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P0C6W4

- R1AB_BCHK5

UniProt

P0C6W4 - R1AB_BCHK5

Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Bat coronavirus HKU5 (BtCoV) (BtCoV/HKU5/2004)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (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.By similarity
    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
    The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Its ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G). Activity of helicase is dependent on magnesium 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
    Sitei195 – 1962CleavageSequence Analysis
    Sitei851 – 8522Cleavage; by PL-PROSequence Analysis
    Active sitei1668 – 16681For PL-PRO activityPROSITE-ProRule annotation
    Active sitei1838 – 18381For PL-PRO activityPROSITE-ProRule annotation
    Sitei2830 – 28312Cleavage; by PL-PROSequence Analysis
    Sitei3338 – 33392Cleavage; by 3CL-PROSequence Analysis
    Active sitei3379 – 33791For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3486 – 34861For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3644 – 36452Cleavage; by 3CL-PROSequence Analysis
    Sitei3936 – 39372Cleavage; by 3CL-PROSequence Analysis
    Sitei4019 – 40202Cleavage; by 3CL-PROSequence Analysis
    Sitei4218 – 42192Cleavage; by 3CL-PROSequence Analysis
    Sitei4328 – 43292Cleavage; by 3CL-PROSequence Analysis
    Sitei4467 – 44682Cleavage; by 3CL-PROSequence Analysis
    Sitei5401 – 54022Cleavage; by 3CL-PROSequence Analysis
    Sitei5999 – 60002Cleavage; by 3CL-PROSequence Analysis
    Sitei6523 – 65242Cleavage; by 3CL-PROSequence Analysis
    Sitei6874 – 68752Cleavage; by 3CL-PROSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1748 – 178538C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4402 – 441817By similarityAdd
    BLAST
    Zinc fingeri4444 – 445714By similarityAdd
    BLAST
    Nucleotide bindingi5683 – 56908ATPBy 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):
    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
    RNA-directed RNA polymerase (EC:2.7.7.48)
    Short name:
    Pol
    Short name:
    RdRp
    Alternative name(s):
    nsp12
    Helicase (EC:3.6.4.12, EC:3.6.4.13)
    Short name:
    Hel
    Alternative name(s):
    nsp13
    Exoribonuclease (EC:3.1.13.-)
    Short name:
    ExoN
    Alternative name(s):
    nsp14
    Alternative name(s):
    NendoU
    nsp15
    Alternative name(s):
    nsp16
    Gene namesi
    Name:rep
    ORF Names:1a-1b
    OrganismiBat coronavirus HKU5 (BtCoV) (BtCoV/HKU5/2004)
    Taxonomic identifieri694008 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
    Virus hostiPipistrellus abramus (Japanese pipistrelle) (Pipistrellus javanicus abramus) [TaxID: 105295]
    ProteomesiUP000007451: 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
    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.By similarity

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 195195Non-structural protein 1Sequence AnalysisPRO_0000290303Add
    BLAST
    Chaini196 – 851656Non-structural protein 2Sequence AnalysisPRO_0000290304Add
    BLAST
    Chaini852 – 28301979Non-structural protein 3Sequence AnalysisPRO_0000290305Add
    BLAST
    Chaini2831 – 3338508Non-structural protein 4Sequence AnalysisPRO_0000290306Add
    BLAST
    Chaini3339 – 36443063C-like proteinaseSequence AnalysisPRO_0000290307Add
    BLAST
    Chaini3645 – 3936292Non-structural protein 6Sequence AnalysisPRO_0000290308Add
    BLAST
    Chaini3937 – 401983Non-structural protein 7Sequence AnalysisPRO_0000290309Add
    BLAST
    Chaini4020 – 4218199Non-structural protein 8Sequence AnalysisPRO_0000290310Add
    BLAST
    Chaini4219 – 4328110Non-structural protein 9Sequence AnalysisPRO_0000290311Add
    BLAST
    Chaini4329 – 4467139Non-structural protein 10Sequence AnalysisPRO_0000290312Add
    BLAST
    Chaini4468 – 5401934RNA-directed RNA polymeraseSequence AnalysisPRO_0000290313Add
    BLAST
    Chaini5402 – 5999598HelicaseSequence AnalysisPRO_0000290314Add
    BLAST
    Chaini6000 – 6523524ExoribonucleaseSequence AnalysisPRO_0000290315Add
    BLAST
    Chaini6524 – 6874351Uridylate-specific endoribonucleaseSequence AnalysisPRO_0000290316Add
    BLAST
    Chaini6875 – 7182308Putative 2'-O-methyl transferaseSequence AnalysisPRO_0000290317Add
    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

