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Q6WQ42

- POLG_AEVL2

UniProt

Q6WQ42 - POLG_AEVL2

Protein

Genome polyprotein

Gene
N/A
Organism
Avian encephalomyelitis virus (strain L2Z) (AEV)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes By similarity.By similarity
    Protein VP0: VP0 precursor is a component of immature procapsids. The N-terminal domain of VP0, protein VP4, is needed for the assembly of 12 pentamers into the icosahedral structure. Unlike other picornaviruses, AEV VP4 may not be myristoylated By similarity.By similarity
    Protein 2B and 2BC precursor affect membrane integrity and cause an increase in membrane permeability.By similarity
    Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity.By similarity
    Protein 3A, via its hydrophobic domain, serves as membrane anchor.By similarity
    Protein 3B is covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. It acts as a genome-linked replication primer By similarity.By similarity
    Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease By similarity.By similarity
    RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.PROSITE-ProRule annotation

    Catalytic activityi

    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
    Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
    NTP + H2O = NDP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei19 – 202CleavageSequence Analysis
    Sitei242 – 2432Cleavage; by protease 3CSequence Analysis
    Sitei487 – 4882Cleavage; by protease 3CSequence Analysis
    Sitei757 – 7582Cleavage; by hostSequence Analysis
    Sitei806 – 8072Cleavage; by protease 3CBy similarity
    Sitei1021 – 10222Cleavage; by protease 3CSequence Analysis
    Sitei1347 – 13482Cleavage; by protease 3CSequence Analysis
    Sitei1412 – 14132Cleavage; by protease 3CSequence Analysis
    Sitei1433 – 14342Cleavage; by protease 3CSequence Analysis
    Active sitei1477 – 14771For protease 3C activityBy similarity
    Active sitei1515 – 15151For protease 3C activityBy similarity
    Active sitei1603 – 16031For protease 3C activityBy similarity
    Sitei1648 – 16492Cleavage; by protease 3CBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1153 – 11608ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    2. protein oligomerization Source: UniProtKB-KW
    3. RNA-protein covalent cross-linking Source: UniProtKB-KW
    4. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
    5. transcription, DNA-templated Source: InterPro
    6. viral entry into host cell Source: UniProtKB-KW
    7. viral RNA genome replication Source: InterPro
    8. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

    Keywords - Biological processi

    Host-virus interaction, Ion transport, Transport, Viral attachment to host cell, Viral RNA replication, Virus entry into host cell

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 12 chains:
    Alternative name(s):
    VP4-VP2
    Alternative name(s):
    P1A
    Virion protein 4
    Alternative name(s):
    P1B
    Virion protein 2
    Alternative name(s):
    P1C
    Virion protein 3
    Alternative name(s):
    P1D
    Virion protein 1
    Protein 2A
    Short name:
    P2A
    Protein 2B
    Short name:
    P2B
    Protein 2C (EC:3.6.1.15)
    Short name:
    P2C
    Protein 3A
    Short name:
    P3A
    Protein 3B
    Short name:
    P3B
    Alternative name(s):
    VPg
    Protease 3C (EC:3.4.22.28)
    Short name:
    P3C
    Alternative name(s):
    Picornain 3C
    OrganismiAvian encephalomyelitis virus (strain L2Z) (AEV)
    Taxonomic identifieri475780 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeTremovirus
    Virus hostiAnas (ducks) [TaxID: 8835]
    Gallus gallus (Chicken) [TaxID: 9031]
    Phasianidae [TaxID: 9005]
    ProteomesiUP000006886: Genome

    Subcellular locationi

    Chain Protein 2B : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.By similarity
    Chain Protein 2C : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. May associate with membranes through a N-terminal amphipathic helix By similarity.By similarity
    Chain Protein 3A : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.By similarity
    Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
    Note: Interacts with membranes in a complex with viral protein 3AB. Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum By similarity.By similarity

