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P0C6X9

- R1AB_CVMA5

UniProt

P0C6X9 - R1AB_CVMA5

Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.
    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
    The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) By similarity.By similarity
    The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction.By similarity
    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
    NendoU is a Mn2+-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.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

    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
    ATP + H2O = ADP + phosphate.
    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 sitei1121 – 11211For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1272 – 12721For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1716 – 17161For PL2-PRO activityPROSITE-ProRule annotation
    Active sitei1873 – 18731For PL2-PRO activityPROSITE-ProRule annotation
    Sitei2837 – 28382Cleavage; by PL2-PRO
    Sitei3333 – 33342Cleavage; by 3CL-PRO
    Active sitei3374 – 33741For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3478 – 34781For 3CL-PRO activity
    Sitei3635 – 36362Cleavage; by 3CL-PRO
    Sitei3921 – 39222Cleavage; by 3CL-PRO
    Sitei4013 – 40142Cleavage; by 3CL-PRO
    Sitei4207 – 42082Cleavage; by 3CL-PRO
    Sitei4317 – 43182Cleavage; by 3CL-PRO
    Sitei4454 – 44552Cleavage; by 3CL-PRO
    Sitei5382 – 53832Cleavage; by 3CL-PRO
    Sitei5982 – 59832Cleavage; by 3CL-PROCurated
    Sitei6503 – 65042Cleavage; by 3CL-PROCurated
    Sitei6877 – 68782Cleavage; by 3CL-PROCurated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1198 – 122629C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1794 – 183037C4-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4391 – 440717By similarityAdd
    BLAST
    Zinc fingeri4433 – 444614By similarityAdd
    BLAST
    Nucleotide bindingi5663 – 56708ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cysteine-type endopeptidase activity Source: InterPro
    3. endonuclease activity Source: UniProtKB-KW
    4. exoribonuclease activity, producing 5'-phosphomonoesters Source: InterPro
    5. helicase activity Source: UniProtKB-KW
    6. methyltransferase activity Source: InterPro
    7. omega peptidase activity Source: InterPro
    8. RNA binding Source: UniProtKB-KW
    9. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    10. 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 gene expression 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. transcription, DNA-templated Source: InterPro
    8. viral protein processing Source: InterPro
    9. viral RNA genome replication Source: InterPro

    Keywords - Molecular functioni

    Endonuclease, Exonuclease, Helicase, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase

    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 ISG15 by virus, Modulation of host ubiquitin pathway by viral deubiquitinase, Modulation of host ubiquitin pathway by virus, Ubl conjugation pathway, Viral immunoevasion, Viral RNA replication

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Replicase polyprotein 1ab
    Short name:
    pp1ab
    Alternative name(s):
    ORF1ab polyprotein
    Cleaved into the following 15 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
    RNA-directed RNA polymerase (EC:2.7.7.48)
    Short name:
    Pol
    Short name:
    RdRp
    Alternative name(s):
    nsp12
    p100
    Helicase (EC:3.6.4.12, EC:3.6.4.13)
    Short name:
    Hel
    Alternative name(s):
    nsp13
    p67
    Exoribonuclease (EC:3.1.13.-)
    Short name:
    ExoN
    Alternative name(s):
    nsp14
    Alternative name(s):
    NendoU
    nsp15
    p35
    Alternative name(s):
    nsp16
    Gene namesi
    Name:rep
    ORF Names:1a-1b
    OrganismiMurine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus)
    Taxonomic identifieri11142 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
    Virus hostiMus musculus (Mouse) [TaxID: 10090]
    ProteomesiUP000007192: 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.
    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.
    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.
    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.
    Chain Helicase : Host endoplasmic reticulum-Golgi intermediate compartment Curated
    Note: The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA.1 Publication

