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P18247

- POLG_PVYN

UniProt

P18247 - POLG_PVYN

Protein

Genome polyprotein

Gene
N/A
Organism
Potato virus Y (strain N) (PVY)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Capsid protein: involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.1 Publication
    Nuclear inclusion protein B: an RNA-dependent RNA polymerase that plays an essential role in the virus replication.1 Publication
    Helper component proteinase: required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.1 Publication
    Cytoplasmic inclusion protein: has helicase activity. It may be involved in replication.1 Publication
    Both 6K peptides are indispensable for virus replication.By similarity
    Nuclear inclusion protein A: has RNA-binding and proteolytic activities.1 Publication

    Catalytic activityi

    Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
    Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei192 – 1921For P1 proteinase activityBy similarity
    Active sitei201 – 2011For P1 proteinase activitySequence Analysis
    Active sitei235 – 2351For P1 proteinase activityBy similarity
    Sitei284 – 2852Cleavage; by P1 proteinaseSequence Analysis
    Active sitei626 – 6261For helper component proteinase activityBy similarity
    Active sitei699 – 6991For helper component proteinase activityBy similarity
    Sitei740 – 7412Cleavage; by HC-proSequence Analysis
    Sitei1105 – 11062Cleavage; by NIa-proBy similarity
    Sitei1157 – 11582Cleavage; by NIa-proBy similarity
    Sitei1791 – 17922Cleavage; by NIa-proBy similarity
    Sitei1843 – 18442Cleavage; by NIa-proBy similarity
    Sitei2031 – 20322Cleavage; by NIa-proBy similarity
    Active sitei2077 – 20771For nuclear inclusion protein A activityPROSITE-ProRule annotation
    Active sitei2112 – 21121For nuclear inclusion protein A activityPROSITE-ProRule annotation
    Active sitei2182 – 21821For nuclear inclusion protein A activityPROSITE-ProRule annotation
    Sitei2275 – 22762Cleavage; by NIa-proBy similarity
    Sitei2796 – 27972Cleavage; by NIa-proBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1242 – 12498ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cysteine-type endopeptidase activity Source: InterPro
    3. helicase activity Source: UniProtKB-KW
    4. RNA binding Source: InterPro
    5. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    6. structural molecule activity Source: InterPro

    GO - Biological processi

    1. RNA-protein covalent cross-linking Source: UniProtKB-KW
    2. transcription, DNA-templated Source: InterPro
    3. viral RNA genome replication Source: InterPro

    Keywords - Molecular functioni

    Helicase, Hydrolase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Suppressor of RNA silencing, Thiol protease, Transferase

    Keywords - Biological processi

    Viral RNA replication

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.4.22.45. 5005.

    Protein family/group databases

    MEROPSiC04.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 10 chains:
    Alternative name(s):
    N-terminal protein
    Helper component proteinase (EC:3.4.22.45)
    Short name:
    HC-pro
    6 kDa protein 1
    Short name:
    6K1
    6 kDa protein 2
    Short name:
    6K2
    Alternative name(s):
    VPg
    Nuclear inclusion protein A (EC:3.4.22.44)
    Short name:
    NI-a
    Short name:
    NIa
    Alternative name(s):
    49 kDa proteinase
    Short name:
    49 kDa-Pro
    NIa-pro
    Nuclear inclusion protein B (EC:2.7.7.48)
    Short name:
    NI-b
    Short name:
    NIb
    Alternative name(s):
    RNA-directed RNA polymerase
    Capsid protein
    Short name:
    CP
    Alternative name(s):
    Coat protein
    OrganismiPotato virus Y (strain N) (PVY)
    Taxonomic identifieri12219 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePotyviridaePotyvirus
    Virus hostiCapsicum (peppers) [TaxID: 4071]
    Nicotiana [TaxID: 4085]
    Solanum lycopersicum (Tomato) (Lycopersicon esculentum) [TaxID: 4081]
    Solanum tuberosum (Potato) [TaxID: 4113]
    ProteomesiUP000000520: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. helical viral capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Helical capsid protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 30633063Genome polyproteinPRO_0000420017Add
    BLAST
    Chaini1 – 284284P1 proteinaseSequence AnalysisPRO_0000040407Add
    BLAST
    Chaini285 – 740456Helper component proteinaseSequence AnalysisPRO_0000040408Add
    BLAST
    Chaini741 – 1105365Protein P3By similarityPRO_0000040409Add
    BLAST
    Chaini1106 – 1157526 kDa protein 1By similarityPRO_0000040410Add
    BLAST
    Chaini1158 – 1791634Cytoplasmic inclusion proteinBy similarityPRO_0000040411Add
    BLAST
    Chaini1792 – 1843526 kDa protein 2By similarityPRO_0000040412Add
    BLAST
    Chaini1844 – 2031188Viral genome-linked proteinBy similarityPRO_0000040413Add
    BLAST
    Chaini2032 – 2275244Nuclear inclusion protein ABy similarityPRO_0000040414Add
    BLAST
    Chaini2276 – 2796521Nuclear inclusion protein BBy similarityPRO_0000040415Add
    BLAST
    Chaini2797 – 3063267Capsid proteinBy similarityPRO_0000040416Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1907 – 19071O-(5'-phospho-RNA)-tyrosineBy similarity

