Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P09814

- POLG_TVMV

UniProt

P09814 - POLG_TVMV

Protein

Genome polyprotein

Gene
N/A
Organism
Tobacco vein mottling virus (TVMV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.
    Nuclear inclusion protein B: an RNA-dependent RNA polymerase that plays an essential role in the virus replication.
    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 By similarity.By similarity
    Cytoplasmic inclusion protein: has helicase activity. It may be involved in replication.
    Both 6K peptides are indispensable for virus replication.By similarity
    Nuclear inclusion protein A: has RNA-binding and proteolytic activities.

    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 sitei183 – 1831For P1 proteinase activityBy similarity
    Active sitei192 – 1921For P1 proteinase activitySequence Analysis
    Active sitei225 – 2251For P1 proteinase activityBy similarity
    Sitei274 – 2752Cleavage; by P1 proteinaseSequence Analysis
    Active sitei617 – 6171For helper component proteinase activityBy similarity
    Active sitei690 – 6901For helper component proteinase activityBy similarity
    Sitei731 – 7322Cleavage; by HC-proSequence Analysis
    Sitei1078 – 10792Cleavage; by NIa-proBy similarity
    Sitei1130 – 11312Cleavage; by NIa-proBy similarity
    Sitei1765 – 17662Cleavage; by NIa-proBy similarity
    Sitei1818 – 18192Cleavage; by NIa-proBy similarity
    Sitei2001 – 20022Cleavage; by NIa-proBy similarity
    Active sitei2047 – 20471For nuclear inclusion protein A activityPROSITE-ProRule annotation
    Active sitei2082 – 20821For nuclear inclusion protein A activityPROSITE-ProRule annotation
    Active sitei2152 – 21521For nuclear inclusion protein A activityPROSITE-ProRule annotation
    Sitei2242 – 22432Cleavage; by NIa-proBy similarity
    Sitei2758 – 27592Cleavage; by NIa-proBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1215 – 12228ATPPROSITE-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

    Protein family/group databases

    MEROPSiC04.003.

    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
    OrganismiTobacco vein mottling virus (TVMV)
    Taxonomic identifieri12228 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePotyviridaePotyvirus
    Virus hostiNicotiana tabacum (Common tobacco) [TaxID: 4097]
    Rumex [TaxID: 3618]
    ProteomesiUP000007549: 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 – 30233023Genome polyproteinPRO_0000420031Add
    BLAST
    Chaini1 – 274274P1 proteinaseSequence AnalysisPRO_0000040483Add
    BLAST
    Chaini275 – 731457Helper component proteinaseSequence AnalysisPRO_0000040484Add
    BLAST
    Chaini732 – 1078347Protein P3By similarityPRO_0000040485Add
    BLAST
    Chaini1079 – 1130526 kDa protein 1By similarityPRO_0000040486Add
    BLAST
    Chaini1131 – 1765635Cytoplasmic inclusion proteinBy similarityPRO_0000040487Add
    BLAST
    Chaini1766 – 1818536 kDa protein 2By similarityPRO_0000040488Add
    BLAST
    Chaini1819 – 2001183Viral genome-linked proteinBy similarityPRO_0000040489Add
    BLAST
    Chaini2002 – 2242241Nuclear inclusion protein ABy similarityPRO_0000040490Add
    BLAST
    Chaini2243 – 2758516Nuclear inclusion protein BBy similarityPRO_0000040491Add
    BLAST
    Chaini2759 – 3023265Capsid proteinBy similarityPRO_0000040492Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1878 – 18781O-(5'-phospho-RNA)-tyrosine
    Modified residuei1878 – 18781O-UMP-tyrosine; transient1 Publication

    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.
    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

    Miscellaneous databases

    PMAP-CutDBP09814.

    Structurei

    Secondary structure

    1
    3023
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2013 – 20164
    Beta strandi2019 – 20268
    Beta strandi2029 – 203810
    Beta strandi2041 – 20444
    Helixi2046 – 20494
    Beta strandi2055 – 20606
    Beta strandi2063 – 20697
    Helixi2070 – 20723
    Beta strandi2075 – 20773
    Beta strandi2080 – 20823
    Beta strandi2084 – 20874
    Beta strandi2110 – 21178
    Beta strandi2122 – 21309
    Beta strandi2138 – 21436
    Beta strandi2155 – 21584
    Turni2159 – 21613
    Beta strandi2164 – 21729
    Turni2173 – 21753
    Beta strandi2178 – 21825
    Helixi2187 – 21915
    Helixi2206 – 22083
    Beta strandi2754 – 27574

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MMGX-ray1.70A/B2002-2242[»]
    C/D2753-2760[»]
    ProteinModelPortaliP09814.
    SMRiP09814. Positions 2010-2221.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1202 – 1354153Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1367 – 1532166Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini2002 – 2218217Peptidase C4PROSITE-ProRule annotationAdd
    BLAST
    Domaini2484 – 2608125RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi325 – 3284Involved in interaction with stylet and aphid transmissionBy similarity
    Motifi583 – 5853Involved in virions binding and aphid transmissionBy similarity
    Motifi1304 – 13074DEFH box
    Motifi1856 – 18638Nuclear 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.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    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.
    PS51195. Q_MOTIF. 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: P09814-1) [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