    GO - Cellular componenti

    1. host cell endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
    2. host cell membrane Source: UniProtKB-SubCell
    3. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Host cytoplasm, Host membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi3331 – 33311F → A, H or W: No effect. 1 Publication
    Mutagenesisi3332 – 33321L → I or S: No processing between peptide HD2 and 3CL-PRO. 1 Publication
    Mutagenesisi3333 – 33331Q → A, K or R: No processing between peptide HD2 and 3CL-PRO. 1 Publication
    Mutagenesisi3334 – 33341S → A: No effect. 1 Publication
    Mutagenesisi3334 – 33341S → C: No processing between peptide HD2 and 3CL-PRO. 1 Publication
    Mutagenesisi3335 – 33351G → A: No effect. 1 Publication
    Mutagenesisi3335 – 33351G → P: No processing between peptide HD2 and 3CL-PRO. 1 Publication
    Mutagenesisi3336 – 33361I → L: No effect. 1 Publication
    Mutagenesisi3478 – 34781C → A: Complete loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi5381 – 53811L → I: No processing between RDRP and helicase. 1 Publication
    Mutagenesisi5381 – 53811L → M: No effect. 1 Publication
    Mutagenesisi5382 – 53821Q → K or R: No processing between RDRP and helicase. 1 Publication
    Mutagenesisi5383 – 53831S → A: No effect. 1 Publication
    Mutagenesisi5383 – 53831S → N: No processing between RDRP and helicase. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 247247Non-structural protein 1CuratedPRO_0000037338Add
    BLAST
    Chaini248 – 832585Non-structural protein 2CuratedPRO_0000037339Add
    BLAST
    Chaini833 – 28372005Non-structural protein 3CuratedPRO_0000037340Add
    BLAST
    Chaini2838 – 3333496Non-structural protein 4PRO_0000037341Add
    BLAST
    Chaini3334 – 36353023C-like proteinasePRO_0000037342Add
    BLAST
    Chaini3636 – 3921286Non-structural protein 6CuratedPRO_0000037343Add
    BLAST
    Chaini3922 – 401392Non-structural protein 7PRO_0000037344Add
    BLAST
    Chaini4014 – 4207194Non-structural protein 8PRO_0000037345Add
    BLAST
    Chaini4208 – 4317110Non-structural protein 9PRO_0000037346Add
    BLAST
    Chaini4318 – 4454137Non-structural protein 10PRO_0000037347Add
    BLAST
    Chaini4455 – 5382928RNA-directed RNA polymerasePRO_0000037348Add
    BLAST
    Chaini5383 – 5982600HelicaseCuratedPRO_0000037349Add
    BLAST
    Chaini5983 – 6503521ExoribonucleaseBy similarityPRO_0000037350Add
    BLAST
    Chaini6504 – 6877374Uridylate-specific endoribonucleaseBy similarityPRO_0000037351Add
    BLAST
    Chaini6878 – 7176299Putative 2'-O-methyl transferaseBy similarityPRO_0000037352Add
    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

    Secondary structure

    1
    7176
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3246 – 32494
    Beta strandi3254 – 32563
    Helixi3258 – 326710
    Helixi3270 – 32789
    Helixi3280 – 32845
    Beta strandi3287 – 32904
    Helixi3292 – 331322
    Beta strandi3318 – 33203
    Beta strandi3326 – 33305