    Post-translational modificationi

    VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.By similarity
    Potyviral RNA is expressed as two polyproteins which undergo post-translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI By similarity.By similarity

    Keywords - PTMi

    Covalent protein-RNA linkage, Phosphoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliP18247.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1229 – 1381153Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1400 – 1559160Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini2032 – 2250219Peptidase C4PROSITE-ProRule annotationAdd
    BLAST
    Domaini2519 – 2643125RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi334 – 3374Involved in interaction with stylet and aphid transmissionBy similarity
    Motifi592 – 5943Involved in virions binding and aphid transmissionBy similarity
    Motifi1331 – 13344DECH box
    Motifi1884 – 18929Nuclear localization signalSequence Analysis

    Domaini

    The N-terminus of helper component proteinase is involved in interaction with stylets. The central part is involved in interaction with virions and the C-terminus is involved in cell-to cell movement of the virus.

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 peptidase C4 domain.PROSITE-ProRule annotation
    Contains 1 peptidase C6 domain.Curated
    Contains 1 peptidase S30 domain.Curated
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR002540. Pept_S30_P1_potyvir.
    IPR001456. Peptidase_C6.
    IPR001592. Poty_coat.
    IPR001730. Potyv_NIa-pro_dom.
    IPR013648. PP_Potyviridae.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF00863. Peptidase_C4. 1 hit.
    PF00851. Peptidase_C6. 1 hit.
    PF01577. Peptidase_S30. 1 hit.
    PF00767. Poty_coat. 1 hit.
    PF08440. Poty_PP. 1 hit.
    PF00680. RdRP_1. 1 hit.
    [Graphical view]
    PRINTSiPR00966. NIAPOTYPTASE.
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 2 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51436. POTYVIRUS_NIA_PRO. 1 hit.
    PS50507. RDRP_SSRNA_POS. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

