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P0C6U9

- R1A_CVM2

UniProt

P0C6U9 - R1A_CVM2

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Murine coronavirus (strain 2) (MHV-2) (Murine hepatitis virus)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 46 (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-PROBy similarity
    Sitei832 – 8332Cleavage; by PL1-PROBy similarity
    Active sitei1068 – 10681For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1219 – 12191For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1663 – 16631For PL2-PRO activityPROSITE-ProRule annotation
    Active sitei1820 – 18201For PL2-PRO activityPROSITE-ProRule annotation
    Sitei2783 – 27842Cleavage; by PL2-PROBy similarity
    Sitei3279 – 32802Cleavage; by 3CL-PROBy similarity
    Active sitei3320 – 33201For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3424 – 34241For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3582 – 35832Cleavage; by 3CL-PROBy similarity
    Sitei3869 – 38702Cleavage; by 3CL-PROBy similarity
    Sitei3961 – 39622Cleavage; by 3CL-PROBy similarity
    Sitei4155 – 41562Cleavage; by 3CL-PROBy similarity
    Sitei4265 – 42662Cleavage; by 3CL-PROBy similarity
    Sitei4402 – 44032Cleavage; by 3CL-PROBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1145 – 117329C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1741 – 177737C4-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4339 – 435517By similarityAdd
    BLAST
    Zinc fingeri4381 – 439414By 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 2) (MHV-2) (Murine hepatitis virus)
    Taxonomic identifieri76344 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]

    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 – 44164416Replicase polyprotein 1aPRO_0000338266Add
    BLAST
    Chaini1 – 247247Non-structural protein 1By similarityPRO_0000338267Add
    BLAST
    Chaini248 – 832585Non-structural protein 2By similarityPRO_0000338268Add
    BLAST
    Chaini833 – 27831951Non-structural protein 3By similarityPRO_0000338269Add
    BLAST
    Chaini2784 – 3279496Non-structural protein 4By similarityPRO_0000338270Add
    BLAST
    Chaini3280 – 35823033C-like proteinaseBy similarityPRO_0000338271Add
    BLAST
    Chaini3583 – 3869287Non-structural protein 6By similarityPRO_0000338272Add
    BLAST
    Chaini3870 – 396192Non-structural protein 7By similarityPRO_0000338273Add
    BLAST
    Chaini3962 – 4155194Non-structural protein 8By similarityPRO_0000338274Add
    BLAST
    Chaini4156 – 4265110Non-structural protein 9By similarityPRO_0000338275Add
    BLAST
    Chaini4266 – 4402137Non-structural protein 10By similarityPRO_0000338276Add
    BLAST
    Chaini4403 – 441614Non-structural protein 11Sequence AnalysisPRO_0000338277Add
    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

    ProteinModelPortaliP0C6U9.
    SMRiP0C6U9. Positions 3997-4147, 4271-4395.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2232 – 225221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2260 – 228021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2346 – 236621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2388 – 240821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2789 – 280921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2869 – 288921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3042 – 306221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3064 – 308421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3096 – 311621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3123 – 314321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3148 – 316821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3591 – 361121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3621 – 364121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3647 – 366721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3690 – 371021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3717 – 373721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3744 – 376421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3788 – 380821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1031 – 1268238Peptidase C16 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1269 – 1429161MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1625 – 1884260Peptidase C16 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini3280 – 3582303Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2232 – 2408177HD1Add
    BLAST
    Regioni2789 – 3168380HD2Add
    BLAST
    Regioni3525 – 3808284HD3Add
    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 fingeri1145 – 117329C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1741 – 177737C4-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4339 – 435517By similarityAdd
    BLAST
    Zinc fingeri4381 – 439414By 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. 1 hit.
    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: P0C6U9-1) [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