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GTHX-ray2.70A6504-6872[»]
    2GTIX-ray2.15A6504-6872[»]
    3VC8X-ray2.00A/B3245-3333[»]
    3VCBX-ray2.40A/B3245-3333[»]
    ProteinModelPortaliP0C6X9.
    SMRiP0C6X9. Positions 4049-4199, 4323-4447, 6504-6872.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C6X9.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2225 – 224521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2286 – 230621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2314 – 233421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2400 – 242021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2442 – 246221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2625 – 264521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2847 – 286721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3096 – 311621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3118 – 313821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3150 – 317021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3177 – 319721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3202 – 322221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3644 – 366421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3674 – 369421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3699 – 371921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3742 – 376221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3769 – 378921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3796 – 381621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3840 – 386021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1084 – 1333250Peptidase C16 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1323 – 1482160MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1678 – 1937260Peptidase C16 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini3334 – 3635302Peptidase C30PROSITE-ProRule annotationAdd
    BLAST
    Domaini5062 – 5224163RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini5383 – 546684CV MBDAdd
    BLAST
    Domaini5638 – 5819182(+)RNA virus helicase ATP-bindingAdd
    BLAST
    Domaini5820 – 5989170(+)RNA virus helicase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2225 – 2645421HD1Add
    BLAST
    Regioni2847 – 3222376HD2Add
    BLAST
    Regioni3526 – 3860335HD3Add
    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
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1198 – 122629C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1794 – 183037C4-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4391 – 440717By similarityAdd
    BLAST
