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P0C6V1

- R1A_CVMJH

UniProt

P0C6V1 - R1A_CVMJH

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Murine coronavirus (strain JHM) (MHV-JHM) (Murine hepatitis virus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 50 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) 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. 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 By similarity.By similarity

    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
    Sitei247 – 2482Cleavage; by PL1-PROCurated
    Sitei832 – 8332Cleavage; by PL1-PROCurated
    Active sitei1120 – 11201For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1271 – 12711For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1715 – 17151For PL2-PRO activityPROSITE-ProRule annotation
    Active sitei1872 – 18721For PL2-PRO activityPROSITE-ProRule annotation
    Sitei2840 – 28412Cleavage; by PL2-PROCurated
    Sitei3336 – 33372Cleavage; by 3CL-PROCurated
    Active sitei3377 – 33771For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3481 – 34811For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3639 – 36402Cleavage; by 3CL-PROCurated
    Sitei3927 – 39282Cleavage; by 3CL-PROCurated
    Sitei4019 – 40202Cleavage; by 3CL-PROCurated
    Sitei4213 – 42142Cleavage; by 3CL-PROCurated
    Sitei4323 – 43242Cleavage; by 3CL-PROCurated
    Sitei4460 – 44612Cleavage; by 3CL-PROCurated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1197 – 122529C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1793 – 182937C4-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4397 – 441317By similarityAdd
    BLAST
    Zinc fingeri4439 – 445214By 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):
    p28
    Non-structural protein 2
    Short name:
    nsp2
    Alternative name(s):
    p65
    Alternative name(s):
    PL1-PRO/PL2-PRO
    PL1/PL2
    Papain-like proteinases 1/2
    p210
    Non-structural protein 4
    Short name:
    nsp4
    Alternative name(s):
    Peptide HD2
    p44
    3C-like proteinase (EC:3.4.22.-)
    Short name:
    3CL-PRO
    Short name:
    3CLp
    Alternative name(s):
    M-PRO
    nsp5
    p27
    Non-structural protein 6
    Short name:
    nsp6
    Non-structural protein 7
    Short name:
    nsp7
    Alternative name(s):
    p10
    Non-structural protein 8
    Short name:
    nsp8
    Alternative name(s):
    p22
    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
    p15
    Non-structural protein 11
    Short name:
    nsp11
    Gene namesi
    ORF Names:1a
    OrganismiMurine coronavirus (strain JHM) (MHV-JHM) (Murine hepatitis virus)
    Taxonomic identifieri11144 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000007193: 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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2835 – 28351F → A: No processing between p210 and peptide HD2. 1 Publication
    Mutagenesisi2836 – 28361S → A: No effect. 1 Publication
    Mutagenesisi2837 – 28371L → A: No effect. 1 Publication
    Mutagenesisi2838 – 28381K → A: No effect. 1 Publication
    Mutagenesisi2838 – 28381K → N: No effect. 1 Publication
    Mutagenesisi2839 – 28391G → A: Partial processing between p210 and peptide HD2. 1 Publication
    Mutagenesisi2839 – 28391G → N: No processing between p210 and peptide HD2. 1 Publication
    Mutagenesisi2839 – 28391G → V: No processing between p210 and peptide HD2. 1 Publication
    Mutagenesisi2840 – 28401G → A: No processing between p210 and peptide HD2. 1 Publication
    Mutagenesisi2840 – 28401G → N: No processing between p210 and peptide HD2. 1 Publication
    Mutagenesisi2840 – 28401G → V: No processing between p210 and peptide HD2. 1 Publication
    Mutagenesisi2841 – 28411A → N: No effect. 1 Publication
    Mutagenesisi2842 – 28421V → N or M: No effect. 1 Publication
    Mutagenesisi2846 – 28461V → M: No effect. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 44744474Replicase polyprotein 1aPRO_0000338290Add
    BLAST
    Chaini1 – 247247Non-structural protein 1CuratedPRO_0000338291Add
    BLAST
    Chaini248 – 832585Non-structural protein 2CuratedPRO_0000338292Add
    BLAST
    Chaini833 – 28402008Non-structural protein 3CuratedPRO_0000338293Add
    BLAST
    Chaini2841 – 3336496Non-structural protein 4CuratedPRO_0000338294Add
    BLAST
    Chaini3337 – 36393033C-like proteinaseCuratedPRO_0000338295Add
    BLAST
    Chaini3640 – 3927288Non-structural protein 6CuratedPRO_0000338296Add
    BLAST
    Chaini3928 – 401992Non-structural protein 7CuratedPRO_0000338297Add
    BLAST
    Chaini4020 – 4213194Non-structural protein 8PRO_0000338298Add
    BLAST
    Chaini4214 – 4323110Non-structural protein 9CuratedPRO_0000338299Add
    BLAST
    Chaini4323 – 4474152Non-structural protein 11Sequence AnalysisPRO_0000338301Add
    BLAST
    Chaini4324 – 4460137Non-structural protein 10CuratedPRO_0000338300Add
    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

