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P0C6F7

- R1A_BC133

UniProt

P0C6F7 - R1A_BC133

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Bat coronavirus 133/2005 (BtCoV) (BtCoV/133/2005)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3.1 Publication
    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
    Non-structural protein 1: binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.1 Publication

    Catalytic activityi

    TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
    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
    Sitei195 – 1962CleavageSequence Analysis
    Sitei847 – 8482Cleavage; by PL-PROSequence Analysis
    Active sitei1641 – 16411For PL-PRO activityPROSITE-ProRule annotation
    Active sitei1807 – 18071For PL-PRO activityPROSITE-ProRule annotation
    Sitei2791 – 27922Cleavage; by PL-PROSequence Analysis
    Sitei3298 – 32992Cleavage; by 3CL-PROSequence Analysis
    Active sitei3339 – 33391For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3446 – 34461For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3604 – 36052Cleavage; by 3CL-PROSequence Analysis
    Sitei3896 – 38972Cleavage; by 3CL-PROSequence Analysis
    Sitei3979 – 39802Cleavage; by 3CL-PROSequence Analysis
    Sitei4178 – 41792Cleavage; by 3CL-PROSequence Analysis
    Sitei4288 – 42892Cleavage; by 3CL-PROSequence Analysis
    Sitei4427 – 44282Cleavage; by 3CL-PROSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1721 – 175838C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4362 – 437817By similarityAdd
    BLAST
    Zinc fingeri4404 – 441714By 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 catabolism of host mRNA Source: UniProtKB-KW
    2. induction by virus of host autophagy Source: UniProtKB-KW
    3. modulation by virus of host protein ubiquitination Source: UniProtKB-KW
    4. suppression by virus of host IRF3 activity Source: UniProtKB-KW
    5. suppression by virus of host ISG15 activity Source: UniProtKB-KW
    6. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
    7. viral genome replication Source: InterPro
    8. viral protein processing Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Activation of host autophagy by virus, Decay of host mRNAs by virus, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host IRF3 by virus, Inhibition of host ISG15 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):
    Leader protein
    Non-structural protein 2
    Short name:
    nsp2
    Alternative name(s):
    p65 homolog
    Alternative name(s):
    PL2-PRO
    Papain-like proteinase
    Short name:
    PL-PRO
    Non-structural protein 4
    Short name:
    nsp4
    3C-like proteinase (EC:3.4.22.-)
    Short name:
    3CL-PRO
    Short name:
    3CLp
    Alternative name(s):
    nsp5
    Non-structural protein 6
    Short name:
    nsp6
    Non-structural protein 7
    Short name:
    nsp7
    Non-structural protein 8
    Short name:
    nsp8
    Non-structural protein 9
    Short name:
    nsp9
    Non-structural protein 10
    Short name:
    nsp10
    Alternative name(s):
    Growth factor-like peptide
    Short name:
    GFL
    Non-structural protein 11
    Short name:
    nsp11
    Gene namesi
    ORF Names:1a
    OrganismiBat coronavirus 133/2005 (BtCoV) (BtCoV/133/2005)
    Taxonomic identifieri389230 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirusunclassified Betacoronavirus
    Virus hostiTylonycteris pachypus (Lesser bamboo bat) [TaxID: 258959]
    ProteomesiUP000007449: 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 – 44414441Replicase polyprotein 1aPRO_0000338062Add
    BLAST
    Chaini1 – 195195Non-structural protein 1Sequence AnalysisPRO_0000338063Add
    BLAST
    Chaini196 – 847652Non-structural protein 2Sequence AnalysisPRO_0000338064Add
    BLAST
    Chaini848 – 27911944Non-structural protein 3Sequence AnalysisPRO_0000338065Add
    BLAST
    Chaini2792 – 3298507Non-structural protein 4Sequence AnalysisPRO_0000338066Add
    BLAST
    Chaini3299 – 36043063C-like proteinaseSequence AnalysisPRO_0000338067Add
    BLAST
    Chaini3605 – 3896292Non-structural protein 6Sequence AnalysisPRO_0000338068Add
    BLAST
    Chaini3897 – 397983Non-structural protein 7Sequence AnalysisPRO_0000338069Add
    BLAST
    Chaini3980 – 4178199Non-structural protein 8Sequence AnalysisPRO_0000338070Add
    BLAST
    Chaini4179 – 4288110Non-structural protein 9Sequence AnalysisPRO_0000338071Add
    BLAST
    Chaini4288 – 4441154Non-structural protein 11Sequence AnalysisPRO_0000338073Add
    BLAST
    Chaini4289 – 4427139Non-structural protein 10Sequence AnalysisPRO_0000338072Add
    BLAST