    Zinc fingeri4433 – 444614By similarityAdd
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
    IPR022570. Coronavirus_NSP1.
    IPR009461. Coronavirus_NSP16.
    IPR027352. CV_MBD_dom.
    IPR002589. Macro_dom.
    IPR009466. NSP11.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR027417. P-loop_NTPase.
    IPR002705. Pept_C30/C16_B_coronavir.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009469. RNA_pol_N_coronovir.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view]
    PfamiPF06478. Corona_RPol_N. 1 hit.
    PF11963. DUF3477. 2 hits.
    PF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF06471. NSP11. 1 hit.
    PF06460. NSP13. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF01831. Peptidase_C16. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF00680. RdRP_1. 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.
    SSF52540. SSF52540. 1 hit.
    SSF53335. SSF53335. 2 hits.
    PROSITEiPS51653. CV_MBD. 1 hit.
    PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 2 hits.
    PS51657. PSRV_HELICASE. 1 hit.
    PS50507. RDRP_SSRNA_POS. 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 1ab (identifier: P0C6X9-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    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 LPNASEKLGN PERSEEDGFC PSAAQEPKVK     50
    GKTLVNHVRV NCSRLPALEC CVQSAIIRDI FVDEDPQKVE ASTMMALQFG 100
    SAVLVKPSKR LSIQAWTNLG VLPKTAAMGL FKRVCLCNTR ECSCDAHVAF 150
    HLFTVQPDGV CLGNGRFIGW FVPVTAIPEY AKQWLQPWSI LLRKGGNKGS 200
    VTSGHFRRAV TMPVYDFNVE DACEEVHLNP KGKYSCKAYA LLKGYRGVKP 250
    ILFVDQYGCD YTGCLAKGLE DYGDLTLSEM KELFPVWRDS LDSEVLVAWH 300
    VDRDPRAAMR LQTLATVRCI DYVGQPTEDV VDGDVVVREP AHLLAANAIV 350
    KRLPRLVETM LYTDSSVTEF CYKTKLCECG FITQFGYVDC CGDTCDFRGW 400
    VAGNMMDGFP CPGCTKNYMP WELEAQSSGV IPEGGVLFTQ STDTVNRESF 450
    KLYGHAVVPF GSAVYWSPCP GMWLPVIWSS VKSYSGLTYT GVVGCKAIVQ 500
    ETDAICRSLY MDYVQHKCGN LEQRAILGLD DVYHRQLLVN RGDYSLLLEN 550
    VDLFVKRRAE FACKFATCGD GLVPLLLDGL VPRSYYLIKS GQAFTSMMVN 600
    FSHEVTDMCM DMALLFMHDV KVATKYVKKV TGKLAVRFKA LGVAVVRKIT 650
    EWFDLAVDIA ASAAGWLCYQ LVNGLFAVAN GVITFVQEVP ELVKNFVDKF 700
    KAFFKVLIDS MSVSILSGLT VVKTASNRVC LAGSKVYEVV QKSLSAYVMP 750
    VGCSEATCLV GEIEPAVFED DVVDVVKAPL TYQGCCKPPT SFEKICIVDK 800
    LYMAKCGDQF YPVVVDNDTV GVLDQCWRFP CAGKKVEFND KPKVRKIPST 850
    RKIKITFALD ATFDSVLSKA CSEFEVDKDV TLDELLDVVL DAVESTLSPC 900
    KEHDVIGTKV CALLDRLAGD YVYLFDEGGD EVIAPRMYCS FSAPDDEDCV 950
    AADVVDADEN QDDDAEDSAV LVADTQEEDG VAKGQVEADS EICVAHTGSQ 1000
    EELAEPDAVG SQTPIASAEE TEVGEASDRE GIAEAKATVC ADAVDACPDQ 1050