    ProteinModelPortaliP0C6V1.
    SMRiP0C6V1. Positions 4055-4205, 4329-4453.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2289 – 230921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2320 – 234021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2403 – 242321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2445 – 246521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2846 – 286621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3099 – 311921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3121 – 314121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3153 – 317321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3180 – 320021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3205 – 322521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3648 – 366821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3678 – 369821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3705 – 372521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3748 – 376821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3775 – 379521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3802 – 382221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3846 – 386621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1083 – 1320238Peptidase C16 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1321 – 1481161MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1677 – 1936260Peptidase C16 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini3337 – 3639303Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2228 – 2465238HD1Add
    BLAST
    Regioni2846 – 3225380HD2Add
    BLAST
    Regioni3648 – 3866219HD3Add
    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 fingeri1197 – 122529C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1793 – 182937C4-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4397 – 441317By similarityAdd
    BLAST
    Zinc fingeri4439 – 445214By similarityAdd
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    InterProiIPR022570. Coronavirus_NSP1.
    IPR002589. Macro_dom.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR002705. Pept_C30/C16_B_coronavir.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view]
    PfamiPF11963. DUF3477. 2 hits.
    PF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF01831. Peptidase_C16. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF08715. Viral_protease. 1 hit.
    [Graphical view]
    SMARTiSM00506. A1pp. 1 hit.
    [Graphical view]
    SUPFAMiSSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 1 hit.
    SSF50494. SSF50494. 1 hit.
    SSF53335. SSF53335. 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: P0C6V1-1) [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.