    Isoform Genome polyprotein (identifier: P18247-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MATYMSTICF GSFECKLPYS PASCEHIVKE REVPASVDPF ADLETQLSAR     50
    LLKQKYATVR VLKNGTFTYR YKTDAQIMRI QKKLERKDRE EYHFQMAAPS 100
    IVSKITIAGG DPPSKSEPQA PRGIIHTTPR MRKVKTRPII KLTEGQMNHL 150
    IKQIKQIMSE KRGSVHLISK KTTHVQYKKI LGAYSAAVRT AHMMGLRRRV 200
    DFRCDMWTVG LLQRLARTDK WSNQVRTINI RRGDSGVILN TKSLKGHFGR 250
    SSGGLFIVRG SHEGKLYDAR SRVTQSILNS MIQFSNADNF WKGLDGNWAR 300
    MRYPSDHTCV AGLPVEDCGR VAALMAHSIL PCYKITCPTC AQQYASLPVS 350
    DLFKLLHKHA RDGLNRLGAD KDRFIHVNKF LIALEHLTEP VDLNLELFNE 400
    IFKSIGEKQQ APFKNLNVLN NFFLKGKENT AHEWQVAQLS LLELARFQKN 450
    RTDNIKKGDI SFFRNKLSAK ANWNLYLSCD NQLDKNANFL WGQREYHAKR 500
    FFSNFFEEID PAKGYSAYEI RKHPSGTRKL SIGNLVVPLD LAEFRQKMKG 550
    DYRKQPGVSK KCTSSKDGNY VYPCCCTTLD DGSAIESTFY PPTKKHLVIG 600
    NSGDQKFVDL PKGDSEMLYI AKQGYCYINV FLAMLINISE EDAKDFTKKV 650
    RDMCVPKLGT WPTMMDLATT CAQMRIFYPD VHDAELPRIL VDHDTQTCHV 700
    VDSFGSQTTG YHILKASSVS QLILFANDEL ESDIKHYRVG GVPNASPELG 750
    STISPFREGG VIMSESAALK LLLKGIFRPK VMRQLLLDEP YLLILSILSP 800
    GILMAMYNNG IFELAVRLWI NEKQSIAMIA SLLSALALRV SAAETLVAQR 850
    IIIDAAATDL LDATCDGFNL HLTYPTALMV LQVVKNRNEC DDTLFKAGFP 900
    SYNTSVVQIM EKNYLNLLND AWKDLTWREN YPQHGTHTEQ NALSTRYIKP 950
    TEKADLKGLY NISPQAFLGR SAQVVKGTAS GLSERFNNYF NTKCVNISSF 1000
    FIRRIFRRLP TFVTFVNSLL VISMLTSVVA VCQAIILDQR KYRREIELMQ 1050
    IEKNEIVCME LYASLQRKLE RDFTWDEYIE YLKSVNPQIV QFAQAQMEEY 1100
    DVRHQRSTPV VKNLEQVVAF MALVIMVFDA ERSDCVFKTL NKFKGVLSSL 1150
    DYEVRHQSLD DVIKNFDERN EIIDFELSED TIRTSSVLDT KFSDWWDRQI 1200
    QMGHTLPHYR TEGHFMEFTR ATAVQVANDI AHSEHLDFLV RGAVGSGKST 1250
    GLPVHLSVAG SVLLIEPTRP LAENVFKQLS SEPFFKKPTL RMRGNSIFGS 1300
    SPISVMTSGF ALHYFANNRS QLAQFNFVIF DECHVLDPSA MAFRSLLSVY 1350
    HQACKVLKVS ATPVGREVEF TTQQPVKLIV EDTVSFQSFV DAQGSKTNAD 1400
    VVQFGSNVLV YVSSYNEVDT LAKLLTDKNM MVTKVDGRTM KHGCLEIVTK 1450
    GTSARPHFVV ATNIIENGVT LDIDVVVDFG LKVSPFLDID NRSIAYNKVS 1500
    VSYGERIQRL GRVGRFKKGV ALRIGHTEKG IIEIPSMVAT EAALACFAYN 1550
    LPVMTGGVST SLIGNCTVRQ VKTMQQFELS PFFIQNFVAH DGSMHPVIHD 1600
    ILKKYKLRDC MTPLCDQSIP YRASSTWLSV SEYERLGVAL EIPKQVKIAF 1650
    HIKEIPPKLH EMLWETVVKY KDVCLFPSIR ASSISKIAYT LRTDLFAIPR 1700
    TLILVERLLE EERVKQSQFR SLIDEGCSSM FSIVNLTNTL RARYAKDYTA 1750
    ENIQKLEKVR SQLKEFSNLD GSACEENLIK RYESLQFVHH QAATSLAKDL 1800
    KLKGIWNKSL VAKDLIIAGA VAIGGIGLIY SWFTQSVETV SHQGKNKSKR 1850
    IQALKFRHAR DKRAGFEIDN NDDTIEEFFG SAYRKKGKGK GTTVGMGKSS 1900
    RRFINMYGFD PTEYSFIQFV DPLTGRQIEE NVYADIRDIQ ERFSEVRKKM 1950
    VENDDIEMQA LGSNTTIHAY FRKDWCDKAL KIDLMPHNPL KVCDKTNGIA 2000
    KFPERELELR QTGPAVEVDV KDIPAQEVEH EAKSLMRGLR DFNPIAQTVC 2050
    RLKVSVEYGA SEMYGFGFGA YIVANHHLFR SYNGSMEVQS MHGTFRVKNL 2100
    HSLSVLPIKG RDIILIKMPK DFPVFPQKLH FRAPTQNERI CLVGTNFQEK 2150
    YASSIITETS TTYNIPGSTF WKHWIETDNG HCGLPVVSTA DGCIVGIHSL 2200
    ANNAHTTNYY SAFDEDFESK YLRTNEHNEW VKSWVYNPDT VLWGPLKLKD 2250
    STPKGLFKTT KLVQDLIDHD VVVEQAKHSA WMFEALTGNL QAVATMKSQL 2300
    VTKHVVKGEC RHFTEFLTVD AEAEAEAFFR PLMDAYGKSL LNRDAYIKDI 2350
    MKYSKPIDVG VVDRMHLRKP SIGLSSTCNV HGFKKCAYVT DEQEIFKALN 2400
    MKAAVGASYG CKKKDYFEHF TDADKEEIVM QSCLRLYKGL LGIWNGSLKA 2450
    ELRCKEKILA NKTRTFTAAP LDTLLGGKVC VDDFNNQFYS KNIECCWTVG 2500
    MTKFYGGWDK LLRRLPENWV YCDADGSQFD SSLTPYLINA VLTIRSTYME 2550
    DWDVGLQMLR NLYTEIVYTP ISTPDGTIVK KFRGNNSGQP STVVDNSLMV 2600
    VLAMHYALIK ECVEFEEIDS TCVFFVNGDD LLIAVNPEKE SILDRMSQHF 2650
    SDLGLNYDFS SRTRRKEELW FMSHRGLLIE GMYVPKLEEE RIVSILQWDR 2700
    ADLPEHRLEA ICAAMIESWG YSELTHQIRR FYSWLLQQQP FATIAQEGKA 2750
    PYIASMALRK LYMDRAVDEE ELRAFTEMMV ALDDEFELDS YEVHHQANDT 2800
    IDAGGSNKKD AKPEQGSIQP NPNKGKDKDV NAGTSGTHTV PRIKAITSKM 2850
    RMPTSKGATV PNLEHLLEYA PQQIDISNTR ATQSQFDTWY EAVRMAYDIG 2900
    ETEMPTVMNG LMVWCIENGT SPNVNGVWVM MDGNEQVEYP LKPIVENAKP 2950
    TLRQIMAHFS DVAEAYIEMR NKKEPYMPRY GLIRNLRDMG LARYAFDFYE 3000
    VTSRTPVRAR EAHIQMKAAA LKSAQPRLFG LDGGISTQEE NTERHTTEDV 3050
    SPSMHTLLGV KNM 3063