    VEAFEIEKVE DSILDELQTE LNAPADKTYE DVLAFDAVCS EALSAFYAVP 1100
    SDETHFKVCG FYSPAIERTN CWLRSTLIVM QSLPLEFKDL EMQKLWLSYK 1150
    AGYDQCFVDK LVKSVPKSII LPQGGYVADF AYFFLSQCSF KAYANWRCLE 1200
    CDMELKLQGL DAMFFYGDVV SHMCKCGNSM TLLSADIPYT LHFGVRDDKF 1250
    CAFYTPRKVF RAACAVDVND CHSMAVVEGK QIDGKVVTKF IGDKFDFMVG 1300
    YGMTFSMSPF ELAQLYGSCI TPNVCFVKGD VIKVVRLVNA EVIVNPANGR 1350
    MAHGAGVAGA IAEKAGSAFI KETSDMVKAQ GVCQVGECYE SAGGKLCKKV 1400
    LNIVGPDARG HGKQCYSLLE RAYQHINKCD NVVTTLISAG IFSVPTDVSL 1450
    TYLLGVVTKN VILVSNNQDD FDVIEKCQVT SVAGTKALSL QLAKNLCRDV 1500
    KFVTNACSSL FSESCFVSSY DVLQEVEALR HDIQLDDDAR VFVQANMDCL 1550
    PTDWRLVNKF DSVDGVRTIK YFECPGGIFV SSQGKKFGYV QNGSFKEASV 1600
    SQIRALLANK VDVLCTVDGV NFRSCCVAEG EVFGKTLGSV FCDGINVTKV 1650
    RCSAIYKGKV FFQYSDLSEA DLVAVKDAFG FDEPQLLKYY TMLGMCKWPV 1700
    VVCGNYFAFK QSNNNCYINV ACLMLQHLSL KFPKWQWQEA WNEFRSGKPL 1750
    RFVSLVLAKG SFKFNEPSDS IDFMRVVLRE ADLSGATCNL EFVCKCGVKQ 1800
    EQRKGVDAVM HFGTLDKGDL VRGYNIACTC GSKLVHCTQF NVPFLICSNT 1850
    PEGRKLPDDV VAANIFTGGS VGHYTHVKCK PKYQLYDACN VNKVSEAKGN 1900
    FTDCLYLKNL KQTFSSVLTT FYLDDVKCVE YKPDLSQYYC ESGKYYTKPI 1950
    IKAQFRTFEK VDGVYTNFKL VGHSIAEKLN AKLGFDCNSP FVEYKITEWP 2000
    TATGDVVLAS DDLYVSRYSS GCITFGKPVV WLGHEEASLK SLTYFNRPSV 2050
    VCENKFNVLP VDVSEPTDKG PVPAAVLVTG VPGADASAGA GIAKEQKACA 2100
    SASVEDQVVT EVRQEPSVSA ADVKEVKLNG VKKPVKVEGS VVVNDPTSET 2150
    KVVKSLSIVD VYDMFLTGCK YVVWTANELS RLVNSPTVRE YVKWGMGKIV 2200
    TPAKLLLLRD EKQEFVAPKV VKAKAIACYC AVKWFLLYCF SWIKFNTDNK 2250
    VIYTTEVASK LTFKLCCLAF KNALQTFNWS VVSRGFFLVA TVFLLWFNFL 2300
    YANVILSDFY LPNIGPLPTF VGQIVAWFKT TFGVSTICDF YQVTDLGYRS 2350
    SFCNGSMVCE LCFSGFDMLD NYDAINVVQH VVDRRLSFDY ISLFKLVVEL 2400
    VIGYSLYTVC FYPLFVLIGM QLLTTWLPEF FMLETMHWSA RLFVFVANML 2450
    PAFTLLRFYI VVTAMYKVYC LCRHVMYGCS KPGCLFCYKR NRSVRVKCST 2500
    VVGGSLRYYD VMANGGTGFC TKHQWNCLNC NSWKPGNTFI THEAAADLSK 2550
    ELKRPVNPTD SAYYSVTEVK QVGCSMRLFY ERDGQRVYDD VNASLFVDMN 2600
    GLLHSKVKGV PETHVVVVEN EADKAGFLGA AVFYAQSLYR PMLMVEKKLI 2650
    TTANTGLSVS RTMFDLYVDS LLNVLDVDRK SLTSFVNAAH NSLKEGVQLE 2700
    QVMDTFIGCA RRKCAIDSDV ETKSITKSVM SAVNAGVDFT DESCNNLVPT 2750
    YVKSDTIVAA DLGVLIQNNA KHVQANVAKA ANVACIWSVD AFNQLSADLQ 2800
    HRLRKACSKT GLKIKLTYNK QEANVPILTT PFSLKGGAVF SRMLQWLFVA 2850
    NLICFIVLWA LMPTYAVHKS DMQLPLYASF KVIDNGVLRD VSVTDACFAN 2900
    KFNQFDQWYE STFGLAYYRN SKACPVVVAV IDQDIGHTLF NVPTTVLRYG 2950
    FHVLHFITHA FATDSVQCYT PHMQIPYDNF YASGCVLSSL CTMLAHADGT 3000
    PHPYCYTGGV MHNASLYSSL APHVRYNLAS SNGYIRFPEV VSEGIVRVVR 3050
    TRSMTYCRVG LCEEAEEGIC FNFNRSWVLN NPYYRAMPGT FCGRNAFDLI 3100
