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P0C6T6

- R1A_BCHK9

UniProt

P0C6T6 - R1A_BCHK9

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Bat coronavirus HKU9 (BtCoV) (BtCoV/HKU9)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (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 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
    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
    Sitei175 – 1762CleavageSequence Analysis
    Sitei772 – 7732Cleavage; by PL-PROSequence Analysis
    Active sitei1533 – 15331For PL-PRO activityPROSITE-ProRule annotation
    Active sitei1694 – 16941For PL-PRO activityPROSITE-ProRule annotation
    Sitei2609 – 26102Cleavage; by PL-PROSequence Analysis
    Sitei3103 – 31042Cleavage; by 3CL-PROSequence Analysis
    Active sitei3144 – 31441For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3248 – 32481For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3409 – 34102Cleavage; by 3CL-PROSequence Analysis
    Sitei3699 – 37002Cleavage; by 3CL-PROSequence Analysis
    Sitei3782 – 37832Cleavage; by 3CL-PROSequence Analysis
    Sitei3982 – 39832Cleavage; by 3CL-PROSequence Analysis
    Sitei4094 – 40952Cleavage; by 3CL-PROSequence Analysis
    Sitei4233 – 42342Cleavage; by 3CL-PROSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1610 – 164738C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4168 – 418417By similarityAdd
    BLAST
    Zinc fingeri4211 – 422414By 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 HKU9 (BtCoV) (BtCoV/HKU9)
    Taxonomic identifieri694006 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
    Virus hostiRousettus leschenaultii (Leschenault's rousette) [TaxID: 9408]
    ProteomesiUP000006576: 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 – 42484248Replicase polyprotein 1aPRO_0000338110Add
    BLAST
    Chaini1 – 175175Non-structural protein 1Sequence AnalysisPRO_0000338111Add
    BLAST
    Chaini176 – 772597Non-structural protein 2Sequence AnalysisPRO_0000338112Add
    BLAST
    Chaini773 – 26091837Non-structural protein 3Sequence AnalysisPRO_0000338113Add
    BLAST
    Chaini2610 – 3103494Non-structural protein 4Sequence AnalysisPRO_0000338114Add
    BLAST
    Chaini3104 – 34093063C-like proteinaseSequence AnalysisPRO_0000338115Add
    BLAST
    Chaini3410 – 3699290Non-structural protein 6Sequence AnalysisPRO_0000338116Add
    BLAST
    Chaini3700 – 378283Non-structural protein 7Sequence AnalysisPRO_0000338117Add
    BLAST
    Chaini3783 – 3982200Non-structural protein 8Sequence AnalysisPRO_0000338118Add
    BLAST
    Chaini3983 – 4094112Non-structural protein 9Sequence AnalysisPRO_0000338119Add
    BLAST
    Chaini4094 – 4248155Non-structural protein 11Sequence AnalysisPRO_0000338121Add
    BLAST
    Chaini4095 – 4233139Non-structural protein 10Sequence AnalysisPRO_0000338120Add
    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

    ProteinModelPortaliP0C6T6.
    SMRiP0C6T6. Positions 934-1096, 3106-3403, 3699-3782, 3820-3972, 3985-4094, 4104-4224.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2040 – 206021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2081 – 210121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2162 – 218221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2183 – 220321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2218 – 223821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2621 – 264121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2719 – 273921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2865 – 288521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2887 – 290721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2916 – 293621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2946 – 296621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2970 – 299021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3423 – 344321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3449 – 346921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3474 – 349421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3517 – 353721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3569 – 358921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3592 – 361221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3620 – 364021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini930 – 1097168MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1492 – 1757266Peptidase C16PROSITE-ProRule annotationAdd
    BLAST
    Domaini3104 – 3409306Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2015 – 2238224HD1By similarityAdd
    BLAST
    Regioni2621 – 2990370HD2By similarityAdd
    BLAST
    Regioni3423 – 3640218HD3By similarityAdd
    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 fingeri1610 – 164738C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4168 – 418417By similarityAdd
    BLAST
    Zinc fingeri4211 – 422414By 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: P0C6T6-1) [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