    GO - Cellular componenti

    1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    2. integral to membrane of host cell Source: UniProtKB-KW
    3. membrane Source: UniProtKB-KW
    4. viral capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 21342134Genome polyproteinBy similarityPRO_0000310521Add
    BLAST
    Chaini1 – 242242Protein VP0Sequence AnalysisPRO_0000310522Add
    BLAST
    Chaini1 – 1919Protein VP4Sequence AnalysisPRO_0000310523Add
    BLAST
    Chaini20 – 242223Protein VP2Sequence AnalysisPRO_0000310524Add
    BLAST
    Chaini243 – 487245Protein VP3Sequence AnalysisPRO_0000310525Add
    BLAST
    Chaini488 – 757270Protein VP1Sequence AnalysisPRO_0000310526Add
    BLAST
    Chaini758 – 80649Protein 2ASequence AnalysisPRO_0000310527Add
    BLAST
    Chaini807 – 1021215Protein 2BSequence AnalysisPRO_0000310528Add
    BLAST
    Chaini1022 – 1347326Protein 2CSequence AnalysisPRO_0000310529Add
    BLAST
    Chaini1348 – 141265Protein 3ASequence AnalysisPRO_0000310530Add
    BLAST
    Chaini1413 – 143321Protein 3BSequence AnalysisPRO_0000310531Add
    BLAST
    Chaini1434 – 1648215Protease 3CSequence AnalysisPRO_0000310532Add
    BLAST
    Chaini1649 – 2134486RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_0000310533Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1415 – 14151O-(5'-phospho-RNA)-tyrosineBy similarity

    Post-translational modificationi

    Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle By similarity.By similarity
    VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase By similarity.By similarity

    Keywords - PTMi

    Covalent protein-RNA linkage, Phosphoprotein

    Proteomic databases

    PRIDEiQ6WQ42.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6WQ42.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 13771377CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1393 – 2134742CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1378 – 139215Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1127 – 1289163SF3 helicasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1433 – 1627195Peptidase C3Add
    BLAST
    Domaini1880 – 2001122RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi251 – 2544Poly-Ser

    Sequence similaritiesi

    Belongs to the picornaviridae polyprotein family.Curated
    Contains 1 peptidase C3 domain.Curated
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
    Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di2.60.120.20. 3 hits.
    InterProiIPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR007053. LRAT-like_dom.
    IPR027417. P-loop_NTPase.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view]
    PfamiPF04970. LRAT. 1 hit.
    PF00548. Peptidase_C3. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00073. Rhv. 2 hits.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q6WQ42-1 [UniParc]FASTAAdd to Basket