    HQVLGGLVRP IDFFALTASS VAGAILAIIV VLAFYYLIKL KRAFGDYTSV 3150
    VVINVIVWCI NFLMLFVFQV YPTLSCLYAC FYFYTTLYFP SEISVVMHLQ 3200
    WLVMYGAIMP LWFCIIYVAV VVSNHALWLF SYCRKIGTEV RSDGTFEEMA 3250
    LTTFMITKES YCKLKNSVSD VAFNRYLSLY NKYRYFSGKM DTAAYREAAC 3300
    SQLAKAMETF NHNNGNDVLY QPPTASVTTS FLQSGIVKMV SPTSKVEPCI 3350
    VSVTYGNMTL NGLWLDDKVY CPRHVICSSA DMTDPDYPNL LCRVTSSDFC 3400
    VMSGRMSLTV MSYQMQGCQL VLTVTLQNPN TPKYSFGVVK PGETFTVLAA 3450
    YNGRPQGAFH VTLRSSHTIK GSFLCGSCGS VGYVLTGDSV RFVYMHQLEL 3500
    STGCHTGTDF SGNFYGPYRD AQVVQLPVQD YTQTVNVVAW LYAAIFNRCN 3550
    WFVQSDSCSL EEFNVWAMTN GFSSIKADLV LDALASMTGV TVEQVLAAIK 3600
    RLHSGFQGKQ ILGSCVLEDE TPSDVYQQLA GVKLQSKRTR VIKGTCCWIL 3650
    ASTFLFCSII SAFVKWTMFM YVTTHMLGVT LCALCFVSFA MLLIKHKHLY 3700
    LTMYIMPVLC TFYTNYLVVY KQSFRGLAYA WLSHFVPAVD YTYMDEVLYG 3750
    VVLLVAMVFV TMRSINHDVF SIMFLVGRLV SLVSMWYFGA NLEEEVLLFL 3800
    TSLFGTYTWT TMLSLATAKV IAKWLAVNVL YFTDVPQIKL VLLSYLCIGY 3850
    VCCCYWGILS LLNSIFRMPL GVYNYKISVQ ELRYMNANGL RPPRNSFEAL 3900
    MLNFKLLGIG GVPVIEVSQI QSRLTDVKCA NVVLLNCLQH LHIASNSKLW 3950
    QYCSTLHNEI LATSDLSMAF DKLAQLLVVL FANPAAVDSK CLASIEEVSD 4000
    DYVRDNTVLQ ALQSEFVNMA SFVEYELAKK NLDEAKASGS ANQQQIKQLE 4050
    KACNIAKSAY ERDRAVARKL ERMADLALTN MYKEARINDK KSKVVSALQT 4100
    MLFSMVRKLD NQALNSILDN AVKGCVPLNA IPSLTSNTLT IIVPDKQVFD 4150
    QVVDNVYVTY AGNVWHIQFI QDADGAVKQL NEIDVNSTWP LVIAANRHNE 4200
    VSTVVLQNNE LMPQKLRTQV VNSGSDMNCN TPTQCYYNTT GTGKIVYAIL 4250
    SDCDGLKYTK IVKEDGNCVV LELDPPCKFS VQDVKGLKIK YLYFVKGCNT 4300
    LARGWVVGTL SSTVRLQAGT ATEYASNSAI LSLCAFSVDP KKTYLDYIKQ 4350
    GGVPVTNCVK MLCDHAGTGM AITIKPEATT NQDSYGGASV CIYCRSRVEH 4400
    PDVDGLCKLR GKFVQVPLGI KDPVSYVLTH DVCQVCGFWR DGSCSCVGTG 4450
    SQFQSKDTNF LNRIRGTSVN ARLVPCASGL DTDVQLRAFD ICNANRAGIG 4500
    LYYKVNCCRF QRVDEDGNKL DKFFVVKRTN LEVYNKEKEC YELTKECGVV 4550
    AEHEFFTFDV EGSRVPHIVR KDLSKFTMLD LCYALRHFDR NDCSTLKEIL 4600
    LTYAECEESY FQKKDWYDFV ENPDIINVYK KLGPIFNRAL LNTAKFADAL 4650
    VEAGLVGVLT LDNQDLYGQW YDFGDFVKTV PGCGVAVADS YYSYMMPMLT 4700
    MCHALDSELF VNGTYREFDL VQYDFTDFKL ELFTKYFKHW SMTYHPNTCE 4750
    CEDDRCIIHC ANFNILFSMV LPKTCFGPLV RQIFVDGVPF VVSIGYHYKE 4800
    LGVVMNMDVD THRYRLSLKD LLLYAADPAL HVASASALLD LRTCCFSVAA 4850
    ITSGVKFQTV KPGNFNQDFY EFILSKGLLK EGSSVDLKHF FFTQDGNAAI 4900
    TDYNYYKYNL PTMVDIKQLL FVLEVVNKYF EIYEGGCIPA TQVIVNNYDK 4950
    SAGYPFNKFG KARLYYEALS FEEQDEIYAY TKRNVLPTLT QMNLKYAISA 5000
    KNRARTVAGV SILSTMTGRM FHQKCLKSIA ATRGVPVVIG TTKFYGGWDD 5050
    MLRRLIKDVD SPVLMGWDYP KCDRAMPNIL RIVSSLVLAR KHDSCCSHTD 5100
    RFYRLANECA QVLSEIVMCG GCYYVKPGGT SSGDATTAFA NSVFNICQAV 5150
