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P0C6V6

- R1A_PEDV7

UniProt

P0C6V6 - R1A_PEDV7

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Porcine epidemic diarrhea virus (strain CV777) (PEDV)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 By similarity.By similarity
    The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function By similarity.PROSITE-ProRule annotation
    Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter.By similarity
    Nsp9 is a ssRNA-binding protein.By similarity

    Catalytic activityi

    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei110 – 1112Cleavage; by PL1-PROBy similarity
    Sitei895 – 8962Cleavage; by PL1-PROBy similarity
    Active sitei1091 – 10911For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1239 – 12391For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1729 – 17291For PL2-PRO activityPROSITE-ProRule annotation
    Active sitei1888 – 18881For PL2-PRO activityPROSITE-ProRule annotation
    Sitei2516 – 25172Cleavage; by PL2-PROBy similarity
    Sitei2997 – 29982Cleavage; by 3CL-PROBy similarity
    Active sitei3038 – 30381For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3141 – 31411For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3299 – 33002Cleavage; by 3CL-PROBy similarity
    Sitei3579 – 35802Cleavage; by 3CL-PROBy similarity
    Sitei3662 – 36632Cleavage; by 3CL-PROBy similarity
    Sitei3857 – 38582Cleavage; by 3CL-PROBy similarity
    Sitei3965 – 39662Cleavage; by 3CL-PROBy similarity
    Sitei4100 – 41012Cleavage; by 3CL-PROBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1162 – 119332C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4039 – 405517By similarityAdd
    BLAST
    Zinc fingeri4081 – 409414By similarityAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: InterPro
    2. omega peptidase activity Source: InterPro
    3. RNA binding Source: UniProtKB-KW
    4. RNA-directed RNA polymerase activity Source: InterPro
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. induction by virus of host autophagy Source: UniProtKB-KW
    2. modulation by virus of host protein ubiquitination Source: UniProtKB-KW
    3. suppression by virus of host IRF3 activity Source: UniProtKB-KW
    4. viral genome replication Source: InterPro
    5. viral protein processing Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Activation of host autophagy by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host IRF3 by virus, Inhibition of host RLR pathway by virus, Modulation of host ubiquitin pathway by viral deubiquitinase, Modulation of host ubiquitin pathway by virus, Ubl conjugation pathway, Viral immunoevasion

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Replicase polyprotein 1a
    Short name:
    pp1a
    Alternative name(s):
    ORF1a polyprotein
    Cleaved into the following 11 chains:
    Non-structural protein 1
    Short name:
    nsp1
    Alternative name(s):
    p9
    Non-structural protein 2
    Short name:
    nsp2
    Alternative name(s):
    p87
    Alternative name(s):
    PL1-PRO/PL2-PRO
    PLP1/PLP2
    Papain-like proteinases 1/2
    p195
    Non-structural protein 4
    Short name:
    nsp4
    Alternative name(s):
    Peptide HD2
    3C-like proteinase (EC:3.4.22.-)
    Short name:
    3CL-PRO
    Short name:
    3CLp
    Alternative name(s):
    M-PRO
    nsp5
    p34
    Non-structural protein 6
    Short name:
    nsp6
    Non-structural protein 7
    Short name:
    nsp7
    Alternative name(s):
    p5
    Non-structural protein 8
    Short name:
    nsp8
    Alternative name(s):
    p23
    Non-structural protein 9
    Short name:
    nsp9
    Alternative name(s):
    p12
    Non-structural protein 10
    Short name:
    nsp10
    Alternative name(s):
    Growth factor-like peptide
    Short name:
    GFL
    p14
    Non-structural protein 11
    Short name:
    nsp11
    Gene namesi
    ORF Names:1a
    OrganismiPorcine epidemic diarrhea virus (strain CV777) (PEDV)
    Taxonomic identifieri229032 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
    Virus hostiSus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000008159: Genome

    Subcellular locationi

    Chain Non-structural protein 7 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity
    Chain Non-structural protein 8 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity
    Chain Non-structural protein 9 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity
    Chain Non-structural protein 10 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity

