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P0C6W5

- R1AB_BCHK9

UniProt

P0C6W5 - R1AB_BCHK9

Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Bat coronavirus HKU9 (BtCoV) (BtCoV/HKU9)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (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.1 Publication

    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
    Sitei175 – 1762CleavageSequence Analysis
    Sitei772 – 7732Cleavage; by PL-PROSequence Analysis
    Active sitei1533 – 15331For PL-PRO activityPROSITE-ProRule annotation
    Active sitei1694 – 16941For PL-PRO activityPROSITE-ProRule annotation
    Sitei2609 – 26102Cleavage; by PL-PROSequence Analysis
    Sitei3103 – 31042Cleavage; by 3CL-PROSequence Analysis
    Active sitei3144 – 31441For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3248 – 32481For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3409 – 34102Cleavage; by 3CL-PROSequence Analysis
    Sitei3699 – 37002Cleavage; by 3CL-PROSequence Analysis
    Sitei3782 – 37832Cleavage; by 3CL-PROSequence Analysis
    Sitei3982 – 39832Cleavage; by 3CL-PROSequence Analysis
    Sitei4094 – 40952Cleavage; by 3CL-PROSequence Analysis
    Sitei4233 – 42342Cleavage; by 3CL-PROSequence Analysis
    Sitei5165 – 51662Cleavage; by 3CL-PROSequence Analysis
    Sitei5766 – 57672Cleavage; by 3CL-PROSequence Analysis
    Sitei6296 – 62972Cleavage; by 3CL-PROSequence Analysis
    Sitei6633 – 66342Cleavage; by 3CL-PROSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1610 – 164738C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4168 – 418417By similarityAdd
    BLAST
    Zinc fingeri4211 – 422414By similarityAdd
    BLAST
    Nucleotide bindingi5447 – 54548ATPSequence Analysis

    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 HKU9 (BtCoV) (BtCoV/HKU9)
    Taxonomic identifieri694006 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
    Virus hostiRousettus leschenaultii (Leschenault's rousette) [TaxID: 9408]
    ProteomesiUP000006576: Genome

    Subcellular locationi

    Chain Non-structural protein 7 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity
    Chain Non-structural protein 8 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity
    Chain Non-structural protein 9 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity
    Chain Non-structural protein 10 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity
    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 – 175175Non-structural protein 1Sequence AnalysisPRO_0000291350Add
    BLAST
    Chaini176 – 772597Non-structural protein 2Sequence AnalysisPRO_0000291351Add
    BLAST
    Chaini773 – 26091837Non-structural protein 3Sequence AnalysisPRO_0000291352Add
    BLAST
    Chaini2610 – 3103494Non-structural protein 4Sequence AnalysisPRO_0000291353Add
    BLAST
    Chaini3104 – 34093063C-like proteinaseSequence AnalysisPRO_0000291354Add
    BLAST
    Chaini3410 – 3699290Non-structural protein 6Sequence AnalysisPRO_0000291355Add
    BLAST
    Chaini3700 – 378283Non-structural protein 7Sequence AnalysisPRO_0000291356Add
    BLAST
    Chaini3783 – 3982200Non-structural protein 8Sequence AnalysisPRO_0000291357Add
    BLAST
    Chaini3983 – 4094112Non-structural protein 9Sequence AnalysisPRO_0000291358Add
    BLAST
    Chaini4095 – 4233139Non-structural protein 10Sequence AnalysisPRO_0000291359Add
    BLAST
    Chaini4234 – 5165932RNA-directed RNA polymeraseSequence AnalysisPRO_0000291360Add
    BLAST
    Chaini5166 – 5766601HelicaseSequence AnalysisPRO_0000291361Add
    BLAST
    Chaini5767 – 6296530ExoribonucleaseSequence AnalysisPRO_0000291362Add
    BLAST
    Chaini6297 – 6633337Uridylate-specific endoribonucleaseSequence AnalysisPRO_0000291363Add
    BLAST
    Chaini6634 – 6930297Putative 2'-O-methyl transferaseSequence AnalysisPRO_0000291364Add
    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

    PRIDEiP0C6W5.