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    MAKMGKYGLG FKWAPEFPWM LPNASEKLGN PERSEEDGFC PSAAQEPKVK     50
    GKTLVNHVRV DCSRLPALEC CVQSAIIRDI FVDEDPQKVE ASTMMALQFG 100
    SAVLVKPSKR LSVQAWAKLG VLPKTPAMGL FKRFCLCNTR ECVCDAHVAF 150
    QLFTVQPDGV CLGNGRFIGW FVPVTAIPEY AKQWLQPWSI LLRKGGNKGS 200
    VTSGHFRRAV TMPVYDFNVE DACEEVHLNP RGKYSCKAYA LLRGYRGVKP 250
    ILFVDQYGCD YTGCLAKGLE DYGDLTLSEM KELSPVWRDS LDNEVVVAWH 300
    VDRDPRAVMR LQTLATVRSI EYVGQPIEDM VDGDVVMREP AHLLAPNAIV 350
    KRLPRLVETM LYTDSSVTEF CYKTKLCDCG FITQFGYVDC CGDTCGFRGW 400
    VPGNMMDGFP CPGCCKSYMP WELEAQSSGV IPEGGVLFTQ STDTVNRESF 450
    KLYGHAVVPF GGAAYWSPYP GMWLPVIWSS VKSYSYLTYT GVVGCKAIVQ 500
    ETDAICRFLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN RGDYSLLLEN 550
    VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSLMVN 600
    FSREVVDMCM DMALLFMHDV KVATKYVKKV TGKVAVRFKA LGIAVVRKIT 650
    EWFDLAVDTA ASAAGWLCYQ LVNGLFAVAN GVITFIQEVP ELVKNFVDKF 700
    KTFFKVLIDS MSVSILSGLT VVKTASNRVC LAGSKVYEVV QKSLPAYIMP 750
    VGCSEATCLV GEIEPAVFED DVVDVVKAPL TYQGCCKPPS SFEKICIVDK 800
    LYMAKCGDQF YPVVVDNDTV GVLDQCWRFP CAGKKVVFND KPKVKEVPST 850
    RKIKIIFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC 900
    KEHGVIGTKV CALLERLVDD YVYLFDEGGE EVIASRMYCS FSAPDEDCVA 950
    TDVVYADENQ DDDADDPVVL VADTQEEDGV AREQVDSADS EICVAHTGGQ 1000
    EMTEPDVVGS QTPIASAEET EVGEACDREG IAEVKATVCA DALDACPDQV 1050
    EAFDIEKVED SILSELQTEL NAPADKTYED VLAFDAIYSE TLSAFYAVPS 1100
    DETHFKVCGF YSPAIERTNC WLRSTLIVMQ SLPLEFKDLG MQKLWLSYKA 1150
    GYDQCFVDKL VKSAPKSIIL PQGGYVADFA YFFLSQCSFK VHANWRCLKC 1200
    GMELKLQGLD AVFFYGDVVS HMCKCGNSMT LLSADIPYTF DFGVRDDKFC 1250
    AFYTPRKVFR AACAVDVNDC HSMAVVDGKQ IDGKVVTKFN GDKFDFMVGH 1300
    GMTFSMSPFE IAQLYGSCIT PNVCFVKGDV IKVLRRVGAE VIVNPANGRM 1350
    AHGAGVAGAI AKAAGKAFIN ETADMVKAQG VCQVGGCYES TGGKLCKKVL 1400
    NIVGPDARGH GNECYSLLER AYQHINKCDN VVTTLISAGI FSVPTDVSLT 1450
    YLLGVVTKNV ILVSNNQDDF DVIEKCQVTS VAGTKALSFQ LAKNLCRDVK 1500
    FVTNACSSLF SESSFVSSYD VLQEVEALRH DIQLDDDARV FVQANMDCLP 1550
    TDWRLVNKFD SVDGVRTIKY FECPGEVFVS SQGKKFGYVQ NGSFKEASVS 1600
    QIRALLANKV DVLCTVDGVN FRSCCVAEGE VFGKTLGSVF CDGINVTKVR 1650
    CSAIHKGKVF FQYSGLSAAD LAAVKDAFGF DEPQLLQYYS MLGMCKWPVV 1700
    VCGNYFAFKQ SNNNCYINVA CLMLQHLSLK FPKWQWRRPG NEFRSGKPLR 1750
    FVSLVLAKGS FKFNEPSDST DFIRVELREA DLSGATCDLE FICKCGVKQE 1800
    QRKGVDAVMH FGTLDKSGLV KGYNIACTCG DKLVHCTQFN VPFLICSNTP 1850
    EGKKLPDDVV AANIFTGGSV GHYTHVKCKP KYQLYDACNV SKVSEAKGNF 1900
    TDCLYLKNLK QTFSSVLTTY YLDDVKCVAY KPDLSQYYCE SGKYYTKPII 1950
    KAQFRTFEKV EGVYTNFKLV GHDIAEKLNA KLGFDCNSPF MEYKITEWPT 2000
    ATGDVVLASD DLYVSRYSGG CVTFGKPVIW RGHEEASLKS LTYFNRPSVV 2050
    CENKFNVLPV DVSEPTDRRP VPSAVLVTGA ASGADASAIS TEPGTAKEQK 2100
    ACASDSVEDQ IVMEAQKKSS VTTVAVKEVK LNGVKKPVKW NCSVVVNDPT 2150
    SETKVVKSLS IVDVYDMFLT GCRYVVWTAN ELSRLINSPT VREYVKWGMS 2200