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    MSKLFSTVGR TVDEVLSVLN DEDTESYAGP DRTAVVGGGF LTTVDQSSVS     50
    TATMGSLQDV QYRTAVDIPG SRVTQGERFF LIDQREWNST QSEWQLLGKI 100
    DIVKELLDQS YAVDGLLKYH SYARFGLDVI VQINPTSFQA GGLIAALVPY 150
    DQVDIESIVA MTTYCHGKVN CNINYVVRMK VPYIYSRGCY NLRNSAYSIW 200
    MLVIRVWSRL QLGSGTSTQI TITTLARFVD LELHGLSPLV AQMMRNEFRL 250
    SSSSNIVNLA NYDDARAKVS LALGQEEFSR DSSSTGGELV HHFSQWTSIP 300
    CLAFTFTFPG TVGPGTHIWS TTVDPFSCNL RASSTVHPTN LSSIAGMFCF 350
    WRGDIVFEFQ VFCTKYHSGR LMFVYVPGDE NTKISTLTAK QASTGLTAVF 400
    DINGVNSTLV FRCPFISDTP YRVNPTTHKS LWPYATGKLV CYVYNILNAP 450
    ASVSPSVSIN VYKSAADLEL YAPVYGVSPT NTSIFAQGKE DEGGFFSVPE 500
    VEQHVVEDKE PQGPLHVTPF GAVKAMEDPQ LARKTPGTFP ELAPGKPRHT 550
    VDHMDLYKFM GRAHYLWGHE FTKTDMQYTF QIPLSPIKEG FVTGTLRWFL 600
    SLFQLYRGSL DITMTFAGKT NVDGIVYFVP EGVAIETERE EQTPLLTLNY 650
    KTSVGAIRFN TGQTTNVQFR IPFYTPLEHI ATHSKNAMDS VLGAITTQIT 700
    NYSAQDEYLQ VTYYISFNED SQFSVPRAVP VVSSFTDTSS KTVMNTYWLD 750
    DDELVEESSH SSFDEIEEAQ CSKCKMDLGD IVICSGEKAK HFGVYVGDGV 800
    VHVDPEGNAT NWFMKRKATV KKSKNLDKWC FALSPRIDRT LICETANLMV 850
    GREVEYDIFV KNCETYARGI ASGDYGTKEG EKWKTLLSAV GVAAMTTTMM 900
    AMRHQLLDTS LTKLPQKVGE VTNEVRKILE DTSAGVREFK EKVSSILRKT 950
    WPGKTSIKIM KWTFRIVKMC VGVGLCYAHG WDSKPVTAVV TMFSMDFLDL 1000
    VIDGIEIGRM IIHELTTPKA QGLSEINQVL SIAKNAKDVI KMLIEIFCKV 1050
    IERITGEHGK KIQWAQDKKE EIMNVLERAE KWITTSDDHS EGIECLKLVR 1100
    SIQSVIRGEE SLKELAGELR AVGTHVLNKL GRLDKPNAPI LVRAEPTVLY 1150
    LYGNRGGGKS LASMAIAVKL CKELGISHVE GIYTKPIMSD FWDGYAGQPV 1200
    VIMDDLGQST SDEDWTNFCQ LVSSCPLRLN MANLEKKGTQ FNSPFIIASS 1250
    NLSHPCPKTV YCTDAIARRL HIKVKVSPKE EFSTHAMLDV AKAKKAGAYC 1300
    NLDCLDFQKI SDLASTPVSV QDIVLALLHT NVDKQTVMGN IIQYWAQSNP 1350
    REVFDTMAEG KNSGKYLWLF EKIKTSKWYI LGCVGAALSV SVLGVFAYHM 1400
    IKNHFRDQQH DQSAYSAAIK PLRVVRLEQS DAQSVVDISN VVHGNLVRVG 1450
    VGPNEARIHW LNNGWGVYNT YILMPYHGIK DADVDDDLYI ERAGTIYSTN 1500
    MKMVQVLFLE SREGDLVLIN VPRLPKFRDI RNHFSTEENI RRAEGMPGTL 1550
    CTLDHERFTL VTESDLKMVE AATYVCEDDK GVRTDISVGR SWKAKACTVA 1600
    GMCGGALVTS NNKMQNAIVG IHVAGGAPAI SRVITKEMIE EMLKTRAQCS 1650
    RIWKTEFVEK KISVGSKTKY HKSPLYDFCP QKVIKCPTKL FYQGEIDVMQ 1700
    VMLAKYSSPI VSEPLGYATV VEAYTNRMVS FFSEPRQLTY DECINGIEGL 1750
    DAIDLKTSAG FPYNTLSLKK SDLIINGKKA QRLQQDVEKM EEDLHMNRSI 1800
    QVVFTTCAKD ELRPLSKGML GKTRAIKACP VSFTILFRKY LGYALAQIQS 1850
    HPGFHTGIAV GVDPDQDWHC MWYSIVTQCD LVVGLDFSNY DASLSPFMIY 1900
    HAGRVLGQIC GLDPRLVDRI MEPIVNSVHQ LGSMRYYVDG SMPSGTPATS 1950
    VLNSIINVVN ISHVLCALEK ISVFEVFKLS KILTYGDDVL FCIKKESLDQ 2000
    KSFPLSSFVQ GLKELGMSPT GADKMEVKVT PVHKMSFLKR TFYVDEWSIC 2050
    HPRISEETVY SMLAWKSDNA SMKHVIETSI WFMFHHGPRK YVIFCTCLRG 2100
    VLCRVGIGLY IPTYKELEVR YDRLVKDRVI DDSF 2134
    Length:2,134
    Mass (Da):238,653
    Last modified:July 5, 2004 - v1
    Checksum:iC194284F02131E6B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY275539 Genomic RNA. Translation: AAN09930.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY275539 Genomic RNA. Translation: AAN09930.2 .

    3D structure databases

    ProteinModelPortali Q6WQ42.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q6WQ42.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.60.120.20. 3 hits.
    InterProi IPR000605. Helicase_SF3_ssDNA/RNA_vir.
    IPR014759. Helicase_SF3_ssRNA_vir.
    IPR007053. LRAT-like_dom.
    IPR027417. P-loop_NTPase.
    IPR000199. Peptidase_C3A/C3B_picornavir.
    IPR001676. Picornavirus_capsid.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR029053. Viral_coat.
    [Graphical view ]
    Pfami PF04970. LRAT. 1 hit.
    PF00548. Peptidase_C3. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF00073. Rhv. 2 hits.
    PF00910. RNA_helicase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
    PS51218. SF3_HELICASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Determination of the whole genome of avian encephalomyelitis virus isolate from China."
      Wei L., Liu J., Yao W.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiPOLG_AEVL2
    AccessioniPrimary (citable) accession number: Q6WQ42
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 76 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete 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