GenomeNet

Database: UniProt
Entry: Q6XW15
LinkDB: Q6XW15
Original site: Q6XW15 
ID   POLG_BTMV               Reviewed;        3085 AA.
AC   Q6XW15;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   18-SEP-2019, entry version 102.
DE   RecName: Full=Genome polyprotein;
DE   Contains:
DE     RecName: Full=P1 proteinase;
DE              EC=3.4.-.-;
DE     AltName: Full=N-terminal protein;
DE   Contains:
DE     RecName: Full=Helper component proteinase;
DE              Short=HC-pro;
DE              EC=3.4.22.45;
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=49 kDa proteinase;
DE              Short=49 kDa-Pro;
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=Capsid protein;
DE              Short=CP;
DE     AltName: Full=Coat protein;
OS   Beet mosaic virus (BtMV).
OC   Viruses; Riboviria; Potyviridae; Potyvirus.
OX   NCBI_TaxID=114921;
OH   NCBI_TaxID=124763; Amaranthus retroflexus (Redroot amaranth) (Redroot pigweed).
OH   NCBI_TaxID=350892; Beta vulgaris subsp. maritima (Sea beet) (Beta maritima).
OH   NCBI_TaxID=3555; Beta vulgaris subsp. vulgaris.
OH   NCBI_TaxID=3559; Chenopodium album (Fat-hen).
OH   NCBI_TaxID=200951; Melilotus indicus (Sourclover) (Yellow sweet clover).
OH   NCBI_TaxID=50192; Sonchus arvensis (Perennial sowthistle).
OH   NCBI_TaxID=3562; Spinacia oleracea (Spinach).
OH   NCBI_TaxID=60916; Trifolium incarnatum (Crimson clover).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15168206; DOI=10.1007/s00705-003-0278-3;
RA   Nemchinov L.G., Hammond J., Jordan R., Hammond R.W.;
RT   "The complete nucleotide sequence, genome organization, and specific
RT   detection of beet mosaic virus.";
RL   Arch. Virol. 149:1201-1214(2004).
RN   [2]
RP   REVIEW.
RX   PubMed=11226583; DOI=10.1016/s0168-1702(01)00220-9;
RA   Urcuqui-Inchima S., Haenni A.L., Bernardi F.;
RT   "Potyvirus proteins: a wealth of functions.";
RL   Virus Res. 74:157-175(2001).
CC   -!- FUNCTION: Capsid protein: involved in aphid transmission, cell-to-
CC       cell and systemis movement, encapsidation of the viral RNA and in
CC       the regulation of viral RNA amplification.
CC   -!- FUNCTION: Nuclear inclusion protein B: an RNA-dependent RNA
CC       polymerase that plays an essential role in the virus replication.
CC   -!- FUNCTION: Helper component proteinase: required for aphid
CC       transmission and also has proteolytic activity. Only cleaves a
CC       Gly-Gly dipeptide at its own C-terminus. Interacts with virions
CC       and aphid stylets. Acts as a suppressor of RNA-mediated gene
CC       silencing, also known as post-transcriptional gene silencing
CC       (PTGS), a mechanism of plant viral defense that limits the
CC       accumulation of viral RNAs. May have RNA-binding activity (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: Cytoplasmic inclusion protein: has helicase activity. It
CC       may be involved in replication (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Both 6K peptides are indispensable for virus
CC       replication. {ECO:0000250}.
CC   -!- FUNCTION: Nuclear inclusion protein A: has RNA-binding and
CC       proteolytic activities.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC         restricted by preferences for the amino acids in P6 - P1' that
CC         vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-
CC         Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The
CC         natural substrate is the viral polyprotein, but other proteins
CC         and oligopeptides containing the appropriate consensus sequence
CC         are also cleaved.; EC=3.4.22.44;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557,
CC         ChEBI:CHEBI:83400; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00539};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus,
CC         commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the
CC         processing of the potyviral polyprotein.; EC=3.4.22.45;
CC   -!- SUBCELLULAR LOCATION: Capsid protein: Virion {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Genome polyprotein;
CC         IsoId=Q6XW15-1; Sequence=Displayed;
CC         Note=Produced by conventional translation.;
CC       Name=P3N-PIPO polyprotein;
CC         IsoId=P0CJ96-1; Sequence=External;
CC         Note=Produced by -1 ribosomal frameshifting in P3 ORF.;
CC   -!- DOMAIN: The N-terminus of helper component proteinase is involved
CC       in interaction with stylets. The central part is involved in
CC       interaction with virions and the C-terminus is involved in cell-to
CC       cell movement of the virus.