    KLIIPANLLL LRDEKQEFVA PKVVKAKAIA CYGAVKWFLL YCFSWIKFNT 2250
    DNKVIYTTEV ASKLTFKLCC LAFKNALQTF NWSVVSRGFF LVATVFLLWF 2300
    NFLYANVILS DFYLPNIGPL PMFVGQIVAW VKTTFGVLTI CDFYQVTDLG 2350
    YRSSFCNGSM VCELCFSGFD MLDNYESINV VQHVVDRRVS FDYISLFKLV 2400
    VELVIGYSLY TVCFYPLFVL VGMQLLTTWL PEFFMLGTMH WSARLFVFVA 2450
    NMLPAFTLLR FYIVVTAMYK VYCLCRHVMY GCSKPGCLFC YKRNRSVRVK 2500
    CSTVVGGSLR YYDVMANGGT GFCTKHQWNC LNCNSWKPGN TFITHEAAAD 2550
    LSKELKRPVN PTDSAYYSVI EVKQVGCSMR LFYERDGQRV YDDVSASLFV 2600
    DMNGLLHSKV KGVPETHVVV VENEADKAGF LNAAVFYAQS LYRPMLMVEK 2650
    KLITTANTGL SVSRTMFDLY VYSLLRHLDV DRKSLTSFVN AAHNSLKEGV 2700
    QLEQVMDTFV GCARRKCAID SDVETKSITK SVMAAVNAGV EVTDESCNNL 2750
    VPTYVKSDTI VAADLGVLIQ NNAKHVQSNV AKAANVACIW SVDAFNQLSA 2800
    DLQHRLRKAC VKTGLKIKLT YNKQEANVPI LTTPFSLKGG AVFSRVLQWL 2850
    FVANLICFIV LWALMPTYAV HKSDMQLPLY ASFKVIDNGV LRDVSVTDAC 2900
    FANKFNQFDQ WYESTFGLVY YRNSKACPVV VAVIDQDIGH TLFNVPTKVL 2950
    RYGFHVLHFI THAFATDRVQ CYTPHMQIPY DNFYASGCVL SSLCTMLAHA 3000
    DGTPHPYCYT EGVMHNASLY SSLVPHVRYN LASSNGYIRF PEVVSEGIVR 3050
    VVRTRSMTYC RVGLCEEAEE GICFNFNSSW VLNNPYYRAM PGTFCGRNAF 3100
    DLIHQVLGGL VQPIDFFALT ASSVAGAILA IIVVLAFYYL IKLKRAFGDY 3150
    TSVVVINVIV WCINFLMLFV FQVYPTLSCL YACFYFYTTL YFPSEISVVM 3200
    HLQWLVMYGA IMPLWFCITY VAVVVSNHAL WLFSYCRKIG TDVRSDGTFE 3250
    EMALTTFMIT KESYCKLKNS VSDVAFNRYL SLYNKYRYFS GKMDTATYRE 3300
    AACSQLAKAM ETFNHNNGND VLYQPPTASV TTSFLQSGIV KMVSPTSKVE 3350
    PCVVSVTYGN MTLNGLWLDD KVYCPRHVIC SSADMTDPDY PNLLCRVTSS 3400
    DFCVMSDRMS LTVMSYQMQG SLLVLTVTLQ NPNTPKYSFG VVKPGETFTV 3450
    LAAYNGRPQG AFHVVMRSSH TIKGSFLCGS CGSVGYVLTG DSVRFVYMHQ 3500
    LELSTGCHTG TDFSGNFYGP YRDAQVVQLP VQDYTQTVNV VAWLYAAILN 3550
    RCNWFVQSDS CSLEEFNVWA MTNGFSSIKA DLVLDALASM TGVTVEQVLA 3600
    AIKRLHSGFQ GKQILGSCVL EDELTPSDVY QQLAGVKLQS KRTRVIKGTC 3650
    CWILASTFLF CSIISAFVKW TMFMYVTTHM LGVTLCALCF VIFAMLLIKH 3700
    KHLYLTMYIM PVLCTLFYTN YLVVGYKQSF RGLAYAWLSY FVPAVDYTYM 3750
    DEVLYGVVLL VAMVFVTMRS INHDVFSTMF LVGRLVSLVS MWYFGANLEE 3800
    EVLLFLTSLF GTYTWTTMLS LATAKVIAKW LAVNVLYFTD IPQIKLVLLS 3850
    YLCIGYVCCC YWGVLSLLNS IFRMPLGVYN YKISVQELRY MNANGLRPPR 3900
    NSFEALMLNF KLLGIGGVPV IEVSQIQSRL TDVKCANVVL LNCLQHLHIA 3950
    SNSKLWQYCS TLHNEILATS DLSVAFDKLA QLLVVLFANP AAVDSKCLAS 4000
    IEEVSDDYVR DNTVLQALQS EFVNMASFVE YELAKKNLDE AKASGSANQQ 4050
    QIKQLEKACN IAKSAYERDR AVARKLERMA DLALTNMYKE ARINDKKSKV 4100
    VSALQTMLFS MVRKLDNQAL NSILDNAVKG CVPLNAIPPL TSNTLTIIVP 4150
    DKQVFDQVVD NVYVTYAPNV WHIQSIQDAD GAVKQLNEID VNSTWPLVIS 4200
    ANRHNEVSTV VLQNNELMPQ KLRTQVVNSG SDMNCNIPTQ CYYNTTGTGK 4250
    IVYAILSDCD GLKYTKIVKE DGNCVVLELD PPCKFSVQDV KGLKIKYLYF 4300
    VKGCNTLARG WVVGTLSSTV RLQAGTATEY ASNSAILSLC AFSVDPKKTY 4350
    LDYIQQGGVP VTNCVKMLCD HAGTGMAITI KPEATTNQDS YGGASVCIYC 4400
    RSRVEHPDVD GLCKLRGKFV QVPLGIKDPV SYVLTHDVCQ VCGFWRDGSC 4450
    SCVGTGSQFQ SKDTNFLNGF GVQV 4474