    MAKMGKYGLG FKWAPEFPWM LPNASEKLGS PERSEEDGFC PSAAQEPKTK     50
    GKTLINHVRV DCSRLPALEC CVQSAIIRDI FVDEDPLNVE ASTMMALQFG 100
    SAVLVKPSKR LSIQAWAKLG VLPKTPAMGL FKRFCLCNTR ECVCDAHVAF 150
    QLFTVQPDGV CLGNGRFIGW FVPVTAIPAY AKQWLQPWSI LLRKGGNKGS 200
    VTSGHFRRAV TMPVYDFNVE DACEEVHLNP KGKYSRKAYA LLKGYRGVKS 250
    ILFLDQYGCD YTGRLAKGLE DYGDCTLEEM KELFPVWCDS LDNEVVVAWH 300
    VDRDPRAVMR LQTLATIRSI GYVGQPTEDL VDGDVVVREP AHLLAANAIV 350
    KRLPRLVETM LYTDSSVTEF CYKTKLCDCG FITQFGYVDC CGDACDFRGW 400
    VPGNMMDGFL CPGCSKSYMP WELEAQSSGV IPKGGVLFTQ STDTVNRESF 450
    KLYGHAVVPF GSAVYWSPYP GMWLPVIWSS VKSYADLTYT GVVGCKAIVQ 500
    ETDAICRSLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN RGDYSLLLEN 550
    VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSMMVN 600
    FSHEVTDMCM DMALLFMHDV KVATKYVKKV TGKLAVRFKA LGVAVVRKIT 650
    EWFDLAVDTA ASAAGWLCYQ LVNGLFAVAN GGITFLSDVP ELVKNFVDKF 700
    KVFFKVLIDS MSVSVLSGLT VVKTASNRVC LAGCKVYEVV QKRLSAYVMP 750
    VGCNEATCLV GEIEPAVVED DVVDVVKAPL TYQGCCKPPT SFEKICVVDK 800
    LYMAKCGDQF YPVVVDNDTI GVLDQCWRFP CAGKKVEFND KPKVKEIPST 850
    RKIKINFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC 900
    KEHDVIGTKV CALLNRLAED YVYLFDEGGE EVIAPKMYCS FSAPDDEDCV 950
    AADVVDADEN QGDDADDSAA LVTDTQEEDG VAKGQVGVAE SDARLDQVEA 1000
    FDIEKVEDPI LNELSAELNA PADKTYEDVL AFDAIYSEAL SAFYAVPGDE 1050
    THFKVCGFYS PAIERTNCWL RSTLIVMQSL PLEFKDLEMQ KLWLSYKSSY 1100
    NKEFVDKLVK SVPKSIILPQ GGYVADFAYF FLSQCSFKAY ANWRCLKCDM 1150
    DLKLQGLDAM FFYGDVVSHV CKCGTGMTLL SADIPYTLHF GLRDDKFCAF 1200
    YTPRKVFRAA CVVDVNDCHS MAVVDGKQID GKVVTKFNGD KYDFMVGHGM 1250
    AFSMSAFEIA QLYGSCITPN VCFVKGDVIK VLRRVGAEVI VNPANGRMAH 1300
    GAGVAGAIAK AAGKSFIKET ADMVKNQGVC QVGECYESTG GNLCKTVLNI 1350
    VGPDARGHGK QCYSFLERAY QHINKCDDVV TTLISAGIFS VPTDVSLTYL 1400
    IGVVTKNVIL VSNNKDDFDV IEKCQVTSIA GTKALSLQLA KNLCRDVKFE 1450
    TNACDSLFSD SCFVSSYDVL QEVELLRHDI QLDDDARVFV QAHMDNLPAD 1500
    WRLVNKFDSV DGVRTVKYFE CPGEIFVSSQ GKKFGYVQNG SFKVASVSQI 1550
    RALLANKVDV LCTVDGVNFR SCCVAEGEVF GKTLGSVFCD GINVTKVRCS 1600
    AIHKGKVFFQ YSGLSAADLV AVTDAFGFDE PQLLKYYNML GMCKWPVVVC 1650
    GNYFAFKQSN NNCYINVACL MLQHLSLKFH KWQWQEAWNE FRSGKPLRFV 1700
    SLVLAKGSFK FNEPSDSTDF MRVVLREADL SGATCDFEFV CKCGVKQEQR 1750
    KGVDAVMHFG TLDKGDLAKG YTIACTCGNK LVHCTQLNVP FLICSNKPEG 1800