    MAATMIFGSF THDLLGKAMS TIHSAVTAEK DIFSSIKERL ERKRHGKICR     50
    MKNGSIYIKA ASSTKVEKIN AAAKKLADDK AAFLKAQPTI VDKIIVNEKI 100
    QVVEAEEVHK REDVQTVFFK KTKKRAPKLR ATCSSSGLDN LYNAVANIAK 150
    ASSLRVEVIH KKRVCGEFKQ TRFGRALFID VAHAKGHRRR IDCRMHRREQ 200
    RTMHMFMRKT TKTEVRSKHL RKGDSGIVLL TQKIKGHLSG VRDEFFIVRG 250
    TCDDSLLEAR ARFSQSITLR ATHFSTGDIF WKGFNASFQE QKAIGLDHTC 300
    TSDLPVEACG HVAALMCQSL FPCGKITCKR CIANLSNLDF DTFSELQGDR 350
    AMRILDVMRA RFPSFTHTIR FLHDLFTQRR VTNPNTAAFR EILRLIGDRN 400
    EAPFAHVNRL NEILLLGSKA NPDSLAKASD SLLELARYLN NRTENIRNGS 450
    LKHFRNKISS KAHSNLALSC DNQLDQNGNF LWGLAGIAAK RFLNNYFETI 500
    DPEQGYDKYV IRKNPNGERK LAIGNFIIST NLEKLRDQLE GESIARVGIT 550
    EECVSRKDGN YRYPCCCVTL EDGSPMYSEL KMPTKNHLVI GNSGDPKYLD 600
    LPGEISNLMY IAKEGYCYIN IFLAMLVNVD EANAKDFTKR VRDESVQKLG 650
    KWPSLIDVAT ECALLSTYYP AAASAELPRL LVDHAQKTIH VVDSYGSLNT 700
    GYHILKANTV SQLEKFASNT LESPMAQYKV GGLVYSENND ASAVKALTQA 750
    IFRPDVLSEL IEKEPYLMVF ALVSPGILMA MSNSGALEFG ISKWISSDHS 800
    LVRMASILKT LASKVSVADT LALQKHIMRQ NANFLCGELI NGFQKKKSYT 850
    HATRFLLMIS EENEMDDPVL NAGYRVLEAS SHEIMEKTYL ALLETSWSDL 900
    SLYGKFKSIW FTRKHFGRYK AELFPKEQTD LQGRYSNSLR FHYQSTLKRL 950
    RNKGSLCRER FLESISSARR RTTCAVFSLL HKAFPDVLKF INTLVIVSLS 1000
    MQIYYMLVAI IHEHRAAKIK SAQLEERVLE DKTMLLYDDF KAKLPEGSFE 1050
    EFLEYTRQRD KEVYEYLMME TTEIVEFQAK NTGQASLERI IAFVSLTLML 1100
    FDNERSDCVY KILTKFKGIL GSVENNVRFQ SLDTIVPTQE EKNMVIDFEL 1150
    DSDTAHTPQM QEQTFSDWWS NQIANNRVVP HYRTEGYFMQ FTRNTASAVS 1200
    HQIAHNEHKD IILMGAVGSG KSTGLPTNLC KFGGVLLLEP TRPLAENVTK 1250
    QMRGSPFFAS PTLRMRNLST FGSSPITVMT TGFALHFFAN NVKEFDRYQF 1300
    IIFDEFHVLD SNAIAFRNLC HEYSYNGKII KVSATPPGRE CDLTTQYPVE 1350
    LLIEEQLSLR DFVDAQGTDA HADVVKKGDN ILVYVASYNE VDQLSKMLNE 1400
    RGFLVTKVDG RTMKLGGVEI ITKGSSIKKH FIVATNIIEN GVTLDVDVVV 1450
    DFGLKVVPNL DSDNRLVSYC KIPISLGERI QRFGRVGRNK PGVALRIGET 1500
    IKGLVEIPSM IATEAAFLCF VYGLPVTTQN VSTSILSQVS VRQARVMCQF 1550
    ELPIFYTAHL VRYDGAMHPA IHNALKRFKL RDSEINLNTL AIPTSSSKTW 1600
    YTGKCYKQLV GRLDIPDEIK IPFYTKEVPE KVPEQIWDVM VKFSSDAGFG 1650
    RMTSAAACKV AYTLQTDIHS IQRTVQIIDR LLENEMKKRN HFNLVVNQSC 1700
    SSHFMSLSSI MASLRAHYAK NHTGQNIEIL QKAKAQLLEF SNLAIDPSTT 1750
    EALRDFGYLE AVRFQSESEM ARGLKLSGHW KWSLISRDLI VVSGVGIGLG 1800
    CMLWQFFKEK MHEPVKFQGK SRRRLQFRKA RDDKMGYIMH GEGDTIEHFF 1850
    GAAYTKKGKS KGKTHGAGTK AHKFVNMYGV SPDEYSYVRY LDPVTGATLD 1900
    ESPMTDLNIV QEHFGEIRRE AILADAMSPQ QRNKGIQAYF VRNSTMPILK 1950
    VDLTPHIPLK VCESNNIAGF PEREGELRRT GPTETLPFDA LPPEKQEVAF 2000
    ESKALLKGVR DFNPISACVW LLENSSDGHS ERLFGIGFGP YIIANQHLFR 2050
    RNNGELTIKT MHGEFKVKNS TQLQMKPVEG RDIIVIKMAK DFPPFPQKLK 2100
    FRQPTIKDRV CMVSTNFQQK SVSSLVSESS HIVHKEDTSF WQHWITTKDG 2150
    QCGSPLVSII DGNILGIHSL THTTNGSNYF VEFPEKFVAT YLDAADGWCK 2200
    NWKFNADKIS WGSFTLVEDA PEDDFMAKKT VAAIMDDLVR TQGEKRKWML 2250
    EAAHTNIQPV AHLQSQLVTK HIVKGRCKMF ALYLQENADA RDFFKSFMGA 2300
    YGPSHLNKEA YIKDIMKYSK QIVVGSVDCD TFESSLKVLS RKMKEWGFEN 2350
    LEYVTDEQTI KNALNMDAAV GALYSGKKKQ YFEDLSDDAV ANLVQKSCLR 2400
    LFKNKLGVWN GSLKAELRPF EKLIENKTRT FTAAPIETLL GGKVCVDDFN 2450
    NHFYSKHIQC PWSVGMTKFY GGWNELLGKL PDGWVYCDAD GSQFDSSLSP 2500
    YLINAVLRLR LSSMEEWDVG QKMLQNLYTE IVYTPISTPD GTIVKKFKGN 2550
    NSGQPSTVVD NTLMVVLAMY YALSKLGVDI NSQEDVCKFF ANGDDLIIAI 2600
    SPELEHVLDG FQQHFSDLGL NYDFSSRTRD KKELWFMSHR ALSKDGILIP 2650
    KLEPERIVSI LEWDRSAEPH HRLEAICASM IEAWGYTDLL QNIRRFYKWT 2700
    IEQEPYRSLA EQGLAPYLSE VALRRLYTSQ IATDNELTDY YKEILANNEF 2750
    LRETVRFQSD TVDAGKDKAR DQKLADKPTL AIDRTKDKDV NTGTSGTFSI 2800
    PRLKKAAMNM KLPKVGGSSV VNLDHLLTYK PAQEFVVNTR ATHSQFKAWH 2850
    TNVMAELELN EEQMKIVLNG FMIWCIENGT SPNISGVWTM MDGDEQVEYP 2900
    IEPMVKHANP SLRQIMKHFS NLAEAYIRMR NSEQVYIPRY GLQRGLVDRN 2950
    LAPFAFDFFE VNGATPVRAR EAHAQMKAAA LRNSQQRMFC LDGSVSGQEE 3000
    NTERHTVDDV NAQMHHLLGV KGV 3023

