POL1_BAMMN
ID POL1_BAMMN Reviewed; 2258 AA.
AC P90245;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Genome polyprotein 1;
DE Contains:
DE RecName: Full=Protein P3;
DE Contains:
DE RecName: Full=6 kDa protein 1;
DE Short=6K1;
DE Contains:
DE RecName: Full=Cytoplasmic inclusion protein;
DE Short=CI;
DE EC=3.6.4.-;
DE Contains:
DE RecName: Full=6 kDa protein 2;
DE Short=6K2;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=VPg;
DE Contains:
DE RecName: Full=Nuclear inclusion protein A;
DE Short=NI-a;
DE Short=NIa;
DE EC=3.4.22.44;
DE AltName: Full=NIa-pro;
DE Contains:
DE RecName: Full=Nuclear inclusion protein B;
DE Short=NI-b;
DE Short=NIb;
DE EC=2.7.7.48;
DE AltName: Full=RNA-directed RNA polymerase;
DE Contains:
DE RecName: Full=Coat protein;
DE Short=CP;
OS Barley mild mosaic virus (strain Na1) (BaMMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC Patatavirales; Potyviridae; Bymovirus.
OX NCBI_TaxID=103900;
OH NCBI_TaxID=4513; Hordeum vulgare (Barley).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8973524; DOI=10.1007/bf01718216;
RA Kashiwazaki S.;
RT "The complete nucleotide sequence and genome organization of barley mild
RT mosaic virus (Na1 strain).";
RL Arch. Virol. 141:2077-2089(1996).
CC -!- FUNCTION: [6 kDa protein 1]: Indispensable for virus replication.
CC {ECO:0000250|UniProtKB:P13529}.
CC -!- FUNCTION: [6 kDa protein 2]: Indispensable for virus replication.
CC {ECO:0000250|UniProtKB:P09814}.
CC -!- FUNCTION: [Viral genome-linked protein]: Mediates the cap-independent,
CC EIF4E-dependent translation of viral genomic RNAs (By similarity).
CC Binds to the cap-binding site of host EIF4E and thus interferes with
CC the host EIF4E-dependent mRNA export and translation (By similarity).
CC VPg-RNA directly binds EIF4E and is a template for transcription (By
CC similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are
CC templates for translation (By similarity).
CC {ECO:0000250|UniProtKB:P18247}.
CC -!- FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and
CC proteolytic activities. {ECO:0000250|UniProtKB:P04517}.
CC -!- FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA
CC polymerase that plays an essential role in the virus replication.
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=Hydrolyzes glutaminyl bonds, and activity is further
CC restricted by preferences for the amino acids in P6 - P1' that vary
CC with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or
CC Gly) for the enzyme from tobacco etch virus. The natural substrate is
CC the viral polyprotein, but other proteins and oligopeptides
CC containing the appropriate consensus sequence are also cleaved.;
CC EC=3.4.22.44; Evidence={ECO:0000250|UniProtKB:P04517};
CC -!- SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle.
CC Note=Probably colocalizes with 6K2-induced vesicles associated with
CC host chloroplasts. {ECO:0000250|UniProtKB:P13529}.
CC -!- SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate with
CC host chloroplasts. {ECO:0000250|UniProtKB:P09814}.
CC -!- SUBCELLULAR LOCATION: [Coat protein]: Virion {ECO:0000305}.
CC -!- PTM: [Viral genome-linked protein]: VPg is uridylylated by the
CC polymerase and is covalently attached to the 5'-end of the genomic RNA.
CC This uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.
CC -!- PTM: [Genome polyprotein 1]: The viral RNA1 of bymoviruses is expressed
CC as a single polyprotein which undergoes post-translational proteolytic
CC processing by the main proteinase NIa-pro resulting in the production
CC of at least eight individual proteins. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bymoviruses polyprotein 1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D83408; BAA18953.1; -; Genomic_RNA.
DR PRIDE; P90245; -.
DR Proteomes; UP000007444; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; 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:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; 2.40.10.10; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001592; Poty_coat.
DR InterPro; IPR001730; Potyv_NIa-pro_dom.
DR InterPro; IPR013648; PP_Potyviridae.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00863; Peptidase_C4; 1.
DR Pfam; PF00767; Poty_coat; 1.
DR Pfam; PF08440; Poty_PP; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR PRINTS; PR00966; NIAPOTYPTASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW Helical capsid protein; Helicase; Host cytoplasmic vesicle; Hydrolase;
KW Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW RNA-directed RNA polymerase; Transferase; Viral RNA replication; Virion.