    Proteomic databases

    PRIDEiP0C6W4.

    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

    ProteinModelPortaliP0C6W4.
    SMRiP0C6W4. Positions 3937-4007, 4268-4328, 4335-4459.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2158 – 217821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2196 – 221621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2268 – 228821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2372 – 239221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2396 – 241621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2421 – 244121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2848 – 286821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3119 – 313921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3152 – 317221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3203 – 322321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3650 – 367021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3684 – 370421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3709 – 372921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3760 – 377718HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3782 – 380221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3823 – 384321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3855 – 387521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1186 – 1345160MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1628 – 1902275Peptidase C16PROSITE-ProRule annotationAdd
    BLAST
    Domaini3339 – 3644306Peptidase C30PROSITE-ProRule annotationAdd
    BLAST
    Domaini5081 – 5243163RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini5402 – 548584CV MBDAdd
    BLAST
    Domaini5658 – 5839182(+)RNA virus helicase ATP-bindingAdd
    BLAST
    Domaini5840 – 6014175(+)RNA virus helicase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2158 – 2441284HD1By similarityAdd
    BLAST
    Regioni2848 – 3223376HD2By similarityAdd
    BLAST
    Regioni3650 – 3875226HD3By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi964 – 1066103Glu-richAdd
    BLAST
    Compositional biasi5406 – 543126Cys-richAdd
    BLAST

    Domaini

    The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane.By similarity

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1748 – 178538C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4402 – 441817By similarityAdd
    BLAST
    Zinc fingeri4444 – 445714By 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.
    IPR009461. Coronavirus_NSP16.
    IPR027352. CV_MBD_dom.
    IPR002589. Macro_dom.
    IPR009466. NSP11.
    IPR024375. Nsp3_coronavir.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR027417. P-loop_NTPase.
    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.
    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.
    PF05409. Peptidase_C30. 1 hit.
    PF00680. RdRP_1. 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.
    SSF52540. SSF52540. 1 hit.
    SSF53335. SSF53335. 1 hit.
    PROSITEiPS51653. CV_MBD. 1 hit.
    PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 1 hit.
    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: P0C6W4-1) [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.