    SANVCSLMAC NGHKIEDLSI RELQKRLYSN VYRADHVDPA FVSEYYEFLN 5200
    KHFSMMILSD DGVVCYNSEF ASKGYIANIS AFQQVLYYQN NVFMSEAKCW 5250
    VETDIEKGPH EFCSQHTMLV KMDGDEVYLP YPDPSRILGA GCFVDDLLKT 5300
    DSVLLIERFV SLAIDAYPLV YHENPEYQNV FRVYLEYIKK LYNDLGNQIL 5350
    DSYSVILSTC DGQKFTDETF YKNMYLRSAV LQSVGACVVC SSQTSLRCGS 5400
    CIRKPLLCCK CAYDHVMSTD HKYVLSVSPY VCNSPGCDVN DVTKLYLGGM 5450
    SYYCEDHKPQ YSFKLVMNGM VFGLYKQSCT GSPYIEDFNK IASCKWTEVD 5500
    DYVLANECTE RLKLFAAETQ KATEEAFKQC YASATIREIV SDRELILSWE 5550
    IGKVRPPLNK NYVFTGYHFT NNGKTVLGEY VFDKSELTNG VYYRATTTYK 5600
    LSVGDVFILT SHAVSSLSAP TLVPQENYTS IRFASVYSVP ETFQNNVPNY 5650
    QHIGMKRYCT VQGPPGTGKS HLAIGLAVYY CTARVVYTAA SHAAVDALCE 5700
    KAHKFLNIND CTRIVPAKVR VDCYDKFKVN DTTRKYVFTT INALPELVTD 5750
    IIVVDEVSML TNYELSVINS RVRAKHYVYI GDPAQLPAPR VLLNKGTLEP 5800
    RYFNSVTKLM CCLGPDIFLG TCYRCPKEIV DTVSALVYNN KLKAKNDNSS 5850
    MCFKVYYKGQ TTHESSSAVN MQQIHLISKF LKANPSWSNA VFISPYNSQN 5900
    YVAKRVLGLQ TQTVDSAQGS EYDFVIYSQT AETAHSVNVN RFNVAITRAK 5950
    KGILCVMSSM QLFESLNFTT LTLDKINNPR LQCTTNLFKD CSRSYVGYHP 6000
    AHAPSFLAVD DKYKVGGDLA VCLNVADSAV TYSRLISLMG FKLDLTLDGY 6050
    CKLFITRDEA IKRVRAWVGF DAEGAHAIRD SIGTNFPLQL GFSTGIDFVV 6100
    EATGMFAERD GYVFKKAAAR APPGEQFKHL IPLMSRGQKW DVVRIRIVQM 6150
    LSDHLVDLAD SVVLVTWAAS FELTCLRYFA KVGREVVCSV CTKRATCFNS 6200
    RTGYYGCWRH SYSCDYLYNP LIVDIQQWGY TGSLTSNHDP ICSVHKGAHV 6250
    ASSDAIMTRC LAVHDCFCKS VNWNLEYPII SNEVSVNTSC RLLQRVMFRA 6300
    AMLCNRYDVC YDIGNPKGLA CVKGYDFKFY DASPVVKSVK QFVYKYEAHK 6350
    DQFLDGLCMF WNCNVDKYPA NAVVCRFDTR VLNKLNLPGC NGGSLYVNKH 6400
    AFHTSPFTRA AFENLKPMPF FYYSDTPCVY MEGMESKQVD YVPLRSATCI 6450
    TRCNLGGAVC LKHAEEYREY LESYNTATTA GFTFWVYKTF DFYNLWNTFT 6500
    RLQSLENVVY NLVNAGHFDG RAGELPCAVI GEKVIAKIQN EDVVVFKNNT 6550
    PFPTNVAVEL FAKRSIRPHP ELKLFRNLNI DVCWSHVLWD YAKDSVFCSS 6600
    TYKVCKYTDL QCIESLNVLF DGRDNGALEA FKKCRNGVYI NTTKIKSLSM 6650
    IKGPQRADLN GVVVEKVGDS DVEFWFAVRK DGDDVIFSRT GSLEPSHYRS 6700
    PQGNPGGNRV GDLSGNEALA RGTIFTQSRL LSSFTPRSEM EKDFMDLDDD 6750
    VFIAKYSLQD YAFEHVVYGS FNQKIIGGLH LLIGLARRQQ KSNLVIQEFV 6800
    TYDSSIHSYF ITDENSGSSK SVCTVIDLLL DDFVDIVKSL NLKCVSKVVN 6850
    VNVDFKDFQF MLWCNEEKVM TFYPRLQAAA DWKPGYVMPV LYKYLESPLE 6900
    RVNLWNYGKP ITLPTGCMMN VAKYTQLCQY LSTTTLAVPA NMRVLHLGAG 6950
    SDKGVAPGSA VLRQWLPAGS ILVDNDVNPF VSDSVASYYG NCITLPFDCQ 7000
    WDLIISDMYD PLTKNIGEYN VSKDGFFTYL CHLIRDKLAL GGSVAIKITE 7050
    FSWNAELYSL MGKFAFWTIF CTNVNASSSE GFLIGINWLN KTRTEIDGKT 7100
    MHANYLFWRN STMWNGGAYS LFDMSKFPLK AAGTAVVSLK PDQINDLVLS 7150
    LIEKGKLLVR DTRKEVFVGD SLVNVK 7176