    KKLPDDVVAA NIFTGGSLGH YTHVKCKPKY QLYDACNVSK VSEAKGNFTD 1850
    CLYLKNLKQT FSSKLTTFYL DDVKCVEYNP DLSQYYCESG KYYTKPIIKA 1900
    QFRTFEKVEG VYTNFKLVGH SIAEKFNAKL GFDCNSPFTE YKITEWPTAT 1950
    GDVVLASDDL YVSRYSGGCV TFGKPVIWLG HEEASLKSLT YFNRPSVVCE 2000
    NKFNVLPVDV SEPTDKGPVP AAVLVTGALS GAATAPGTAK EQKVCASDSV 2050
    VDQVVSGFLS DLSGATVDVK EVKLNGVKKP IKVEDSVVVN DPTSETKVVK 2100
    SLSIVDVYDM FLTGCRYVVW MANELSRLVN SPTVREYVKW GMTKIVIPAK 2150
    LVLLRDEKQE FVAPKVVKAK VIACYSAVKW FFLYCFSWIK FNTDNKVIYT 2200
    TEVASKLTFN LCCLAFKNAL QTFNWNVVSR GFFLVATVFL LWFNFLYANV 2250
    ILSDFYLPNI GFFPTFVGQI VAWVKTTFGI FTLCDLYQVS DVGYRSSFCN 2300
    GSMVCELCFS GFDMLDNYDA INVVQHVVDR RVSFDYISLF KLVVELVIGY 2350
    SLYTVCFYPL FGLIGMQLLT TWLPEFFMLE TMHWSARFFV FVANMLPAFT 2400
    LLRFYIVVTA MYKIFCLCRH VMYGCSRPGC LFCYKRNRSV RVKCSTVVGG 2450
    TLRYYDVMAN GGTGFCAKHQ WNCLNCSAFG PGNTFITHEA AADLSKELKR 2500
    PVNPTDSAYY LVTEVKQVGC SMRLFYERDG QRVYDDVSAS LFVDMNGLLH 2550
    SKVKGVPETH VVVVENEADK AGFLNAAVFY AQSLYRPMLL VEKKLITTAN 2600
    TGLSVSQTMF DLYVDSLLGV LDVDRKSLTS FVNAAHNSLK EGVQLEQVMD 2650
    TFIGCARRKC AIDSDVETKS ITKSIMSAVN AGVDFTDESC NNLVPTYVKS 2700
    DTIVAADLGV LIQNNAKHVQ ANVAKAANVA CIWSVDAFNQ LSADLQHRLR 2750
    KACSKTGLKI KLTYNKQEAN VPILTTPFSL KGGAVFSKVL QWLFVVNLIC 2800
    FIVLWALMPT YAVHKSDMQL PLYASFKVID NGVLRDVTVT DACFANKFIQ 2850
    FDQWYESTFG LVYYRNSRAC PVVVAVIDQD IGYTLFNVPT KVLRYGFHVL 2900
    HFITHAFATD SVQCYTPHMQ IPYDNFYASG CVLSSLCTML AHADGTPHPY 2950
    CYTEGIMHNA SLYDSLAPHV RYNLANSNGY IRFPEVVSEG IVRIVRTRSM 3000
    TYCRVGLCED AEEGVCFNFN SSWVLNNPYY RAMPGTFCGR NAFDLIHQVL 3050
    GGLVRPIDFF ALTASSVAGA ILAIIVVLAF YYLIKLKRAF GDYTSVVVIN 3100
    VIVWCINFLM LFVFQVYPTL SCLYACFYFY TTLYFPSEIS VVMHLQWLVM 3150
    YGAIMPLWFC IIYVAVVVSN HALWLFSYCR KLGTEVRSDG TFEEMSLTTF 3200
    MITKESYCKL KNSVSDVAFN RYLSLYNKYR YFSGKMDTAA YREAACSQLA 3250
    KAMETFNHNN GNDVLYQPPT ASVTTSFLQS GIVKMVFPTS KVEPCVVSVT 3300
    YGNMTLNGLW LDDKVYCPRH VICSSADMTD PDYSNLLCRV ISSDFCVMSG 3350
    RMSLTVMSYQ MQGSLLVLTV TLQNPNTPKY SFGVVKPGET FTVLAAYNGK 3400
    SQGAFHVTMR SSYTIKGSFL CGSCGSVGYV LTGDSVRFVY MHQLELSTGC 3450
    HTGTDFSGNF YGPYRDAQVV QLPVQDYTQT VNVVAWLYAA ILNRCNWFVQ 3500
    SDSCSLEEFN VWAMTNGFSS IKADLVLDAL ASMTGVTVEQ ILAAIKRLYS 3550
    GFQGKQILGS CVLEDELTPS DVYQQLAGVK LQSKRTRVVK GTCCWILAST 3600
    LLFCSIISAF VKWTMFMYVT THMLGVTLCA LCFVSFAMLL VKHKHLYLTM 3650