    GO - Cellular componenti

    1. host cell membrane Source: UniProtKB-SubCell
    2. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Host cytoplasm, Host membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 41174117Replicase polyprotein 1aPRO_0000338347Add
    BLAST
    Chaini1 – 110110Non-structural protein 1By similarityPRO_0000338348Add
    BLAST
    Chaini111 – 895785Non-structural protein 2By similarityPRO_0000338349Add
    BLAST
    Chaini896 – 25161621Non-structural protein 3By similarityPRO_0000338350Add
    BLAST
    Chaini2517 – 2997481Non-structural protein 4By similarityPRO_0000338351Add
    BLAST
    Chaini2998 – 32993023C-like proteinaseBy similarityPRO_0000338352Add
    BLAST
    Chaini3300 – 3579280Non-structural protein 6By similarityPRO_0000338353Add
    BLAST
    Chaini3580 – 366283Non-structural protein 7By similarityPRO_0000338354Add
    BLAST
    Chaini3663 – 3857195Non-structural protein 8By similarityPRO_0000338355Add
    BLAST
    Chaini3858 – 3965108Non-structural protein 9By similarityPRO_0000338356Add
    BLAST
    Chaini3966 – 4100135Non-structural protein 10By similarityPRO_0000338357Add
    BLAST
    Chaini4111 – 41177Non-structural protein 11By similarityPRO_0000338358

    Post-translational modificationi

    Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed By similarity.By similarity

    Interactioni

    Subunit structurei

    3CL-PRO exists as monomer and homodimer. The 3 peptides nsp2, nsp3 and nsp4 may form a complex. Nsp9 is a dimer. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp10 forms a dodecamer By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP0C6V6.
    SMRiP0C6V6. Positions 2998-3297, 3860-3964, 3972-4096.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1959 – 197921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2022 – 204221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2105 – 212521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2127 – 214721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2150 – 217021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2528 – 254821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2619 – 263921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2654 – 267421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2754 – 277421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2787 – 280721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2814 – 283421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2863 – 288321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3336 – 335621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3361 – 338121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3399 – 341921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3431 – 345121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3454 – 347421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3476 – 349621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3500 – 352021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1057 – 1296240Peptidase C16 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1297 – 1465169MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1691 – 1951261Peptidase C16 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2998 – 3299302Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1959 – 2170212HD1Add
    BLAST
    Regioni2528 – 2883356HD2Add
    BLAST
    Regioni3336 – 3520185HD3Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1816 – 1932117Val-richAdd
    BLAST

    Domaini

    The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane.

    Sequence similaritiesi

    Contains 1 Macro domain.PROSITE-ProRule annotation
    Contains 2 peptidase C16 domains.PROSITE-ProRule annotation
    Contains 1 peptidase C30 domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1162 – 119332C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4039 – 405517By similarityAdd
    BLAST
    Zinc fingeri4081 – 409414By similarityAdd
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    InterProiIPR002589. Macro_dom.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR011050. Pectin_lyase_fold/virulence.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view]
    PfamiPF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF08715. Viral_protease. 2 hits.
    [Graphical view]
    SMARTiSM00506. A1pp. 1 hit.
    [Graphical view]
    SUPFAMiSSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 1 hit.
    SSF50494. SSF50494. 1 hit.
    SSF51126. SSF51126. 1 hit.
    PROSITEiPS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 2 hits.
    [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 Replicase polyprotein 1a (identifier: P0C6V6-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1a, ORF1a polyprotein