    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. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP0C6F7.
    SMRiP0C6F7. Positions 3896-3979, 4228-4288, 4298-4418.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2152 – 217221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2229 – 224921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2333 – 235321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2357 – 237721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2382 – 240221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2807 – 282721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3079 – 309921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3112 – 313221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3156 – 317621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3610 – 363021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3644 – 366421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3669 – 368921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3714 – 373421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3742 – 376221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3791 – 381121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3815 – 383521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1159 – 1328170MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1600 – 1871272Peptidase C16PROSITE-ProRule annotationAdd
    BLAST
    Domaini3299 – 3604306Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2119 – 2402284HD1By similarityAdd
    BLAST
    Regioni2807 – 3176370HD2By similarityAdd
    BLAST
    Regioni3610 – 3835226HD3By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi960 – 1059100Glu-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.By similarity

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1721 – 175838C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4362 – 437817By similarityAdd
    BLAST
    Zinc fingeri4404 – 441714By similarityAdd
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    InterProiIPR002589. Macro_dom.
    IPR024375. Nsp3_coronavir.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    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.
    PF11633. SUD-M. 1 hit.
    PF08715. Viral_protease. 1 hit.
    [Graphical view]
    SUPFAMiSSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 1 hit.
    SSF50494. SSF50494. 1 hit.
    PROSITEiPS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 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 Replicase polyprotein 1a (identifier: P0C6F7-1) [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