    MEGVPDPPKL KSMVVTTLKW CDPFANPNVT GWDIPIEEAL EYAKQQLRTP     50
    EPQLVFVPYY LSHAPGISGD RVVITDSIWY ATNFGWQPIR ELAMDKDGVR 100
    YGRGGTHGVL LPMQDPSFIM GDIDIQIRKY GIGANSPPDV LPLWDGFSDP 150
    GPDVGPYLDF PDNCCPTKPK AKRGGDVYLS DQYGFDNNGI LVEPVMKLLG 200
    VIKSDFTLEQ LLAALGKYRT EDGYDLPDGY VKVAIKVGRK AVPVLKQSIF 250
    TVVGVTEQLV PGYYYPFSTS SVVEHTKPTR GGPVGKTVEA VMLSLYGTNN 300
    YNPATPVARL KCSYCDYYGW TPLKDIGTVN CLCGAEFQLT SSCVDAESAG 350
    VIKPGCVMLL DKSPGMRLIP GNRTYVSFGG AIWSPIGKVN GVTVWVPRAY 400
    SIVAGEHSGA VGSGDTVAIN KELVEYLIEG IRVDADTLDN PTCATFIANL 450
    DCDTKAPVVH TVESLQGLCL ANKIMLGDKP LPTDEFHPFI VGLAYHVQRA 500
    CWYGALASRT FEAFRDFVRT EEERFAQFFG KVCAPINGCV YLAYTTGRVT 550
    LFSAYQVLNT AIAKSKDAFG GVAAIVVDML KPILEWVLKK MSIAKGAWLP 600
    YAEGLLALFK AQFTVVKGKF QFLRASLNSK CHSLCDLLTT IMSKLLTSVK 650
    WAGCKVDALY TGTYYYFSRK GVLTEVQLCA KRLGLLLTPK QQKMEVEVLD 700
    GDFDAPVTLT DLELEECTGV LEEVFGASDV KLVKGTLVSL ASKLFVRTED 750
    GFLYRYVKSG GVLGKAFRLR GGGVSKVTFG DEEVHTIPNT VTVNFSYDVC 800
    EGLDAILDKV MAPFQVEEGT KLEDLACVVQ KAVYERLSDL FSDCPAELRP 850
    INLEDFLTSE CFVYSKDYEK ILMPEMYFSL EDAVPVDDEM VDDIEDTVEQ 900
    ASDSDDQWLG DEGAEDCDNT IQDVDVATSM TTPCGYTKIA EHVYIKCADI 950
    VQEARNYSYA VLVNAANVNL HHGGGVAGAL NRATNNAMQK ESSEYIKANG 1000
    SLQPGGHVLL SSHGLASHGI LHVVGPDKRL GQDLALLDAV YAAYTGFDSV 1050
    LTPLVSAGIF GFTVEESLCS LVKNVACTTY VVVYDRQLYE RALATSFDVP 1100
    GPQSSVQHVP AIDWAEAVEV QESIVDQVET PSLGAVDTVD SNADSGLNET 1150
    ARSPENVVGS VPDDVVADVE SCVRDLVRQV VKKVKRDKRP PPIVPQQTVE 1200
    QQPQEISSPG DCNTVLVDVV SMSFSAMVNF GKEKGLLIPV VIDYPAFLKV 1250
    LKRFSPKEGL FSSNGYEFYG YSRDKPLHEV SKDLNSLGRP LIMIPFGFIV 1300
    NGQTLAVSAV SMRGLTVPHT VVVPSESSVP LYRAYFNGVF SGDTTAVQDF 1350
    VVDILLNGAR DWDVLQTTCT VDRKVYKTIC KRGNTYLCFD DTNLYAITGD 1400
    VVLKFATVSK ARAYLETKLC APEPLIKVLT TVDGINYSTV LVSTAQSYRA 1450
    QIGTVFCDGH DWSNKNPMPT DEGTHLYKQD NFSSAEVTAI REYYGVDDSN 1500
    IIARAMSIRK TVQTWPYTVV DGRVLLAQRD SNCYLNVAIS LLQDIDVSFS 1550
    TPWVCRAYDA LKGGNPLPMA EVLIALGKAT PGVSDDAHMV LSAVLNHGTV 1600
    TARRVMQTVC EHCGVSQMVF TGTDACTFYG SVVLDDLYAP VSVVCQCGRP 1650
    AIRYVSEQKS PWLLMSCTPT QVPLDTSGIW KTAIVFRGPV TAGHYMYAVN 1700
    GTLISVYDAN TRRRTSDLKL PATDILYGPT SFTSDSKVET YYLDGVKRTT 1750
    IDPDFSKYVK RGDYYFTTAP IEVVAAPKLV TSYDGFYLSS CQNPQLAESF 1800