    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

    MASNHVTLAF ANDAEISAFG FCTASEAVSY YSEAAASGFM QCRFVSLDLA     50
    DTVEGLLPED YVMVVIGTTK LSAYVDTFGS RPRNICGWLL FSNCNYFLEE 100
    LELTFGRRGG NIVPVDQYMC GADGKPVLQE SEWEYTDFFA DSEDGQLNIA 150
    GITYVKAWIV ERSDVSYASQ NLTSIKSITY CSTYEHTFLD GTAMKVARTP 200
    KIKKNVVLSE PLATIYREIG SPFVDNGSDA RSIIRRPVFL HAFVKCKCGS 250
    YHWTVGDWTS YVSTCCGFKC KPVLVASCSA MPGSVVVTRA GAGTGVKYYN 300
    NMFLRHVADI DGLAFWRILK VQSKDDLACS GKFLEHHEEG FTDPCYFLND 350
    SSLATKLKFD ILSGKFSDEV KQAIIAGHVV VGSALVDIVD DALGQPWFIR 400
    KLGDLASAPW EQLKAVVRGL GLLSDEVVLF GKRLSCATLS IVNGVFEFLA 450
    DVPEKLAAAV TVFVNFLNEF FESACDCLKV GGKTFNKVGS YVLFDNALVK 500
    LVKAKARGPR QAGICEVRYT SLVVGSTTKV VSKRVENANV NLVVVDEDVT 550
    LNTTGRTVVV DGLAFFESDG FYRHLADADV VIEHPVYKSA CELKPVFECD 600
    PIPDFPLPVA ASVAELCVQT DLLLKNYNTP YKTYSCVVRG DKCCITCTLQ 650
    FKAPSYVEDA VNFVDLCTKN IGTAGFHEFY ITAHEQQDLQ GFLTTCCTMS 700
    GFECFMPTIP QCPAVLEEID GGSIWRSFIT GLNTMWDFCK RLKVSFGLDG 750
    IVVTVARKFK RLGALLAEMY NTYLSTVVEN LVLAGVSFKY YATSVPKIVL 800
    GGCFHSVKSV FASVFQIPVQ AGIEKFKVFL NCVHPVVPRV IETSFVELEE 850
    TTFKPPALNG GIAIVDGFAF YYDGTLYYPT DGNSVVPICF KKKGGGDVKF 900
    SDEVSVKTID PVYKVSLEFE FESETIMAVL NKAVGNRIKV TGGWDDVVEY 950
    INVAIEVLKD HVEVPKYYIY DEEGGTDPNL PVMVSQWPLN DDTISQDLLD 1000
    VEVVTDAPID SEGDEVDSSA PEKVADVANS EPGDDGLPVA PETNVESEVE 1050
    EVAATLSFIK DTPSTVTKDP FAFDFVSYGG LKVLRQSHNN CWVTSTLVQL 1100
    QLLGIVDDPA MELFSAGRVG PMVRKCYESQ KAILGSLGDV SACLESLTKD 1150
    LHTLKITCSV VCGCGTGERI YEGCAFRMTP TLEPFPYGAC AQCAQVLMHT 1200
    FKSIVGTGIF CRDTTALSLD SLVVKPLCAA AFIGKDSGHY VTNFYDAAMA 1250
    IDGYGRHQIK YDTLNTICVK DVNWTAPLVP AVDSVVEPVV KPFYSYKNVD 1300
    FYQGDFSDLV KLPCDFVVNA ANEKLSHGGG IAKAIDVYTK GMLQKCSNDY 1350
    IKAHGPIKVG RGVMLEALGL KVFNVVGPRK GKHAPELLVK AYKSVFANSG 1400
    VALTPLISVG IFSVPLEESL SAFLACVGDR HCKCFCYGDK EREAIIKYMD 1450
    GLVDAIFKEA LVDTTPVQED VQQVSQKPVL PNFEPFRIEG AHAFYECNPE 1500
    GLMSLGADKL VLFTNSNLDF CSVGKCLNDV TSGALLEAIN VFKKSNKTVP 1550
    AGNCVTLDCA NMISITMVVL PFDGDANYDK NYARAVVKVS KLKGKLVLAV 1600
    DDATLYSKLS HLSVLGFVST PDDVERFYAN KSVVIKVTED TRSVKAVKVE 1650
    STATYGQQIG PCLVNDTVVT DNKPVVADVV AKVVPNANWD SHYGFDKAGE 1700
    FHMLDHTGFT FPSEVVNGRR VIKTTDNNCW VNVTCLQLQF ARFRFKSAGL 1750
    QAMWESYCTG DVAMFVHWLY WLTGVDKGQP SDSENALNML SKYIVPAGSV 1800
    TIERVTHDGC CCSKRVVTAP VVNASVLKLG VEDGLCPHGL NYIGKVVVVK 1850
    GTTIVVNVGK PVVAPSHLFL KGVSYTTFLD NGNGVVGHYT VFDHGTGMVH 1900
    DGDAFVPGDL NVSPVTNVVV SEQTAVVIKD PVKKAELDAT KLLDTMNYAS 1950
    ERFFSFGDFM SRNLITVFLY ILSILGLCFR AFRKRDVKVL AGVPQRTGII 2000
    LRKSMRYNAK ALGVFFKLKL YWFKVLGKFS LGIYALYALL FMTIRFTPIG 2050