CC   -!- PTM: VPg is uridylylated by the polymerase and is covalently
CC       attached to the 5'-end of the genomic RNA. This uridylylated form
CC       acts as a nucleotide-peptide primer for the polymerase (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Genome polyprotein of potyviruses undergoes post-
CC       translational proteolytic processing by the main proteinase NIa-
CC       pro resulting in the production of at least ten individual
CC       proteins. The P1 proteinase and the HC-pro cleave only their
CC       respective C-termini autocatalytically. 6K1 is essential for
CC       proper proteolytic separation of P3 from CI (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potyviridae genome polyprotein family.
CC       {ECO:0000305}.
DR   EMBL; AY206394; AAP41071.1; -; Genomic_RNA.
DR   RefSeq; NP_954611.1; NC_005304.1. [Q6XW15-1]
DR   MEROPS; C06.001; -.
DR   PRIDE; Q6XW15; -.
DR   GeneID; 2943205; -.
DR   KEGG; vg:2943205; -.
DR   Proteomes; UP000007617; 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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; 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; 3.90.70.150; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR001456; HC-pro.
DR   InterPro; IPR031159; HC_PRO_CPD_dom.
DR   InterPro; IPR042308; HC_PRO_CPD_sf.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002540; Pept_S30_P1_potyvir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001592; Poty_coat.
DR   InterPro; IPR001730; Potyv_NIa-pro_dom.
DR   InterPro; IPR039560; Potyvirid-P3.
DR   InterPro; IPR013648; PP_Potyviridae.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00863; Peptidase_C4; 1.
DR   Pfam; PF00851; Peptidase_C6; 1.
DR   Pfam; PF01577; Peptidase_S30; 1.
DR   Pfam; PF00767; Poty_coat; 1.
DR   Pfam; PF08440; Poty_PP; 1.
DR   Pfam; PF13608; Potyvirid-P3; 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; 2.
DR   PROSITE; PS51744; HC_PRO_CPD; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR   PROSITE; PS51871; PV_P1_PRO; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Capsid protein; Complete proteome;
KW   Covalent protein-RNA linkage; Helical capsid protein; Helicase;
KW   Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW   Protease; Ribosomal frameshifting; RNA-directed RNA polymerase;
KW   Serine protease; Suppressor of RNA silencing; Thiol protease;
KW   Transferase; Viral RNA replication; Virion.
FT   CHAIN         1   3085       Genome polyprotein.
FT                                /FTId=PRO_0000419994.
FT   CHAIN         1    313       P1 proteinase. {ECO:0000255}.
FT                                /FTId=PRO_0000040246.
FT   CHAIN       314    770       Helper component proteinase.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000040247.
FT   CHAIN       771   1117       Protein P3. {ECO:0000255}.
FT                                /FTId=PRO_0000040248.
FT   CHAIN      1118   1169       6 kDa protein 1. {ECO:0000250}.
FT                                /FTId=PRO_0000040249.
FT   CHAIN      1170   1803       Cytoplasmic inclusion protein.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040250.
FT   CHAIN      1804   1855       6 kDa protein 2. {ECO:0000250}.
FT                                /FTId=PRO_0000040251.
FT   CHAIN      1856   2046       Viral genome-linked protein.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040252.
FT   CHAIN      2047   2293       Nuclear inclusion protein A.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040253.
FT   CHAIN      2294   2809       Nuclear inclusion protein B.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000040254.
FT   CHAIN      2810   3085       Capsid protein.
FT                                /FTId=PRO_0000040255.
FT   DOMAIN      170    313       Peptidase S30. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01219}.
FT   DOMAIN      648    770       Peptidase C6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01080}.
FT   DOMAIN     1241   1393       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1412   1571       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     2047   2266       Peptidase C4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00766}.
FT   DOMAIN     2535   2659       RdRp catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00539}.
FT   NP_BIND    1254   1261       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       365    368       Involved in interaction with stylet and
FT                                aphid transmission. {ECO:0000250}.
FT   MOTIF       622    624       Involved in virions binding and aphid
FT                                transmission. {ECO:0000250}.