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    MSFVAGVAPQ GARGKYRAEL NTEKRTDHVS LKASLCDAGD LVLKISPWFM     50
    DGESAYKHVS EQLSKGSKLL FVPQTLKGFI RHLPGPRVYL VERLTGGTYS 100
    DPFMVNQLAY QNAAGEGVIG TTLQGKRVGM FFPFDADLVT GEFQFLLRKK 150
    GFGGNRFRDA PWDYNWTPYS DLMDALEADP CGKYSQSLLK KLVGGDFTPI 200
    DQYMCGKNGK PIAEFAALMA SEGITKLADV EAEVKSRTDS DRYIVFKNKL 250
    YRIVWNVQRK DVAYSKQSAF TMNSIVQLDT MEDVPRHSFT IGSEIQVIAP 300
    STAVQANGHL NLKQRLLYAF YGKQAVSEPN YIYHSAYVDC TSCGKGSWLT 350
    GNAVQGFACD CGAHYCANDV DLQSSGLVRK NAVLLTTCPC NKDGECKHTL 400
    PQLVSMMTDK CDVEVVGKTF ILTYGGVIYA YMGCSGGTMH FIPRAKSCVS 450
    KIGDAIFTGC TGTWSKVCET ANLFLERAQH AINFVNEFVL TETVVALLSG 500
    TTSSIEELRD LCRNATFEKV RDYLTPRGWI VTMGSYIEGV INVGAAGVCN 550
    AALNAPFIVL SGLGESFKKV AATPWKLCSS LRETLDHYAD SITYRVFPYD 600
    IPCDVTDYTA LLLDCAVLTG ASAYFVARYV DEKVEQLTNL VFSSCQSAVA 650
    AFVQACMSTY KATAKFISDM FTLIKVVSER LYVYTSVGFV VVGDYSSQLL 700
    KQFMHILSKA MQLLHTTVSW AGSKLPSVVY NGRDSLVFPS GTYYCVSTQG 750
    RSLQDQFDLV IPGDLSKKQI GILEPTPNST TVDKKINTNV VEVVVGQLEP 800
    TKEHSPELVV GDYVIISNKI FVRSVEDSET VFYPLCTDGK IVPTLFRLKG 850
    GAPPKGVKFG GEQTKEITAV RSVSVDYDVH PVLDALLAGS ELATFTVEKD 900
    LPVKDFVDVV KDEVIELLSK LLRGYNVDGF DLEDFADTPC YVYNAEGDLA 950
    WSSTMTFSVN PVEEVEEECD DDYVEDEYLS EEMLVEEDEN SWAAAVEAVI 1000
    PMEDVQLDTL VAEIDVSEPA DDVAEQASTE EVEVPSACVL EASQVANAAE 1050
    VESCEAEVSS SIPLHEDANA AKANDCAEGM PALDSTETVS KLSVDTPVGD 1100
    VTQDDATSSN ATVISEDVHT ATHSKGLVAV PEVVPEKALG TSVERMRSTS 1150
    EWTVVETSLK QETAVIVKND SSAKPQRVKK PKAENPLKNF KHIVLNNDVT 1200
    LVFGDAIAVA RATEDCILVN AANTHLKHGG GIAAAIDRAS GGLVQAESDD 1250
    YVNFYGPLNV GDSTLLKGHG LATGILHVVG PDARANQDIQ LLKRCYKAFN 1300
    KYPLVVSPLI SAGIFCVEPR VSLEYLLSVV HTKTYVVVNS EKVYNDLAAP 1350
    KPPTGLTYSH EGWRGIIRNA KSFGFTCFIC TDQSANAKLL KGRGVDLTKK 1400
    TQTVDGVKYY LYSSKDPLTD IITAANACKG ICAMPIGYVT HGLDLAQAGQ 1450
    QVKKITVPYV CLLASKDQVP ILNSDVAVQT PEQSFINTVI ANGGYHCWHL 1500
    VTGELIVKGV SYRKLLNWSD QTICYADNKF YVVKGQIALP FDSLEKCRTY 1550
    LTSRAAQQKN VDVLVTIDGV NFRTVVLNNT TTYRVQLGSV FYKGSDISDT 1600
    IPTEKMSGEA VYLADNLSEA EKAVLSEVYG TADTAFLHRY YSLLALVKKW 1650
    KYTVHDGVKS LKLNSNNCYV NVTMLMLDML KEIKFIVPAL QAAYLKHKGG 1700
    DSTEFIALIM AYGDCTYGEP DDASRLLHTI LSKAELTTQA KMVWRQWCNV 1750