    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

    ProteinModelPortaliP0C6W5.
    SMRiP0C6W5. Positions 934-1096, 3106-3403, 3699-3782, 3820-3972, 3985-4094, 4104-4224.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2015 – 203521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2040 – 206021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2081 – 210121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2162 – 218221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2183 – 220321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2218 – 223821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2621 – 264121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2719 – 273921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2865 – 288521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2887 – 290721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2916 – 293621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2946 – 296621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2970 – 299021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3423 – 344321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3449 – 346921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3474 – 349421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3517 – 353721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3569 – 358921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3592 – 361221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3620 – 364021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini930 – 1097168MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1492 – 1757266Peptidase C16PROSITE-ProRule annotationAdd
    BLAST
    Domaini3104 – 3409306Peptidase C30PROSITE-ProRule annotationAdd
    BLAST
    Domaini4845 – 5007163RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini5166 – 524984CV MBDAdd
    BLAST
    Domaini5412 – 5603192(+)RNA virus helicase ATP-bindingAdd
    BLAST
    Domaini5604 – 5778175(+)RNA virus helicase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2015 – 2238224HD1By similarityAdd
    BLAST
    Regioni2621 – 2990370HD2By similarityAdd
    BLAST
    Regioni3423 – 3640218HD3By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi5170 – 519526Cys-richAdd
    BLAST
    Compositional biasi6832 – 68354Poly-Ser