    MLSKAGVTTQ GARGKYRAEL YNEKRSDHVA CTVPLCDTED MASKLTPWFE     50
    DGETAFNQVS SILKEKGKIL FVPMHMQRAM KFLPGPRVYL VERLTGGMLS 100
    KHFLVNQLAY KDHVGAAMMR TTLNVKPLGM FFPYDSSLET GEHTFLLRKN 150
    GLGGQLFRER PWDRKETPYV EILDDLEADP TGKYSQNLLK KLIGGDCIPV 200
    DQYMCGKNGK PIADYAKIVA KEGLTTLADI EVDVKSRMDS DRFIVLNKKL 250
    YRVVWNVTRR NVPYSKQTAF TVVSVIQCDD KESVPEHTFT IGSQILMVSP 300
    LKATNNKNFN LKQRLLHTFY GKEAVQQPGY IYHSAYVDCN ACGRGTWCTG 350
    NAIQGFACDC GANYSANDVD LQSSGLVPKN ALFLANCPCA NNGACSHNAA 400
    QVYSILDGKA CVEVGGKSFT LTFGGVVYAY MGCCDGTMYF VPRAKSCVSR 450
    IGDAIFTGCT GTWDKVVETA NLFLEKAQHS LNFCQQFALT EVVLAILSGT 500
    TSTFEELRDL CHNASYEKVR DHLVNHGFVV TIGDYIRDAI NIGANGVCNA 550
    TINAPFIAFT GLGESFKKVA AIPWKICSNL KSALDYYCSN IMFRVFPYDI 600
    PCDVNDFVEL LLDCGKLTVA TSYFVLRYLD EKFDTVLGTV SNACQTALSS 650
    FLNACVAASR ATAGFISDMF KLFKVLMHKL YVYTSCGYVA VAEHSSKIVQ 700
    QVLDIMSKAM KLLHTNVSWA GTKLSAIIYE GREALLFNSG TYFCLSTKAK 750
    TLQDQMNLVL PGDYNKKTLG ILDPVPNADT IDVTANSTVV DVVHGQLEPT 800
    NEHGPSMIVG NYVLVSDKLF VRTDDEEFYP LCINGKVVST LFRLKGGMPS 850
    KKVTFGDVNT VEVTAYRSVS ITYDIHPVLD ALLSSSKLAT FTVEKDLLVE 900
    DFVDVIKDEV LTLLTPLLRG YDIDGFDVED FIDVPCYVYN QDGDCAWSSN 950
    MTFSINPVED VEEVEEFIED DYLSDELPIA DDEEAWTRAV EEVMPLDDIL 1000
    VAEIELEEDL PLETALESVE AEVGESISDE LCVVETAKAQ EPSVESTDST 1050
    PSTSTVVSEN DLSVKPMSRV AETGDVLEVE TAVVGGPVSD VTASVVTNDI 1100
    VSVEQAQQCG VSSLPIQDEA SENQVHQVPD LQCTSETKVE IVQPRQDLRP 1150
    RRLRKSKVDL SKYKHTVINN SVTLVLGDAI QIASLLPKCV LVNAANRHLK 1200
    HGGGIAGAIN KASGGDVQEE SDEYISNSGP LHVGDSVLLK GYGLADAILR 1250
    VVGPDARNNE DAALLKRCYK TFNKHTIVVT PLISSGIFSV DPKVSFEYLL 1300
    ANVTTTTYVV VNNEDIYNTL ATPSKPDGLV YSFEGWRGTV RTAKNYGFTC 1350
    FICTEYSANV KFLRTKGVDT TKKIQTVDGV SYYLYSARDA LTDVIAAANG 1400
    CPGICAMPFG YVTHGLDLAQ SGNYVRQVKV PYVCLLASKE QIPIMNSDVA 1450
    IQTPETAFIN NVTSNGGYHS WHLVSGDLIV KDVCYKKLLH WSGQTICYAD 1500
    NKFYVVKNDV ALPFSDLEAC RAYLTSRAAQ QVNIEVLVTI DGVNFRTVIL 1550
    NDATTFRKQL GATFYKGVDI SDALPTVKMG GESLFVADNL SESEEVVLKE 1600
    YYGTSDVTFL QRYYSLQPLV QQWKFVVHDG VKSLKLSNYN CYINATIMMI 1650
    DMLHDIKFVV PALQNAYLRY KGGDPYDFLA LIMAYGDCTF DNPDDEAKLL 1700
    HTLLAKAELT VSAKMVWREW CTVCGIRDIE YTGMRACVYA GVNSMEELQS 1750
    VFNETCVCGS VKHRQLVEHS TPWLLVSGLN EVKVSTSTDP VYRAFNVFQG 1800
    VETSVGHYVH VRVKDGLFYK YDSGSLTKTS DMKCKMTSVW YPKVRYTADC 1850
    NVVVYDLDGV TKVEVNPDLS NYYMKDGKYY TSKPTIKYSP ATILPGSVYS 1900
    NSCLVGVDGT PGSDTISKFF NDLLGFDETK PISKKLTYSL LPNEDGDVLL 1950
    SEFNNYNPVY KKGVMLKGKP ILWVNNGVCD SALNKPNRAS LRQLYDVAPI 2000
    VLDNKYTVLQ DNTSQLIEPN VPVVEDVSIT TRKLIEVKCK GLNKPFVKGN 2050
    FSFVNDPNGV TVVDTLGLTE LRALYVDINT RYIVLRDNNW SSLFKLHTVE 2100
    SGDLQIVANG GSVTRRARVL LGASSLFASF AKITVTATTA ACKTAGRSFC 2150
    KFVVNYGVLQ NMFLFLKMLF FLPFNYLWPK KQPTVDVGVS GLRTAGVVTT 2200
    NIVKQCGTAA YYMLLGKFKR VDWKATLRLF LLLCTTILLL SSIYHLVIFN 2250
    QVLSSDVMLE DATGILAMYK EVRSYLGIRT LCDGLAVEYR NTSFDVVDFC 2300
    SNRSVLCQWC LIGQDSLTRY SALQMLQTHI TSYVLNIDWI WFALEFFLAY 2350
    VLYTSSFNVL LLVVTAQYFF AYTSAFVNWR AYNYIVSGLF FLVTHIPLHG 2400
    LVRVYNFLAC LWFLRKFYSH VINGCKDTAC LLCYKRNRLT RVEASTIVCG 2450
    TKRTFYIAAN GGTSYCCKHN WNCVECDTAG VGNTFICTEV ANDLTTTLRR 2500
    LIKPTDQSHY YVDSVVVKDA VVELHYNRDG SSCYERYPLC YFTNLEKLKF 2550
    KEVCKTPTGI PEHNFLIYDT NDRGQENLAR SACVYYSQVL CKPMLLVDVN 2600
    LVTTVGDSRE IAIKMLDSFI NSFISLFSVS RDKLEKLINT ARDCVRRGDD 2650
    FQTVLKTFTD AARGHAGVES DVETTMVVDA LQYAHKNDIQ LTTECYNNYV 2700
    PGYIKPDSIN TLDLGCLIDL KAASVNQTSM RNANGACVWN SGDYMKLSDS 2750
    FKRQIRIACR KCNIPFRLTT SKLRAADNIL SVKFSATKIV GGAPSWLLRV 2800
    RDLTVKGYCI LTLFVFTVAV LSWFCLPSYS IATVNFNDDR ILTYKVIENG 2850
    IVRDIAPNDA CFANKYGHFS KWFNENHGGV YRNSVDCPIT IAVIAGVAGA 2900
    RVANVPATLA WVGRQIVLFV SRVFANTNVC FTPTNEIPYD TFSDSGCVLS 2950
    SECTLFRDAE GNLNPFCYDP TVLPGASSYA DMKPHVRYDM YDSDMYIKFP 3000
    EVIFESTLRI TKTLATQYCR FGSCEESAAG VCISTNGSWA LYNQNYSTRP 3050
    GIYCGDDYFD IVRRLAVSLF QPVTYFQLST SLAMGLVLCV FLTAAFYYIN 3100
    KVKRALADYT QCAVVAVVAA LLNSLCLCFI VANPLLVAPY TAMYYYATFY 3150
    LTGEPAFIMH ISWYVMFGTV VPIWMLASYT VGVMLRHLFW VLAYFSKKHV 3200
    DVFTDGKLNC SFQDAASNIF VIGKDTYVAL RNAITQDSFV RYLSLFNKYK 3250
    YYSGAMDTAS YREACAAHLC KALQTYSETG SDILYQPPNC SVTSSVLQSG 3300
    LVKMSAPSGA VENCIVQVTC GSMTLNGLWL DNTVWCPRHI MCPADQLTDP 3350
    NYDALLISKT NHSFIVQKHI GAQANLRVVA HSMVGVLLKL TVDVANPSTP 3400
    AYTFSTVKPG ASFSVLACYN GKPTGVFTVN LRHNSTIKGS FLCGSCGSVG 3450
    YTENGGVLNF VYMHQMELSN GTHTGSSFDG VMYGAFEDKQ THQLQLTDKY 3500
    CTINVVAWLY AAVLNGCKWF VKPTRVGIVT YNEWALSNQF TEFVGTQSID 3550
    MLAHRTGVSV EQMLAAIQSL HAGFQGKTIL GQSTLEDEFT PDDVNMQVMG 3600
    VVMQSGVKRI SYGFMHWLMS TLVLAYVSVM QLTKFTMWTY LFETIPTQMT 3650
    PLLFGFMACV MFTVKHKHTF LSLFLLPVAL CLTYANIVYE PQTLVSSTLI 3700
    AVANWLTPTS VYMRTTHLDF GLYISLSFVL AIIVRRLYRP SMSNLALALC 3750
    SGVMWFYTYV IGDHSSPITY LMFITTLTSD YTITVFATVN LAKFISGLVF 3800
    LYAPHLGFIL PEVKLVLLIY LCLGYMCTMY FGVFSLLNLK LRVPLGVYDY 3850
    SVSTQEFRFL TGNGLHAPRN SWEALILNFK LLGIGGTPCI KVATVQSKLT 3900
    DLKCTSVVLL TVLQQLHLES NSKAWSYCVK LHNEILAAVD PTEAFERFVC 3950
    LFATLMSFSA NVDLDALAND LFENSSVLQA TLTEFSHLAT YAELETAQSS 4000
    YQKALNSGDA SPQVLKALQK AVNVAKNAYE KDKAVARKLE RMAEQAMTSM 4050
    YKQARAEDKK AKIVSAMQTM LFGMIKKLDN DVLNGVIANA RNGCVPLSIV 4100
    PLCASNKLRV VIPDISVWNK VVNWPSVSYA GSLWDVTVIN NVDNEVVKPT 4150
    DVVETNESLT WPLVIECSRA SSSAVKLQNN EIHPKGLKTM VVTAGIDQVN 4200
    CSSSAVAYYE PVQGHRMVMG LLSENAHLKW AKVEGKDGFI NIELQPPCKF 4250
    LIAGPKGPEI RYLYFVKNLN NLHRGQLLGH IAATVRLQAG ANTEFASNST 4300
    VLTLVAFAVD PAKAYLDYVG SGGTPLSNYV KMLAPKTGTG VAISVKPEAT 4350
    ADQETYGGAS VCLYCRAHIE HPDVSGVCKY KTRFVQIPAH VRDPVGFLLK 4400
    NVPCNVCQYW VGYGCNCDAL RNNTVPQSKD TNFLNESGVL V 4441