    CGVQDTTTTG LKACIYVGMN SLDELHATHE ECCQCGDVRK RQLVEHNAPW 1800
    LLLSGLNEAK VMTPTSQSAG PDYTAFNVFQ GVETSVGHYL HVRVKDNLLY 1850
    KYDSGSLSKT SDMKCKMTDV YYPKQRYSAD CNVVVYSLDG NTWADVDPDL 1900
    SAFYMKDGKY FTKKPVIEYS PATILSGSVY TNSCLVGHDG TIGSDAISSS 1950
    FNNLLGFDNS KPVSKKLTYS FFPDFEGDVI LTEYSTYDPI YKNGAMLHGK 2000
    PILWVNNSKF DSALNKFNRA TLRQVYDIAP VTLENKYTVL QDNQIQQVEV 2050
    EAPKEDAKPQ SPVQVAEDID NKLPIIKCKG LKKPFVKDGY SFVNDPQGVN 2100
    VIDTLGIDDL RALYVDRNLR LIVLKENNWS ALFNIHTVEK GDLSVIAASG 2150
    SITRRVKILL GASSLFAQFA SVTVNVTTAM GKALGRMTRN VITNTGIIGQ 2200
    GFALLKMLLI LPFTFWKSKN QSTVKVEVGA LRTAGIVTTN VVKQCASAAY 2250
    DVLVVKFKRI DWKSTLRLLF LICTTGLLLS SLYYLFLFHQ VLTSDVMLDG 2300
    AEGMLATYRE LRSYLGIHSL CDGMVEAYRN VSYDVNDFCS NRSALCNWCL 2350
    IGQDSLTRYS AFQMIQTHVT SYVINIDWVW FVMEFALAYV LYTSTFNVLL 2400
    LVVSSQYFFS YTGAFVNWRS YNYLVSGYFF CVTHIPLLGL VRIYNFLACL 2450
    WFLRRFYNHV INGCKDTACL LCYKRNRLTR VEASTVVCGS KRTFYIVANG 2500
    GTSFCCRHNW NCVDCDTAGI GNTFICEEVA NDLTTSLRRL VKPTDKSHYY 2550
    VESVTVKDSV VQLHYSREGA SCYERYPLCY FTNLDKLKFK EVCKTPTGIP 2600
    EHNFLIYDSS DRGQENLARS ACVYYSQVLS KPMLLVDSNM VTTVGDSREI 2650
    ASKMLDSYVN SFISLFGVNR DKLDKLVATA RDCVKRGDDF QTVIKTFTDA 2700
    ARGPAGVESD VETSSIVDAL QYAYKHDLQL TTEGFNNYVP SYIKPDSVAT 2750
    ADLGCLIDLN AASVNQTSIR NANGACIWNS SDYMKLSDSL KRQIRIACRK 2800
    CNIPFRLTTS RLRSADNILS VKFSATKLSG GAPKWLLKLR DFTWKSYCVV 2850
    TLVVFAMAVL SYLCLPAFNM SQVSFHEDRI LTYKVVENGI IRDITPSDTC 2900
    FANKYQSFSK WFNEHYGGLF NNDISCPVTV AVIAGVAGAR VPNLPANVAW 2950
    VGRQIVLFVS RVFASSNNVC YTPTAEIPYE RFSDSGCVLA SECTLFRDAE 3000
    GKINPYCYDP TVLPGASAYD QMKPHVRYDM YDSDMYIKFP EVVFESTLRI 3050
    TKTLATRYCR FGSCEDANEG VCITTNGSWA IYNDHYANKP GVYCGDNYFD 3100
    IVRRLGLSLF QPVTYFQLST SLALGVMLCI FLTIAFYYVN KVKRALADYT 3150
    QCAVVAVAAA LLNSLCLCFV VSNPLLVLPY TALYYYATFY LTGEPAFVMH 3200
    VSWFVMFGTV VPIWMVFAYI VGVCLRHLLW VMAYFSKKHV EVFTDGKLNC 3250
    SFQDAAANIF VINKDTYVAL RNSITQDSYN RYLSMFNKYK YYSGAMDTAS 3300
    YREASAAHLC KALQVYSETG SDVLFQPPNC SVTSSVLQSG LVKMAAPSGV 3350
    VENCMVQVTC GSMTLNGLWL DNYVWCPRHV MCPADQLSDP NYDALLVSKT 3400
    NLSFIVQKNV GAPANLRVVG HTMVGTLLKL TVESANPQTP AYTFTTVKPG 3450
    ASFSVLACYN GRPTGVFMVN MRQNSTIKGS FLCGSCGSVG YTQEGNVINF 3500
    CYMHQMELSN GTHTGCAFDG VMYGAFEDRQ VHQVQLSDKY CTINIVAWLY 3550
    AAILNGCNWF VKPNKTGIAT FNEWAMSNQF TEFIGTQSVD MLAHKTGVSV 3600