    Note: Produced by conventional translation.

    Length:3,023
    Mass (Da):342,285
    Last modified:May 30, 2000 - v2
    Checksum:i299FDED15C0E5B87
    GO
    Isoform P3N-PIPO polyprotein (identifier: P0CK10-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry P0CK10.
    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:977
    Mass (Da):109,980
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04083 Genomic RNA. Translation: CAA27720.1.
    PIRiA23647. GNVSTV.
    RefSeqiNP_056867.1. NC_001768.1. [P09814-1]

    Genome annotation databases

    GeneIDi1494056.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04083 Genomic RNA. Translation: CAA27720.1 .
    PIRi A23647. GNVSTV.
    RefSeqi NP_056867.1. NC_001768.1. [P09814-1 ]

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MMG X-ray 1.70 A/B 2002-2242 [» ]
    C/D 2753-2760 [» ]
    ProteinModelPortali P09814.
    SMRi P09814. Positions 2010-2221.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C04.003.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1494056.

    Miscellaneous databases

    PMAP-CutDB P09814.

    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.
    IPR014014. RNA_helicase_DEAD_Q_motif.
    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.
    PS51195. Q_MOTIF. 1 hit.
    PS50507. RDRP_SSRNA_POS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Shaw J.G.
      Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "A tyrosine residue in the small nuclear inclusion protein of tobacco vein mottling virus links the VPg to the viral RNA."
      Murphy J.F., Rychlik W., Rhoads R.E., Hunt A.G., Shaw J.G.
      J. Virol. 65:511-513(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1874-1888, COVALENT RNA-LINKAGE AT TYR-1878 OF VPG, URIDYLYLATION AT TYR-1878.
    4. Cited for: REVIEW.

    Entry informationi

    Entry nameiPOLG_TVMV
    AccessioniPrimary (citable) accession number: P09814
    Secondary accession number(s): Q84898
    , Q84899, Q84900, Q84901, Q84902
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 131 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

    3D-structure, Complete proteome, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3