    SPVCDDVVAG YANSSFDKNE YCNSVICKVC LYGYQELSDF SHTQVVWQHL 2100
    RDPLIGNVMP FFYLAFLAIF GGVYVKAITL YFIFQYLNSL GVFLGLQQSI 2150
    WFLQLVPFDV FGDEIVVFFI VTRVLMFIKH VCLGCDKASC VACSKSARLK 2200
    RVPVQTIFQG TSKSFYVHAN GGSKFCKKHN FFCLNCDSYG PGCTFINDVI 2250
    ATEVGNVVKL NVQPTGPATI LIDKVEFSNG FYYLYSGDTF WKYNFDITDS 2300
    KYTCKEALKN CSIITDFIVF NNNGSNVNQV KNACVYFSQM LCKPVKLVDS 2350
    ALLASLSVDF GASLHSAFVS VLSNSFGKDL SSCNDMQDCK STLGFDDVPL 2400
    DTFNAAVAEA HRYDVLLTDM SFNNFTTSYA KPEEKFPVHD IATCMRVGAK 2450
    IVNHNVLVKD SIPVVWLVRD FIALSEETRK YIIRTTKVKG ITFMLTFNDC 2500
    RMHTTIPTVC IANKKGAGLP SFSKVKKFFW FLCLFIVAAF FALSFLDFST 2550
    QVSSDSDYDF KYIESGQLKT FDNPLSCVHN VFINFDQWHD AKFGFTPVNN 2600
    PSCPIVVGVS DEARTVPGIP AGVYLAGKTL VFAINTIFGT SGLCFDASGV 2650
    ADKGACIFNS ACTTLSGLGG TAVYCYKNGL VEGAKLYSEL APHSYYKMVD 2700
    GNAVSLPEII SRGFGIRTIR TKAMTYCRVG QCVQSAEGVC FGADRFFVYN 2750
    AESGSDFVCG TGLFTLLMNV ISVFSKTVPV TVLSGQILFN CIIAFVAVAV 2800
    CFLFTKFKRM FGDMSVGVFT VGACTLLNNV SYIVTQNTLG MLGYATLYFL 2850
    CTKGVRYMWI WHLGFLISYI LIAPWWVLMV YAFSAIFEFM PNLFKLKVST 2900
    QLFEGDKFVG SFENAAAGTF VLDMHAYERL ANSISTEKLR QYASTYNKYK 2950
    YYSGSASEAD YRLACFAHLA KAMMDYASNH NDTLYTPPTV SYNSTLQAGL 3000
    RKMAQPSGVV EKCIVRVCYG NMALNGLWLG DIVMCPRHVI ASSTTSTIDY 3050
    DYALSVLRLH NFSISSGNVF LGVVSATMRG ALLQIKVNQN NVHTPKYTYR 3100
    TVRPGESFNI LACYDGAAAG VYGVNMRSNY TIRGSFINGA CGSPGYNINN 3150
    GTVEFCYLHQ LELGSGCHVG SDLDGVMYGG YEDQPTLQVE GASSLFTENV 3200
    LAFLYAALIN GSTWWLSSSR IAVDRFNEWA VHNGMTTVGN TDCFSILAAK 3250
    TGVDVQRLLA SIQSLHKNFG GKQILGHTSL TDEFTTGEVV RQMYGVNLQG 3300
    GYVSRACRNV LLVGSFLTFF WSELVSYTKF FWVNPGYVTP MFACLSLLSS 3350
    LLMFTLKHKT LFFQVFLIPA LIVTSCINLA FDVEVYNYLA EHFDYHVSLM 3400
    GFNAQGLVNI FVCFVVTILH GTYTWRFFNT PASSVTYVVA LLTAAYNYFY 3450
    ASDILSCAMT LFASVTGNWF VGAVCYKVAV YMALRFPTFV AIFGDIKSVM 3500
    FCYLVLGYFT CCFYGILYWF NRFFKVSVGV YDYTVSAAEF KYMVANGLRA 3550
    PTGTLDSLLL SAKLIGIGGE RNIKISSVQS KLTDIKCSNV VLLGCLSSMN 3600
    VSANSTEWAY CVDLHNKINL CNDPEKAQEM LLALLAFFLS KNSAFGLDDL 3650
    LESYFNDNSM LQSVASTYVG LPSYVIYENA RQQYEDAVNN GSPPQLVKQL 3700
    RHAMNVAKSE FDREASTQRK LDRMAEQAAA QMYKEARAVN RKSKVVSAMH 3750
    SLLFGMLRRL DMSSVDTILN LAKDGVVPLS VIPAVSATKL NIVTSDIDSY 3800
    NRIQREGCVH YAGTIWNIID IKDNDGKVVH VKEVTAQNAE SLSWPLVLGC 3850
    ERIVKLQNNE IIPGKLKQRS IKAEGDGIVG EGKALYNNEG GRTFMYAFIS 3900
    DKPDLRVVKW EFDGGCNTIE LEPPRKFLVD SPNGAQIKYL YFVRNLNTLR 3950
    RGAVLGYIGA TVRLQAGKQT EQAINSSLLT LCAFAVDPAK TYIDAVKSGH 4000
    KPVGNCVKML ANGSGNGQAV TNGVEASTNQ DSYGGASVCL YCRAHVEHPS 4050
    MDGFCRLKGK YVQVPLGTVD PIRFVLENDV CKVCGCWLSN GCTCDRSIMQ 4100
    STDMAYLNEY GALVQLD 4117