    Note: Produced by conventional translation.

    Length:3,063
    Mass (Da):347,539
    Last modified:February 1, 1996 - v2
    Checksum:i3EC79125DE33F1BB
    GO
    Isoform P3N-PIPO polyprotein (identifier: P0CJ93-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry P0CJ93.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by -1 ribosomal frameshifting in P3 ORF.

    Length:986
    Mass (Da):111,724
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12456 Genomic RNA. Translation: CAA30988.1.
    D00441 Genomic RNA. Translation: BAA00342.1.
    PIRiJS0166.
    RefSeqiNP_056759.1. NC_001616.1.

    Genome annotation databases

    GeneIDi1494052.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12456 Genomic RNA. Translation: CAA30988.1 .
    D00441 Genomic RNA. Translation: BAA00342.1 .
    PIRi JS0166.
    RefSeqi NP_056759.1. NC_001616.1.

    3D structure databases

    ProteinModelPortali P18247.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C04.002.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1494052.

    Enzyme and pathway databases

    BRENDAi 3.4.22.45. 5005.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR002540. Pept_S30_P1_potyvir.
    IPR001456. Peptidase_C6.
    IPR001592. Poty_coat.
    IPR001730. Potyv_NIa-pro_dom.
    IPR013648. PP_Potyviridae.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF00863. Peptidase_C4. 1 hit.
    PF00851. Peptidase_C6. 1 hit.
    PF01577. Peptidase_S30. 1 hit.
    PF00767. Poty_coat. 1 hit.
    PF08440. Poty_PP. 1 hit.
    PF00680. RdRP_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00966. NIAPOTYPTASE.
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 2 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51436. POTYVIRUS_NIA_PRO. 1 hit.
    PS50507. RDRP_SSRNA_POS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of potato virus Y (N Strain) genomic RNA."
      Robaglia C., Durand-Tardif M., Tronchet M., Boudazin G., Astier-Manifacier S., Casse-Delbart F.
      J. Gen. Virol. 70:935-947(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Durand-Tardif M.
      Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Suppression of gene silencing: a general strategy used by diverse DNA and RNA viruses of plants."
      Voinnet O., Pinto Y.M., Baulcombe D.C.
      Proc. Natl. Acad. Sci. U.S.A. 96:14147-14152(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. Cited for: REVIEW.

    Entry informationi

    Entry nameiPOLG_PVYN
    AccessioniPrimary (citable) accession number: P18247
    Secondary accession number(s): Q85266
    , Q85267, Q85268, Q85269, Q85270, Q85271, Q85272, Q85273
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3