    NKAINATKTG PMKLLTMYPN VAGDVVAISD DNVVAHPYGS LHMGKPVLFV 1850
    TRPNTWKKLV PLLSTVVVNT PNTYDVLAVD PLPVNNETSE EPISVKAPIP 1900
    LYGLKATMVL NGTTYVPGNK GHLLCLKEFT LTDLQTFYVE GVQPFVLLKA 1950
    SHLSKVLGLR VSDSSLHVNH LSKGVVYAYA ATRLTTRVTT SLLGGLVTRS 2000
    VRKTADFVRS TNPGSKCVGL LCLFYQLFMR FWLLVKKPPI VKVSGIIAYN 2050
    TGCGVTTCVL NYLRSRCGNI SWSRLLKLLR YMLYIWFVWT CLTICGVWLS 2100
    EPYAPSLVTR FKYFLGIVMP CDYVLVNETG TGWLHHLCMA GMDSLDYPAL 2150
    RMQQHRYGSP YNYTYILMLL EAFFAYLLYT PALPIVGILA VLHLIVLYLP 2200
    IPLGNSWLVV FLYYIIRLVP FTSMLRMYIV IAFLWLCYKG FLHVRYGCNN 2250
    VACLMCYKKN VAKRIECSTV VNGVKRMFYV NANGGTHFCT KHNWNCVSCD 2300
    TYTVDSTFIC RQVALDLSAQ FKRPIIHTDE AYYEVTSVEV RNGYVYCYFE 2350
    SDGQRSYERF PMDAFTNVSK LHYSELKGAA PAFNVLVFDA TNRIEENAVK 2400
    TAAIYYAQLA CKPILLVDKR MVGVVGDDAT IARAMFEAYA QNYLLKYSIA 2450
    MDKVKHLYST ALQQISSGMT VESVLKVFVG STRAEAKDLE SDVDTNDLVS 2500
    CIRLCHQEGW EWTTDSWNNL VPTYIKQDTL STLEVGQFMT ANAKYVNANI 2550
    AKGAAVNLIW RYADFIKLSE SMRRQLKVAA RKTGLNLLVT TSSLKADVPC 2600
    MVTPFKIIGG HRRIVSWRRV LIHVFMLLVV LNPQWFTPWY IMRPIEYNVV 2650
    DFKVIDNAVI RDITSADQCF ANKFSAFENW YSNRYGSYVN SRGCPMVVGV 2700
    VSDIVGSLVP GLPARFLRVG TTLLPLVNYG LGAVGSVCYT PHYAINYDVF 2750
    DTSACVLAAT CTLFSSASGE RMPYCADAAL IQNASRYDML KPHVMYPFYE 2800
    HSGYIRFPEV ISAGVHIVRT MAMEYCKVGR CDVSEAGLCM SLQPRWVVNN 2850
    AYFRQQSGVY CGTSAFDLFM NMLLPIFTPV GAVDITTSIL MGALLAVVVS 2900
    MSLYYLLRFR RAFGDYSGVI FTNILAFVLN VIVLCLEGPY PMLPSIYAMV 2950
    FLYATCYFGS DIACMMHVSF LIMFAGVVPL WVTVLYIVVV LSRHILWFAS 3000
    LCTKRTVQVG DLAFHSFQDA ALQTFMLDKE VFLRLKREIS SDAYFKYLAM 3050
    YNKYKYYSGP MDTAAYREAA CSHLVMALEK YSNGGGDTIY QPPRCSVASA 3100
    ALQAGLTRMA HPSGLVEPCL VKVNYGSMTL NGIWLDNFVI CPRHVMCSRD 3150
    ELANPDYPRL SMRAANYDFH VSQNGHNIRV IGHTMEGSLL KLTVDVNNPK 3200
    TPAYSFIRVS TGQAMSLLAC YDGLPTGVYT CTLRSNGTMR ASFLCGSCGS 3250
    PGFVMNGKEV QFCYLHQLEL PNGTHTGTDF SGVFYGPFED KQVPQLAAPD 3300
    CTITVNVLAW LYAAVLSGEN WFLTKSSISP AEFNNCAVKY MCQSVTSESL 3350
    QVLQPLAAKT GISVERMLSA LKVLLSAGFC GRTIMGSCSL EDEHTPYDIG 3400
    RQMLGVKLQG KFQSMFRWTL QWFAIIFVLT ILILLQLAQW TFVGALPFTL 3450
    LLPLIGFVAV CVGFVSLLIK HKHTYLTVYL LPVAMVTAYY NFQYTPEGVQ 3500
    GYLLSLYNYV NPGRIDVIGT DLLTMLIISV ACTLLSVRMV RTDAYSRIWY 3550
    VCTAVGWLYN CWTGSADTVA ISYLTFMVSV FTNYTGVACA SLYAAQFMVW 3600