FT   MOTIF      1343   1346       DESH box.
FT   MOTIF      1895   1904       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   ACT_SITE    224    224       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    233    233       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    266    266       For P1 proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   ACT_SITE    656    656       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE    729    729       For helper component proteinase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   ACT_SITE   2092   2092       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2127   2127       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   ACT_SITE   2198   2198       For nuclear inclusion protein A activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00766}.
FT   SITE        313    314       Cleavage; by P1 proteinase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01219}.
FT   SITE        770    771       Cleavage; by autolysis.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01080}.
FT   SITE       1117   1118       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1169   1170       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1803   1804       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       1855   1856       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2046   2047       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2293   2294       Cleavage; by NIa-pro. {ECO:0000250}.
FT   SITE       2809   2810       Cleavage; by NIa-pro. {ECO:0000250}.
FT   MOD_RES    1919   1919       O-(5'-phospho-RNA)-tyrosine.
FT                                {ECO:0000250}.
SQ   SEQUENCE   3085 AA;  349731 MW;  918576B242794C0D CRC64;
     MATMMHFGQF PSNIPLRAAT CCTKVHSTLV TKEMMASSVK PAESSSVARP IIYSSAATDG
     YEKAQRAFEA SFREKYSGKL EAMKYGKMVK KGGLTYVKRA GPQAIAKGIE MDAAIEKFNT
     AFNAGELENV TLEGDITAGI SVARGESVWL RSVFWSRSLK KQARKKTPKL VAKSDFDDLF
     NKVLKVASLG NIPVEIVGKK ANKILRCGYR RVNTSTIPYF HLPHHNSNYI CRELHPQRVR
     WLVPLLVRHR KIRDQFSDSM IARGWSGLIL PKYIASTCGR RYDEVIVRGR LYGRVEDART
     KLPAGDVGRT MHYSSGEERF FAGWKEGFEK LVPAQKEHIC KIVQDNKFCG KLAASIVQIA
     FPCHKMACDV CRNKFNEMTP EAYSELIDKH IDQRMNEINE AIVRFPGLKQ VVSNFRSKHI
     ASTNIKDNLE VAKLTQGHKA NQMMQLARIN SILIKGNTAT PSEISDASGL LLEITRWFNN
     HLSVIDKGSL RAFRNKRSSK ALVNPSLLCD NQRDKNGNFI WGERGYHSKR FFASHFDEVT
     PGDGYKEYII RKGPQGQRKL AIGNLIVSFD LEKTRQALKG EEVEKLPLSN SCVSKRNGNY
     VYTSCCVTLD DGTPLYSNIK NPTKRHLVVG TTGDPKIVDL PATDTDKMYI AKEGYCYLNI
     FLAMLINVNE NEAKAFTKMV RDIIIPMLGT WPTMQDLATA CFMMTAFFPE TSSAELPRIL
     VDHTNQTMHV IDSFGSLTTG YHVLKAGTAA QLIDFASTEL EGEMKWYRVG GHGLPVKEKM
     ISALITSIFR PKKLVYLIEE DPYVLIMAMC SPRLIISLFN NGALELAAKH WISRDKNVSA