    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 fingeri1610 – 164738C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4168 – 418417By similarityAdd
    BLAST
    Zinc fingeri4211 – 422414By similarityAdd
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    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.
    PF01443. Viral_helicase1. 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: P0C6W5-1) [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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    MEGVPDPPKL KSMVVTTLKW CDPFANPNVT GWDIPIEEAL EYAKQQLRTP     50
    EPQLVFVPYY LSHAPGISGD RVVITDSIWY ATNFGWQPIR ELAMDKDGVR 100
    YGRGGTHGVL LPMQDPSFIM GDIDIQIRKY GIGANSPPDV LPLWDGFSDP 150
    GPDVGPYLDF PDNCCPTKPK AKRGGDVYLS DQYGFDNNGI LVEPVMKLLG 200
    VIKSDFTLEQ LLAALGKYRT EDGYDLPDGY VKVAIKVGRK AVPVLKQSIF 250
    TVVGVTEQLV PGYYYPFSTS SVVEHTKPTR GGPVGKTVEA VMLSLYGTNN 300
    YNPATPVARL KCSYCDYYGW TPLKDIGTVN CLCGAEFQLT SSCVDAESAG 350
    VIKPGCVMLL DKSPGMRLIP GNRTYVSFGG AIWSPIGKVN GVTVWVPRAY 400
    SIVAGEHSGA VGSGDTVAIN KELVEYLIEG IRVDADTLDN PTCATFIANL 450
    DCDTKAPVVH TVESLQGLCL ANKIMLGDKP LPTDEFHPFI VGLAYHVQRA 500
    CWYGALASRT FEAFRDFVRT EEERFAQFFG KVCAPINGCV YLAYTTGRVT 550
    LFSAYQVLNT AIAKSKDAFG GVAAIVVDML KPILEWVLKK MSIAKGAWLP 600
    YAEGLLALFK AQFTVVKGKF QFLRASLNSK CHSLCDLLTT IMSKLLTSVK 650
    WAGCKVDALY TGTYYYFSRK GVLTEVQLCA KRLGLLLTPK QQKMEVEVLD 700
    GDFDAPVTLT DLELEECTGV LEEVFGASDV KLVKGTLVSL ASKLFVRTED 750
    GFLYRYVKSG GVLGKAFRLR GGGVSKVTFG DEEVHTIPNT VTVNFSYDVC 800
    EGLDAILDKV MAPFQVEEGT KLEDLACVVQ KAVYERLSDL FSDCPAELRP 850
    INLEDFLTSE CFVYSKDYEK ILMPEMYFSL EDAVPVDDEM VDDIEDTVEQ 900
    ASDSDDQWLG DEGAEDCDNT IQDVDVATSM TTPCGYTKIA EHVYIKCADI 950
    VQEARNYSYA VLVNAANVNL HHGGGVAGAL NRATNNAMQK ESSEYIKANG 1000
    SLQPGGHVLL SSHGLASHGI LHVVGPDKRL GQDLALLDAV YAAYTGFDSV 1050
    LTPLVSAGIF GFTVEESLCS LVKNVACTTY VVVYDRQLYE RALATSFDVP 1100
    GPQSSVQHVP AIDWAEAVEV QESIVDQVET PSLGAVDTVD SNADSGLNET 1150
    ARSPENVVGS VPDDVVADVE SCVRDLVRQV VKKVKRDKRP PPIVPQQTVE 1200
    QQPQEISSPG DCNTVLVDVV SMSFSAMVNF GKEKGLLIPV VIDYPAFLKV 1250
    LKRFSPKEGL FSSNGYEFYG YSRDKPLHEV SKDLNSLGRP LIMIPFGFIV 1300
    NGQTLAVSAV SMRGLTVPHT VVVPSESSVP LYRAYFNGVF SGDTTAVQDF 1350
    VVDILLNGAR DWDVLQTTCT VDRKVYKTIC KRGNTYLCFD DTNLYAITGD 1400
    VVLKFATVSK ARAYLETKLC APEPLIKVLT TVDGINYSTV LVSTAQSYRA 1450
    QIGTVFCDGH DWSNKNPMPT DEGTHLYKQD NFSSAEVTAI REYYGVDDSN 1500
    IIARAMSIRK TVQTWPYTVV DGRVLLAQRD SNCYLNVAIS LLQDIDVSFS 1550
    TPWVCRAYDA LKGGNPLPMA EVLIALGKAT PGVSDDAHMV LSAVLNHGTV 1600
    TARRVMQTVC EHCGVSQMVF TGTDACTFYG SVVLDDLYAP VSVVCQCGRP 1650
    AIRYVSEQKS PWLLMSCTPT QVPLDTSGIW KTAIVFRGPV TAGHYMYAVN 1700
    GTLISVYDAN TRRRTSDLKL PATDILYGPT SFTSDSKVET YYLDGVKRTT 1750
    IDPDFSKYVK RGDYYFTTAP IEVVAAPKLV TSYDGFYLSS CQNPQLAESF 1800
    NKAINATKTG PMKLLTMYPN VAGDVVAISD DNVVAHPYGS LHMGKPVLFV 1850
    TRPNTWKKLV PLLSTVVVNT PNTYDVLAVD PLPVNNETSE EPISVKAPIP 1900
    LYGLKATMVL NGTTYVPGNK GHLLCLKEFT LTDLQTFYVE GVQPFVLLKA 1950
    SHLSKVLGLR VSDSSLHVNH LSKGVVYAYA ATRLTTRVTT SLLGGLVTRS 2000
    VRKTADFVRS TNPGSKCVGL LCLFYQLFMR FWLLVKKPPI VKVSGIIAYN 2050
    TGCGVTTCVL NYLRSRCGNI SWSRLLKLLR YMLYIWFVWT CLTICGVWLS 2100