    FIMPVLCTLF YTNYLVVYKQ SFRGLAYAWL SHFVPAVDYT YMDEVLYGVV 3700
    LLVAMVFVTM RSINHDVFSV MFLVGRLVSL VSMWYFGANL EEEVLLFLTS 3750
    LFGTYTWTTM LSLATAKVIA KWLAVNVLYF TDVPQVKLVL LSYLCIGYVC 3800
    CCYWGVLSLL NSIFRMPLGV YNYKISVQEL RYMNANGLRP PRNSFEALVL 3850
    NFKLLGIGGV PVIEVSQIQS RLTDVKCVNV VLLNCLQHLH IASSSKLWQY 3900
    CSTLHNEILA TSDLSVAFDK LAQLLVVLFA NPAAVDSKCL ASIEEVSDDY 3950
    VRDSTVLQAL QSEFVNMASF VEYELAKKNL DEAKASGSAN QQQIKQLEKA 4000
    CNIAKSAYER DRAVARKLER MADLALTNMY KEARINDKKS KVVSALQTML 4050
    FSMIRKLDNQ ALNSILDNAV KGCVPLNAIP SLTSNTLTII VPDKQVFDQV 4100
    VDNVYVTYAG NVWHIQSIQD ADGAVKQLNE IDVNITWPLV IAANRHNEVS 4150
    SVVLQNNELM PQKLRTQVVN SGSDMNCNTP TQCYYNTTGM GKIVYAILSD 4200
    CDGLKYTKIV KEDGNCVVLE LDPPCKFSVQ DVKGLKIKYL YFVKGCNTLA 4250
    RGWVVGTLSS TVRLQAGTAT EYASNSAIRS LCAFSVDPKK TYLDYIQQGG 4300
    APVTNCVKML CDHAGTGMAI TIKPEATTNQ DSYGGASVCI YCRSRVEHPD 4350
    VDGLCKLRGK FVQVPLGIKD PVSYVLTHDV CQVCGFWRDG SCSCVGTGSQ 4400
    FQSKDTNFLN GFGVQV 4416

    Note: Produced by conventional translation.

    Length:4,416
    Mass (Da):491,187
    Last modified:June 10, 2008 - v1
    Checksum:i4FD965F1EEC15362
    GO
    Isoform Replicase polyprotein 1ab (identifier: P0C6X8-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry P0C6X8.
    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:7,124
    Mass (Da):797,625
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF201929 Genomic RNA. Translation: AAF19383.1.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF201929 Genomic RNA. Translation: AAF19383.1 .

    3D structure databases

    ProteinModelPortali P0C6U9.
    SMRi P0C6U9. Positions 3997-4147, 4271-4395.
    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. 1 hit.
    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. "Pathogenesis and sequence analysis of mouse hepatitis virus type 2: an experimental model system of acute meningitis and hepatitis in mice."
      Das Sarma J., Hingley S.T., Lai M.M.C., Weiss S.R., Lavi E.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiR1A_CVM2
    AccessioniPrimary (citable) accession number: P0C6U9
    Secondary accession number(s): Q9PYA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 46 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    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