     IFAMLMDLST EMSKAELLIE QHRMINECAK RVHDTQNYLD EVGPHQQEVR TFLALISDEL
     EADKELHKTG FANFSERFHS LTEKMYVDAL EEEWRGLSLL DRFSYATFVY KHKPRSTSVL
     PPKKSEDIDA KFVISPSWFV GKTKEHLSGG RKYVTSQITQ FTSYIKRATL DRAMRIMCSC
     LKDLAYFMNV ALVTHLLISM IAAVYNMLND HRIAKRRLYI LEMQETNTAI WHLYDTWKTV
     NQRDPTHEEF RKYVAKVNKN LLRHLPEEED KAEVEYQANK VYEKKLEKAV ALMALFTMIF
     DTEKSGAVFS ILRNIKSVFS TLGEEVKYQS LDEIQSIEDE KKLTIDFDLD TEITAEHTTM
     DVQFEKWWDK QLSQNRVVPH YRVGGTFIEF TRHTAASVCN TICASSEQEF VVRGAVGSGK
     STGLPSHLSR KGRVLLLEPT RPLAENVCKQ LRKEPFHLSP TLRMRGLTTF GSSNISVMTS
     GYALHFHANN PQRLEEFDFI MIDESHTMDS STMAFYCLLR EYEFKGKILK VSATPPGREC
     EFKTQHDVLI KIEESLSYNS FVTAQGTGSN ADVVQNGDNI LVYVPSYNDV DQLSKGLMEK
     GHLVTKVDGR TMKMGNVEIP TKGTSSKKHF IVATNIIENG VTLDIDVVVD FGLKVVAELD
     SDSRCMRYKK VSISYGERLQ RLGRVGRVKQ GTALRIGHTE TGMTEIPVAI ATEAAFICFA
     YNLPVMTHNV TSSLLSRCTN RQARTMMQYE LSPFFMVELV HFNGCVHPQI ESKLKAYKLR
     DSETQLSTLA IPNSGTSRWK TVGEYKKLGV RIEADDNVRV PFAANGVPDR LYADLWETIQ
     QHKSDAGFGR LTSACASKIS YTLTTQPNAI PRTLAIIEHL LREEQQKKAY FESLNDTLCA
     TSFSLAGMVN NIRRRYLKDH SAHNINVLQN AKSQLNEFNS KAIDPERVGD IMGYGVLDTV
     QYQSATDVQK RLKLKGRWNG SLAATDLLIA GAVFAGGCWM LWEYTKSGNE IVQYQGKRRQ
     MQKLKFRNAR DNKVGREVYG DDGTIEHFFG AAYTERGKRK GNNSTKGMGT KTRRFVHMYG
     FDPTEYSFVR FVDPLTGYSK DESVQTDISL VQSEIGEYRQ KCMEDDDELI DFIKQKPGIQ
     AYFMKNGSDK ALQVDLTPHI PLLSCAKTAT IAGFPERESE LRQTGTPIVV NKNVVPGEHK
     EVVREEGKSI VKGLRNYNPI SSVVCRLTND SNGNAQTLYG VGFGPLIITN SHLFKMNNGT
     LFVRSHQGEF TVQNTTQLQI YHVKDKDMIL IRMPKDFPPF PMKLKFRAPH SEERACLVGS
     RFQQKSLSSE VSDSTLIRPT DSGSGYWKHW VSTKEGDCGL PMVALKDGSL IGIHGLTSVR
     SELNYFVPFT DDFQSKYLSN IESLEWVKHW RHTPDKVAWN GMTLRENGPA SEFSVSKLIA
     DLTHGYVDEV VEQGYSSKWV ANRLDGNLKA VASSSSQLVT KHVVKGPCVL FQEFLATHEE
     AARYFVPRMG EYGPSRLNKE AFLKDFLKYA GPITVGVVNT NSFEDAVASV INMLEDLDYG
     ECAYVTDPDS IFDSLNMKAA VGALYKGKKK EYFEQLNTTE REDLLRLSCE RLYEGKMGVW
     NGSLKAELRP KEKLEQNKTR TFTAAPIDTL LGGKVCVDDF NNRFYSLNLK GPWSVGMTKF
     YGGWNELLQK LPDGWIYCDA DGSQFDSSLT PYLINAVVQI REHFMEDWEI GRTMLRNFYT
     EIVYTPILTP DGTIVKKFKG NNSGQPSTVV DNTLMVILAM HYAMHQQCWK EEEMKEKIRF
     FANGDDLLIA IYPSKEKFLN VLSEYFHELG LKYDFSSRST VRETLWFMSH RGLYLDDMYI
     PKLEEERIVS ILEWDRSNEA THRAEAICAA MIEAWGYPEL LKYIREFYLW MMQHECYRDL
     VRDGKLPYIA ETALRKLYTD KSVDENELVK YWKALAPEED DGPDIVTYQG DEKPSKSSQP
     QSSSPQVPQQ VDAGASSQGR DKQSVIKHDS TKSKDVGQSS TAVPRLKQIS KMRMPVSKGR
     QVLALDHLLD YKPEQVDLSN TRATKEQFDN WYEAVMREYD VSDSQMGVIM NGLMVWCIEN
     GTSPNLSGDW VMMDGEEQVS FPLKPIVENA KPSFRQIMHH FSDAAEAYIE MRNRERPYMP
     RYGAQRNLRD KTLARYAFDF YEVTSRTTDR AREAHFQMKA AALASVSNKL FGLDGSVATT
     SEDTERHTAT DVNAHMHHMM GVRQG
//
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