    Note: Produced by conventional translation.

    Length:4,441
    Mass (Da):492,464
    Last modified:June 10, 2008 - v1
    Checksum:iA6E0DB4CDDA40AC7
    GO
    Isoform Replicase polyprotein 1ab (identifier: P0C6W1-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry P0C6W1.
    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:7,126
    Mass (Da):795,781
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ648794 Genomic RNA. No translation available.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ648794 Genomic RNA. No translation available.

    3D structure databases

    ProteinModelPortali P0C6F7.
    SMRi P0C6F7. Positions 3896-3979, 4228-4288, 4298-4418.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR002589. Macro_dom.
    IPR024375. Nsp3_coronavir.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    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.
    PF11633. SUD-M. 1 hit.
    PF08715. Viral_protease. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 1 hit.
    SSF50494. SSF50494. 1 hit.
    PROSITEi PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Suppression of host gene expression by nsp1 proteins of group 2 bat coronaviruses."
      Tohya Y., Narayanan K., Kamitani W., Huang C., Lokugamage K., Makino S.
      J. Virol. 83:5282-5288(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF NSP1.

    Entry informationi

    Entry nameiR1A_BC133
    AccessioniPrimary (citable) accession number: P0C6F7
    Secondary accession number(s): Q0Q4F3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 45 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

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