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

    Length:7,176
    Mass (Da):802,596
    Last modified:June 10, 2008 - v1
    Checksum:iAE90461FA631BED3
    GO
    Isoform Replicase polyprotein 1a (identifier: P0C6V0-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1a, ORF1a polyprotein

    The sequence of this isoform can be found in the external entry P0C6V0.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by conventional translation.

    Length:4,468
    Mass (Da):496,341
    GO

    Sequence cautioni

    The sequence AAB86818.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence AAB86820.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAA36202.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti287 – 2882WR → CA(PubMed:2545027)Curated
    Sequence conflicti311 – 3111L → V(PubMed:2545027)Curated
    Sequence conflicti570 – 5701D → G(PubMed:2545027)Curated
    Sequence conflicti3620 – 36201E → EL(PubMed:9426441)Curated
    Sequence conflicti3711 – 37111T → TL(PubMed:9426441)Curated
    Sequence conflicti3968 – 39681M → V(PubMed:9426441)Curated
    Sequence conflicti4464 – 44641I → V(PubMed:9426441)Curated
    Sequence conflicti6156 – 61561V → A(PubMed:9426441)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1699 – 16991P → S in strain: Isolate C12 mutant.
    Natural varianti2196 – 21961M → K in strain: Isolate C12 mutant.
    Natural varianti5773 – 57731R → S in strain: Isolate C12 mutant.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51939 Genomic RNA. Translation: CAA36202.1. Sequence problems.
    X73559 Genomic RNA. No translation available.
    AF029248 Genomic RNA. Translation: AAB86818.1. Sequence problems.
    AF029248 Genomic RNA. Translation: AAB86820.1. Sequence problems.
    M27198 Genomic RNA. Translation: AAA74011.1.
    PIRiA32440.
    S15760.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51939 Genomic RNA. Translation: CAA36202.1 . Sequence problems.
    X73559 Genomic RNA. No translation available.
    AF029248 Genomic RNA. Translation: AAB86818.1 . Sequence problems.
    AF029248 Genomic RNA. Translation: AAB86820.1 . Sequence problems.
    M27198 Genomic RNA. Translation: AAA74011.1 .
    PIRi A32440.
    S15760.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GTH X-ray 2.70 A 6504-6872 [» ]
    2GTI X-ray 2.15 A 6504-6872 [» ]
    3VC8 X-ray 2.00 A/B 3245-3333 [» ]
    3VCB X-ray 2.40 A/B 3245-3333 [» ]
    ProteinModelPortali P0C6X9.
    SMRi P0C6X9. Positions 4049-4199, 4323-4447, 6504-6872.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P0C6X9.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR027351. (+)RNA_virus_helicase_core_dom.
    IPR022570. Coronavirus_NSP1.
    IPR009461. Coronavirus_NSP16.
    IPR027352. CV_MBD_dom.
    IPR002589. Macro_dom.
    IPR009466. NSP11.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR027417. P-loop_NTPase.
    IPR002705. Pept_C30/C16_B_coronavir.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009469. RNA_pol_N_coronovir.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view ]
    Pfami PF06478. Corona_RPol_N. 1 hit.
    PF11963. DUF3477. 2 hits.
    PF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF06471. NSP11. 1 hit.
    PF06460. NSP13. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF01831. Peptidase_C16. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF00680. RdRP_1. 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.
    SSF52540. SSF52540. 1 hit.
    SSF53335. SSF53335. 2 hits.
    PROSITEi PS51653. CV_MBD. 1 hit.
    PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 2 hits.
    PS51657. PSRV_HELICASE. 1 hit.
    PS50507. RDRP_SSRNA_POS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure and expression of the second open reading frame of the polymerase gene of the coronavirus MHV-A59; a highly conserved polymerase is expressed by an efficient ribosomal frameshifting mechanism."
      Bredenbeek P.J., Pachuk C.J., Noten A.F.H., Charite J., Luytjes W., Weiss S.R., Spaan W.J.M.
      Nucleic Acids Res. 18:1825-1832(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] (ORF1B).
    2. "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: NUCLEOTIDE SEQUENCE [GENOMIC RNA] (ORF1A).
    3. "Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is associated with a Q159L amino acid substitution in the spike protein."
      Leparc-Goffart I., Hingley S.T., Chua M.M., Jiang X., Lavi E., Weiss S.R.
      Virology 239:1-10(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate C12 mutant.
    4. "Molecular cloning of the gene encoding the putative polymerase of mouse hepatitis coronavirus, strain A59."
      Pachuk C.J., Bredenbeek P.J., Zoltick P.W., Spaan W.J.M., Weiss S.R.
      Virology 171:141-148(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-597.
    5. "Mouse hepatitis virus 3C-like protease cleaves a 22-kilodalton protein from the open reading frame 1a polyprotein in virus-infected cells and in vitro."
      Lu X.T., Sims A.C., Denison M.R.
      J. Virol. 72:2265-2271(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, CHARACTERIZATION OF NSP8.
    6. "The putative helicase of the coronavirus mouse hepatitis virus is processed from the replicase gene polyprotein and localizes in complexes that are active in viral RNA synthesis."
      Denison M.R., Spaan W.J.M., van der Meer Y., Gibson C.A., Sims A.C., Prentice E., Lu X.T.
      J. Virol. 73:6862-6871(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION OF HELICASE.
    7. "Further requirements for cleavage by the murine coronavirus 3C-like proteinase: identification of a cleavage site within ORF1b."
      Pinon J.D., Teng H., Weiss S.R.
      Virology 263:471-484(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF PHE-3331; LEU-3332; GLN-3333; SER-3334; GLY-3335; ILE-3336; CYS-3478; LEU-5381; GLN-5382 AND SER-5383.
    8. "Four proteins processed from the replicase gene polyprotein of mouse hepatitis virus colocalize in the cell periphery and adjacent to sites of virion assembly."
      Bost A.G., Carnahan R.H., Lu X.T., Denison M.R.
      J. Virol. 74:3379-3387(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, CHARACTERIZATION OF NSP7; NSP9 AND NSP10.

    Entry informationi

    Entry nameiR1AB_CVMA5
    AccessioniPrimary (citable) accession number: P0C6X9
    Secondary accession number(s): O39225
    , O39226, P16342, P19750
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 54 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3