLSYVP EEWEEAPRGL
KKLGWNDRSE LPHMPRKTQY VAVNEDLAIP FDNPKIPSVL VSDDPRTVGT PVEGKDPVLV
AMEKFYEPMT DFTEEEVRPG QTEVSLFEQV CDDIVQTWFD AGAEFEDVED DVVINGDDDF
DKLIMDTSEG YPYVLERTHG EKGKTRYFEG GPGAYTLKPG TSVYNDYHKL QEEVQVEGGI
PEMVCIECPK DELLVERKVL QKLGTRNFEI LELPKNMLFR KKFLHWALFL SDMRWCLPCQ
VGIVVQGREW GLLMDRLAAK NSVAYNCDYS KFDGLMSCQV LDAIGKMVNK CYSNANPNLK
KKGKGELPGS PPQLARYNLL MSIFGRKCLA RSQVFEVRGG IRRGALTVLL NSVFNEILIR
YVYKTVIPSP EFNRFETFVT LVVYGDDNLI AVDPSMQKIF TGEVIKKTLA RKKITITDGS
DKLSPVLEAK PLAQLDFLKR SFLVSDSGQV MPALDRTCIY SSLLYLRSAD CDPIPLLHQN
VQNALQELYY RQDREEFDNL RTFYLERLPM WRNGQHRLLD WNQCAEHWRA RYTGCPSDNP
AGVLDMLVDP RCKSFMLPAG PANWSMPIAD RIFVCGPKFS ASGPSYTLCF NRLAAGETGV
QIKPVHAATQ GAMPTAKFVE SFRSIKKRPE LELAISAYES GSNLYFKGCA PYNDIWACAI
SFCSAFGYAQ KQVLLHMYDN CKRLGASSLR SYFNKSLVGD GCARRCEIHT TPAIAKQVER
LLPQVQCKHC EYDPEFASKP TTQLRKCTDP GVDGGKAMYI VRGLGRTAAK LVCSDICDGH
LMSCNTSFDK MVVNLFRRSC FKCL