    EQLLYAIQTL HKGFQGKTIL GNSMLEDEFT PDDVNMQVMG VVMQSGVKRI 3650
    SYGLVHWLFT TLLLAYVATL QLTKFTIWNY LFEVIPLQLT PLVLCVMACV 3700
    MLTVKHKHTF LTLFLLPTAI CLTYANIVYE PQTPVSSALI AVANWLNPAS 3750
    VYMRTTHTDL GVYLSLCFAL AVVVRRLYRP NASNLALALG SAMVWFYTYT 3800
    TGDCSSPLTY LMFLTTLTSD YTVTVFLAVN VAKFFARVVF LYAPHAGFIF 3850
    PEVKLVLLMY LAVGYFCTVY FGVFSLLNLK LRVPLGVYDY TVSTQEFRYL 3900
    TGNGLHAPRN SWEALRLNMK LIGIGGTPCI KIASVQSKLT DLKCTSVVLL 3950
    SVLQQLHLEA NSKAWAHCVK LHNDILAATD PTEAFDNFVC LFATLMSFSA 4000
    NVDLEALASD LLDHPSVLQA TLSEFSHLAS YAELEAAQSS YQKALNSGDA 4050
    SPQVLKALQK AVNIAKNAYE KDKAVARKLE RMAEQAMTSM YKQARAEDKK 4100
    AKIVSAMQTM LFGMIKKLDN DVLNGVISNA RNGCVPLSVV PLCASNKLRV 4150
    VIPDITIWNK VVTWPSLSYA GALWDISLIN NVDGEVVKSS DVTETNESLT 4200
    WPLVLECTRA ASSAVTLQNN EIRPSGLKTM VVSAGIDHAN CNTSSLAYYE 4250
    PVEGRKMLMG ILSENAHLKW AKVEGRDGFV NIELQPPCKF LIAGPKGPEV 4300
    RYLYFVKNLN NLHRGQLLGH IAATVRLQAG SNTEFAINSS VLSAVTFSVD 4350
    PGKAYLDFVN AGGAPLTNCV KMLTPKTGTG IAVSVKPEAN ADQDTYGGAS 4400
    VCLYCRAHIE HPDVTGVCKF KGKFVQVPLH IRDPVGFCLQ NTPCNVCQFW 4450
    IGHGCNCDAL RGTTIPQSKD SNFLNRVRGS IVNARIEPCA SGLTTDVVFR 4500
    AFDICNYKAK VAGIGKYYKT NTCRFVEVDD EGHRLDSFFV VKRHTMENYE 4550
    LEKRCYDLVK DCDAVAVHDF FIFDVDKVKT PHIVRQRLTE YTMMDLVYAL 4600
    RHFDQNNCEV LKSILVKYGC CDASYFDNKL WFDFVENPNV ISVYHKLGER 4650
    IRQAVLNTVK FCDQMVKSGL VGVLTLDNQD LNGKWYDFGD FVITQPGAGV 4700
    AIVDSYYSYL MPVLSMTNCL AAETHRDCDL TKPLIEWPLL EYDYTDYKIG 4750
    LFEKYFKXWD QQYHPNCVNC TDDRCVLHCA NFNVLFSMTL PGTSFGPIVR 4800
    KIFVDGVPFV ISCGYHYKEL GLVMNMDVSL HRHRLSLKEL MMYAADPAMH 4850
    IASASALWDL RTPCFSVAAL TTGLTFQTVR PGNFNKDFYD FVVSKGFFKE 4900
    GSSVTLRHFF FAQDGHAAIT DYSYYAYNLP TMCDIKQMLF CMEVVDRYFE 4950
    IYDGGCLNAS EVIVNNLDKS AGHPFNKFGK ARVYYESLSY QEQDELFAMT 5000
    KRNVLPTITQ MNLKYAISAK NRARTVAGVS ILSTMTNRQY HQKMLKSMAA 5050
    TRGSTCVIGT TKFYGGWDFM LKTLYKDVDN PHLMGWDYPK CDRAMPNMCR 5100
    IFASLILARK HSTCCTNTDR FYRLANECAQ VLSEYVLCGG GYYVKPGGTS 5150
    SGDATTAYAN SVFNILQATT ANVSALMGAN GNTIVDEEVK DMQFELYVNV 5200
    YRKSQPDPKF VDRYYAFLNK HFSMMILSDD GVVCYNSDYA TKGYIASIQN 5250
    FKETLYYQNN VFMSEAKCWV ETDLKKGPHE FCSQHTLFIK DGDDGYFLPY 5300
    PDPSRILSAG CFVDDIVKTD GTLMVERFVS LAIDAYPLTK HDDPEYQNVF 5350
    WVYLQYIEKL YKDLTGHMLD SYSVMLCGDN SAKFWEESFY RDLYTAPTTL 5400