FT CHAIN 1..2258
FT /note="Genome polyprotein 1"
FT /id="PRO_0000456242"
FT CHAIN 1..292
FT /note="Protein P3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040530"
FT CHAIN 293..359
FT /note="6 kDa protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040531"
FT CHAIN 360..1017
FT /note="Cytoplasmic inclusion protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040532"
FT CHAIN 1018..1081
FT /note="6 kDa protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040533"
FT CHAIN 1082..1256
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040534"
FT CHAIN 1257..1496
FT /note="Nuclear inclusion protein A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040535"
FT CHAIN 1497..2007
FT /note="Nuclear inclusion protein B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040536"
FT CHAIN 2008..2258
FT /note="Coat protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000040537"
FT DOMAIN 439..597
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 612..778
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1257..1476
FT /note="Peptidase C4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT DOMAIN 1745..1869
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 2027..2047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2233..2258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2240..2258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1302
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 1338
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT ACT_SITE 1405
FT /note="For nuclear inclusion protein A activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00766"
FT BINDING 487..494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 292..293
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 359..360
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 1017..1018
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 1081..1082
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 1256..1257
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 1496..1497
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 2007..2008
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT MOD_RES 1141
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P09814"
SQ SEQUENCE 2258 AA; 256357 MW; 38A06A36F19D4D4A CRC64;
MEEFIPEVFY QNQVQSLKKI LKSWKRDTSI YAYLAREQEV LAFLVLSPAH IAKLNKLLTE
ESARCALLAQ NCETIEALAV VRQALQGVTL HFGDNGMEKG WLHMMKALDA CLDESFSENA
AALKKSIQAV GHKLIAAKNR IESCERSVNH LTTFQFAREY GLSTTYFEKL SNFGGHIRSF
VWSSDSGEIF PKPKRSSRTK RISTFTSYYW GEFWCNCIWL LCSLWSPARW CFNSVVFIWS
LCGVLNLSMV VLQFTLKRHF GRYYFRYVMS GVLAICAVCC VHLKNRKGPI LQASQKDKRF
IGILAFCITV IYMFDVDLAD SLSNNLHKIS RLVNLFLDDN RGFATPALDN LTDFTTILQS
GTSSDDLKIV QDTLAVVLQV DDEDATQDDA IYDSDGLQTF KQWVSHNQLA GMQLARPLQY
PCSTTYGLTA DNVAELATSM AQEAKQWSQV VGHTGSGKST RLPTAYANCL KGLAGRKKNV
LVCEPTRAAT VNVTSGISQN FGRLVYGRHE GWSNLGDKTI QVMTYGSALA AWKVDNKFLS
QFDAVFLDES HLITTHALVF ESICQEVTNV RKFYVSATPR DGKKCPEAVR RYEIKTVKSE
CSSVDTFVRS QDKENSLYVL QHETVLVFLA GKAECDRAAS NWNKLYSTNM YAYSLTGDNF
TVAYENIVTR MLTDRIIVFC TNILETGVTL NVDCVVDFGF TMRPELDLVD KSLTLMRRRV
TENERAQRIG RAGRLRTGHA ICIGNPETRH DLVPPETLYE AALLSFVHGV QFYINEHFEN
AWIEGVTKSQ ASVMTQFKLS PFLMRDIVRD DGAIPLSLHK ILKNYTHRNT DLIGTKLSVM
SHVYNSWPLY RTVHQSIFRG DSNVPQALKH ARVPFNVSTA HDFPWENFAQ ACLEFQPRVL
QVFSDSSSTS RIINLQIGKM HIVNSMEEVK ININSYQRSA ENLRSVKDSF ESSIFRTKLL
RGNPTGKITK RIETLLDNVR VLQQVHAKLE IIAYSGGEKL NMDKKSVDEL NEIVELQSKN
SLTAEELARI LHLTKPTSTF FNLFAERGRQ MLVTLLVMVA ASLMYLVFWV SPRKQDDITI
EGKGRAYNRD KRMGYDSYEE DEVRHKINKK FKERSTRFSN DSKPETSSKY RNLKQEFVNF
YDLKTDANVL QAVFTAMDGA VLLQTEAPMA DIDRVNRLLN DHFEDSESQA AHEGLNTMVK
CHLTMKDGRQ FELDMEQHDP ETIAKLGGEV GFRMNRYDLR QVGATRYINP KAQTSAATLE
GMTMKPMSAF TIDSAKMVGF IKTAKDTLNC ILYGDWIIAP AHIQQGEGDI TFIFQHTQFT
TTTERLASYG IRQFKGLDLV VIRRPQQIRA VKKDMRASIL DTPTEVQMLY LSTKGGKYQV
STSAVCFPHY NNRWGHVIST AEGMCGCIVF NPTTNHIVGI HVSYNDTRRR NEFQAFTSDV
LTTINAPGHE IPFSPWVFDW KFCGYTTKPR NMQSAPSTLE RLNINATGFG FKLNAQGIKP
AMLRSTETFS REFPNTQFKL IGEVKKGLID KHTITGENPY FLEFLNTFKP YQWVQAFMDE
YAPSILAYDA YFKDLKKYDR PPHASVFCED TLTKAKHKMI KILEEAGMGR TLVRTTEQVL
LDMAWTTSGG PLYHGKKIDI VQHLSDDELV QFSEACQQAL ITGTLDGVWN GSLKAELRSS
QKILERKTRV FTAAPITSLI AMKYYVDDFN KQFYKTHLKA PHTVGINKFN RGWQNLYEKL
NKPGWTHGSG DGSRFDSSID GFLFDVIKDI RKHFMDAEHH KQLDTIYEEI VNTKICLANG
LVIQKNCGNN SGQPSTVVDN TLALMTSFLY AYARLTGDDT FELMDENFVF VCNGDDNKFA
MSPSFMVKFG CDFSPFLSEL GLTYEFDEAT EDICENPYMS LTMVRTSFGI GFSLSIERIV
AILQWSRAGG VLHAYLSGIA ALFESFNTPK LFNLVHTYLL WLVTEHEEEL FSMMELKDMF
MPLPTKEQIA LLHYVGTEPI MEETYLQSGK DDPDPIVPPV SDTDLTNMAA APPDNRRSRA
VVPRGTSDWN LPEPKMRMLG FKSKINIETL ADVPEGYMNT FASVATETQR RKWEEATRGD
FGITDNEKWE KLLIAACIYF ADNGTSPNFD EELTMEVNGG LNSIKEYPVR PFVVRAKKIS
TLRRIFRCYS IETKLMFVKL RRVPQWAIKH GCLDEIVFDF MIPDQFTSRT ALETLKQTKL
AAIGVGTSNS LLTSEQTNMR TTETRRRNDY DGHEALLR