    VLKFLDPTIL LLYGRFRCVL VCYLLVGYLC TCYFGVFNLI NRLFRCTLGN 3650
    YEYVVSSQEL RYMNSHGLLP PTNSWQALML NIKLAGIGGI PIYRVSTIQS 3700
    NMTDLKCTSV VLLSVLQQLR VESSSKLWAL CVKLHNEILA SNSPTEAFEA 3750
    FVSLLSVLLS LPGAINLDEL CSSILENNSV LQAVASEFSN LSSYVDYENA 3800
    QKAYDTAVAT GAPASTVNAL KKAMNVAKSV LDKDVATTRK LERMSELAMT 3850
    AMYKQARAED RRSKVTAAMQ TMLFNMIRRL DSDALSNILN NARNGVVPLG 3900
    VIPRTAANKL LLVVPDFSVY TATITMPTLT YAGSAWDVMQ VADADGKTVN 3950
    ATDITRENSV NLAWPLVVTA QRQQATSPVK LQNNELMPQT VKRMNVVAGV 4000
    SQTACVTDAV AYYNATKEGR HVMAILADTD GLAFAKVEKS TGDGFVILEL 4050
    EPPCKFMVDT PKGPALKYLY FTKGLKNLCR GTVLGTLACT VRLHAGSATE 4100
    VASNSSILSL CSFSVDPEAT YKDYLDNGGS PIGNCVKMLT PHTGTGLAIT 4150
    AKPDANIDQE SFGGASCCLY CRCHIEHPGA SGVCKYKGKF VQIPLVGVND 4200
    PIGFCIRNVV CAVCNMWQGY GCPCSSLREI NLQARDECFL NESGVLVE 4248

    Note: Produced by conventional translation.

    Length:4,248
    Mass (Da):468,590
    Last modified:June 10, 2008 - v1
    Checksum:iC0D0584A862070A7
    GO
    Isoform Replicase polyprotein 1ab (identifier: P0C6W5-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry P0C6W5.
    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:6,930
    Mass (Da):769,729
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF065513 Genomic RNA. No translation available.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF065513 Genomic RNA. No translation available.

    3D structure databases

    ProteinModelPortali P0C6T6.
    SMRi P0C6T6. Positions 934-1096, 3106-3403, 3699-3782, 3820-3972, 3985-4094, 4104-4224.
    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. "Comparative analysis of twelve genomes of three novel group 2c and group 2d coronaviruses reveals unique group and subgroup features."
      Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R., Wong B.H.L., Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F., Chan K.-H., Zheng B.-J., Yuen K.-Y.
      J. Virol. 81:1574-1585(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate HKU9-1.
    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_BCHK9
    AccessioniPrimary (citable) accession number: P0C6T6
    Secondary accession number(s): A3EXG5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 47 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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