    QAVGSCVVCH SQTSLRCGTC IRRPFLCCKC CYDHVIATPH KMVLSVSPYV 5450
    CNAPGCDVAD VTKLYLGGMS YFCIDHRPVC SFPLCANGLV FGLYKNMCTG 5500
    SPSVTEFNRL ATCDWTESGD YTLANTTTEP LKLFAAETLR ATEEASKQSY 5550
    AIATIKEIVG ERELLLVWEA GKAKPPLNRN YVFTGYHITK NSKVQLGEYV 5600
    FERIDYSDAV SYKSSTTYKL AVGDIFVLTS HSVATLQAPT IVNQERYVKI 5650
    TGLYPTLTVP EEFANHVANF QKAGFSKFVT VQGPPGTGKS HFAIGLAIYY 5700
    PTARVVYTAC SHAAVDALCE KAFKYLNIAK CSRIIPAKAR VECYDQFKVN 5750
    ETNSQYLFST INALPETSAD ILVVDEVSMC TNYDLSVINA RIKAKHIVYV 5800
    GDPAQLPAPR TLLTRGTLEP ENFNSVTRLM CNLGPDIFLS VCYRCPEEIV 5850
    NTVSALVYNN KLVAKKPASG QCFKILYKGS VTHDASSAIN RPQLNFVKSF 5900
    IAANPNWSKA VFISPYNSQN AVARSVLGLT TQTVDSSQGS EYPYVIFCQT 5950
    ADTAHANNIN RFNVAVTRAQ KGILCVMTSQ ALFDSLEFAE VSLNNYKLQS 6000
    QIVTGLYKDC SRESSGLHPA YAPTYVSVDD KYKTSDELCV NLNVPANVPY 6050
    SRVISRMGFK LDASIPNYPK LFITRDEAIR QVRSWIGFDV EGAHASRNAC 6100
    GTNVPLQLGF STGVNFVVQP VGVVDTEWGS MLTSIAARPP PGEQFKHLVP 6150
    LMNKGAAWPI VRRRIVQMLS DTLDKLSDYC TFVCWAHGFE LTSASYFCKI 6200
    GKEQRCCMCN RRASTYSSPL HSYACWSHSS GYDYVYNPFF VDVQQWGYIG 6250
    NLATNHDRYC SVHQGAHVAS NDAVMTRCLA IHDCFIERVE WDITYPYISH 6300
    EKRLNSCCRA VERNVVRAAL LAGRFERVYD IGNPKGIPIV DDPVVDWHYY 6350
    DAQPLSKKVQ QLFYTEDCAK NFSDGLCLFW NCNVPRYPNN AIVCRFDTRV 6400
    HSEFNLPGCD GGSLYVNKHA FHTPAYDASA FRDLKPLPFF YYSTTPCEVH 6450
    GNGNMLEDID YVPLKSAVCI TACNLGGAVC RKHAAEYRDY MEAYNLVSAS 6500
    GFRLWCYKTF DVYNLWSTFT KIQGLENIAY NVIKQGHFTG VEGELPVAVV 6550
    NDKIYTKSDV NDVCIFENKT TLPTNIAFEL YAKRAVRSHP DFNLLRNLEV 6600
    DVCYKFVLWD YERSNIYGSA TIGVCKYTDI DVNSALNICF DIRDNGSLER 6650
    FMSLPNGILI SDRKVKNYPC IVSSNYAYFN GTLIRDNTGN SQSSDGEVKQ 6700
    PVTFYIYKKV NNEFVQFTDT YYTLGRTVSD FTPVSEMEKD FLALDSDVFI 6750
    KKYKLEAYAF EHVVYGDFSR TTLGGLHLLI GLYKKHQEGH IIMEEMLKER 6800
    ATVHNYFVTE SNTASFKAVC SVIDLKLDDF VDIIKAMDLS VVSKVVKIPI 6850
    DLTMIEFMLW CKDGQVQTFY PRLQAINDWK PGLAMPSLFK VQNSNLEPCM 6900
    LPNYKQSIPM PQGVHMNIAK YMQLCQYLNT CTIAVPANMR VMHFGAGSDK 6950
    GVAPGSSVLR QWLPTDAILI DNDLNEYVSD ADITLFGDCV TVRVGQQVDL 7000
    LISDMYDPST KVVGETNEAK ALFFVYLCNF IKNNLALGGS VAIKITEHSW 7050
    SAELYELMGR FAWWTVFCTN ANASSSEGFL IGINYLGELK EVIDGNVMHA 7100
    NYIFWRNTTL MNLSTYSLFD LSRFPLKLKG TPVLQLKESQ INELVISLLS 7150
    QGKLIIRDND TLSVSTDVLV NFYRKPHKRS KC 7182