    Note: Produced by conventional translation.

    Length:4,474
    Mass (Da):497,595
    Last modified:June 10, 2008 - v1
    Checksum:i7F09A6BF0E052D83
    GO
    Isoform Replicase polyprotein 1ab (identifier: P0C6Y0-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry P0C6Y0.
    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:7,180
    Mass (Da):803,440
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55148 Genomic RNA. Translation: AAA46457.1.
    M18040 Genomic RNA. Translation: AAA46466.1.
    S51684 Genomic RNA. Translation: AAB19566.1.
    PIRiA36815. RRIHM2.
    B36815. VFIHJH.
    RefSeqiYP_209230.1. AC_000192.1. [P0C6V1-1]

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55148 Genomic RNA. Translation: AAA46457.1 .
    M18040 Genomic RNA. Translation: AAA46466.1 .
    S51684 Genomic RNA. Translation: AAB19566.1 .
    PIRi A36815. RRIHM2.
    B36815. VFIHJH.
    RefSeqi YP_209230.1. AC_000192.1. [P0C6V1-1 ]

    3D structure databases

    ProteinModelPortali P0C6V1.
    SMRi P0C6V1. Positions 4055-4205, 4329-4453.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR022570. Coronavirus_NSP1.
    IPR002589. Macro_dom.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR002705. Pept_C30/C16_B_coronavir.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view ]
    Pfami PF11963. DUF3477. 2 hits.
    PF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF01831. Peptidase_C16. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF08715. Viral_protease. 1 hit.
    [Graphical view ]
    SMARTi SM00506. A1pp. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 1 hit.
    SSF50494. SSF50494. 1 hit.
    SSF53335. SSF53335. 1 hit.
    PROSITEi PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete sequence (22 kilobases) of murine coronavirus gene 1 encoding the putative proteases and RNA polymerase."
      Lee H.-J., Shieh C.-K., Gorbalenya A.E., Koonin E.V., la Monica N., Tuler J., Bagdzhardzhyan A., Lai M.M.C.
      Virology 180:567-582(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Sequence and translation of the murine coronavirus 5'-end genomic RNA reveals the N-terminal structure of the putative RNA polymerase."
      Soe L.H., Shieh C.-K., Baker S.C., Chang M.F., Lai M.M.C.
      J. Virol. 61:3968-3976(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-595.
    3. "Mouse hepatitis virus strain A59 RNA polymerase gene ORF 1a: heterogeneity among MHV strains."
      Bonilla P.J., Gorbalenya A.E., Weiss S.R.
      Virology 198:736-740(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "Murine coronavirus gene 1 polyprotein contains an autoproteolytic activity."
      Baker S.C., La Monica N., Shieh C.K., Lai M.M.
      Adv. Exp. Med. Biol. 276:283-289(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1021-1326.
    5. "Identification of the murine coronavirus MP1 cleavage site recognized by papain-like proteinase 2."
      Kanjanahaluethai A., Jukneliene D., Baker S.C.
      J. Virol. 77:7376-7382(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF PHE-2835; SER-2836; LEU-2837; LYS-2838; GLY-2839; GLY-2840; ALA-2841; VAL-2842 AND VAL-2846.
    6. "Processing of the coronavirus MHV-JHM polymerase polyprotein: identification of precursors and proteolytic products spanning 400 kilodaltons of ORF1a."
      Schiller J.J., Kanjanahaluethai A., Baker S.C.
      Virology 242:288-302(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, SUBCELLULAR LOCATION.
    7. "Conservation of substrate specificities among coronavirus main proteases."
      Hegyi A., Ziebuhr J.
      J. Gen. Virol. 83:595-599(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.

    Entry informationi

    Entry nameiR1A_CVMJH
    AccessioniPrimary (citable) accession number: P0C6V1
    Secondary accession number(s): P19751
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 50 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