    Note: Produced by conventional translation.

    Length:4,117
    Mass (Da):452,818
    Last modified:June 10, 2008 - v1
    Checksum:i4409589DAF0AA869
    GO
    Isoform Replicase polyprotein 1ab (identifier: P0C6Y4-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry P0C6Y4.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by -1 ribosomal frameshifting at the 1a-1b genes boundary.

    Length:6,781
    Mass (Da):753,158
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF353511 Genomic RNA. No translation available.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF353511 Genomic RNA. No translation available.

    3D structure databases

    ProteinModelPortali P0C6V6.
    SMRi P0C6V6. Positions 2998-3297, 3860-3964, 3972-4096.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR002589. Macro_dom.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR011050. Pectin_lyase_fold/virulence.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view ]
    Pfami PF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF08715. Viral_protease. 2 hits.
    [Graphical view ]
    SMARTi SM00506. A1pp. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 1 hit.
    SSF50494. SSF50494. 1 hit.
    SSF51126. SSF51126. 1 hit.
    PROSITEi PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 2 hits.
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    Publicationsi

    1. "Further analysis of the genome of porcine epidemic diarrhea virus."
      Bridgen A., Kocherhans R., Tobler K., Carvajal A., Ackermann M.
      Adv. Exp. Med. Biol. 440:781-786(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Completion of the porcine epidemic diarrhoea coronavirus (PEDV) genome sequence."
      Kocherhans R., Bridgen A., Ackermann M., Tobler K.
      Virus Genes 23:137-144(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiR1A_PEDV7
    AccessioniPrimary (citable) accession number: P0C6V6
    Secondary accession number(s): Q91AV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 42 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