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

    Length:7,182
    Mass (Da):799,932
    Last modified:June 10, 2008 - v1
    Checksum:i455E36D8EF6FD1E1
    GO
    Isoform Replicase polyprotein 1a (identifier: P0C6T5-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1a, ORF1a polyprotein

    The sequence of this isoform can be found in the external entry P0C6T5.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by conventional translation.

    Length:4,481
    Mass (Da):494,801
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF065509 Genomic RNA. Translation: ABN10874.1.
    RefSeqiYP_001039961.1. NC_009020.1. [P0C6W4-1]

    Genome annotation databases

    GeneIDi4836003.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF065509 Genomic RNA. Translation: ABN10874.1 .
    RefSeqi YP_001039961.1. NC_009020.1. [P0C6W4-1 ]

    3D structure databases

    ProteinModelPortali P0C6W4.
    SMRi P0C6W4. Positions 3937-4007, 4268-4328, 4335-4459.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P0C6W4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4836003.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR027351. (+)RNA_virus_helicase_core_dom.
    IPR009461. Coronavirus_NSP16.
    IPR027352. CV_MBD_dom.
    IPR002589. Macro_dom.
    IPR009466. NSP11.
    IPR024375. Nsp3_coronavir.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR027417. P-loop_NTPase.
    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.
    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.
    PF05409. Peptidase_C30. 1 hit.
    PF00680. RdRP_1. 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.
    SSF52540. SSF52540. 1 hit.
    SSF53335. SSF53335. 1 hit.
    PROSITEi PS51653. CV_MBD. 1 hit.
    PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 1 hit.
    PS51657. PSRV_HELICASE. 1 hit.
    PS50507. RDRP_SSRNA_POS. 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 HKU5-1.

    Entry informationi

    Entry nameiR1AB_BCHK5
    AccessioniPrimary (citable) accession number: P0C6W4
    Secondary accession number(s): A3EXC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 57 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