    EPYAPSLVTR FKYFLGIVMP CDYVLVNETG TGWLHHLCMA GMDSLDYPAL 2150
    RMQQHRYGSP YNYTYILMLL EAFFAYLLYT PALPIVGILA VLHLIVLYLP 2200
    IPLGNSWLVV FLYYIIRLVP FTSMLRMYIV IAFLWLCYKG FLHVRYGCNN 2250
    VACLMCYKKN VAKRIECSTV VNGVKRMFYV NANGGTHFCT KHNWNCVSCD 2300
    TYTVDSTFIC RQVALDLSAQ FKRPIIHTDE AYYEVTSVEV RNGYVYCYFE 2350
    SDGQRSYERF PMDAFTNVSK LHYSELKGAA PAFNVLVFDA TNRIEENAVK 2400
    TAAIYYAQLA CKPILLVDKR MVGVVGDDAT IARAMFEAYA QNYLLKYSIA 2450
    MDKVKHLYST ALQQISSGMT VESVLKVFVG STRAEAKDLE SDVDTNDLVS 2500
    CIRLCHQEGW EWTTDSWNNL VPTYIKQDTL STLEVGQFMT ANAKYVNANI 2550
    AKGAAVNLIW RYADFIKLSE SMRRQLKVAA RKTGLNLLVT TSSLKADVPC 2600
    MVTPFKIIGG HRRIVSWRRV LIHVFMLLVV LNPQWFTPWY IMRPIEYNVV 2650
    DFKVIDNAVI RDITSADQCF ANKFSAFENW YSNRYGSYVN SRGCPMVVGV 2700
    VSDIVGSLVP GLPARFLRVG TTLLPLVNYG LGAVGSVCYT PHYAINYDVF 2750
    DTSACVLAAT CTLFSSASGE RMPYCADAAL IQNASRYDML KPHVMYPFYE 2800
    HSGYIRFPEV ISAGVHIVRT MAMEYCKVGR CDVSEAGLCM SLQPRWVVNN 2850
    AYFRQQSGVY CGTSAFDLFM NMLLPIFTPV GAVDITTSIL MGALLAVVVS 2900
    MSLYYLLRFR RAFGDYSGVI FTNILAFVLN VIVLCLEGPY PMLPSIYAMV 2950
    FLYATCYFGS DIACMMHVSF LIMFAGVVPL WVTVLYIVVV LSRHILWFAS 3000
    LCTKRTVQVG DLAFHSFQDA ALQTFMLDKE VFLRLKREIS SDAYFKYLAM 3050
    YNKYKYYSGP MDTAAYREAA CSHLVMALEK YSNGGGDTIY QPPRCSVASA 3100
    ALQAGLTRMA HPSGLVEPCL VKVNYGSMTL NGIWLDNFVI CPRHVMCSRD 3150
    ELANPDYPRL SMRAANYDFH VSQNGHNIRV IGHTMEGSLL KLTVDVNNPK 3200
    TPAYSFIRVS TGQAMSLLAC YDGLPTGVYT CTLRSNGTMR ASFLCGSCGS 3250
    PGFVMNGKEV QFCYLHQLEL PNGTHTGTDF SGVFYGPFED KQVPQLAAPD 3300
    CTITVNVLAW LYAAVLSGEN WFLTKSSISP AEFNNCAVKY MCQSVTSESL 3350
    QVLQPLAAKT GISVERMLSA LKVLLSAGFC GRTIMGSCSL EDEHTPYDIG 3400
    RQMLGVKLQG KFQSMFRWTL QWFAIIFVLT ILILLQLAQW TFVGALPFTL 3450
    LLPLIGFVAV CVGFVSLLIK HKHTYLTVYL LPVAMVTAYY NFQYTPEGVQ 3500
    GYLLSLYNYV NPGRIDVIGT DLLTMLIISV ACTLLSVRMV RTDAYSRIWY 3550
    VCTAVGWLYN CWTGSADTVA ISYLTFMVSV FTNYTGVACA SLYAAQFMVW 3600
    VLKFLDPTIL LLYGRFRCVL VCYLLVGYLC TCYFGVFNLI NRLFRCTLGN 3650
    YEYVVSSQEL RYMNSHGLLP PTNSWQALML NIKLAGIGGI PIYRVSTIQS 3700
    NMTDLKCTSV VLLSVLQQLR VESSSKLWAL CVKLHNEILA SNSPTEAFEA 3750
    FVSLLSVLLS LPGAINLDEL CSSILENNSV LQAVASEFSN LSSYVDYENA 3800
    QKAYDTAVAT GAPASTVNAL KKAMNVAKSV LDKDVATTRK LERMSELAMT 3850
    AMYKQARAED RRSKVTAAMQ TMLFNMIRRL DSDALSNILN NARNGVVPLG 3900
    VIPRTAANKL LLVVPDFSVY TATITMPTLT YAGSAWDVMQ VADADGKTVN 3950
    ATDITRENSV NLAWPLVVTA QRQQATSPVK LQNNELMPQT VKRMNVVAGV 4000
    SQTACVTDAV AYYNATKEGR HVMAILADTD GLAFAKVEKS TGDGFVILEL 4050
    EPPCKFMVDT PKGPALKYLY FTKGLKNLCR GTVLGTLACT VRLHAGSATE 4100
    VASNSSILSL CSFSVDPEAT YKDYLDNGGS PIGNCVKMLT PHTGTGLAIT 4150
    AKPDANIDQE SFGGASCCLY CRCHIEHPGA SGVCKYKGKF VQIPLVGVND 4200
    PIGFCIRNVV CAVCNMWQGY GCPCSSLREI NLQARDECFL NRVRGTSGVA 4250
    RLVPLGSGVQ PDIVLRAFDI CNTKVAGFGL HLKNNCCRYQ ELDADGTQLD 4300
    SYFVVKRHTE SNYLLEQRCY EKLKDCGVVA RHDFFKFNIE GVMTPHVSRE 4350
    RLTKYTMADL VYSLRHFDNN NCDTLKEILV LRGCCTADYF DRKDWYDPVE 4400
    NPDIIRVYHN LGETVRKAVL SAVKMADSMV EQGLIGVLTL DNQDLNGQWY 4450
    DFGDFIEGPA GAGVAVMDTY YSLAMPVYTM TNMLAAECHV DGDFSKPKRV 4500
    WDICKYDYTQ FKYSLFSKYF KYWDMQYHPN CVACADDRCI LHCANFNILF 4550
    SMVLPNTSFG PLVQKIYVDG VPFVVSTGYH YRELGVVMNQ DIRQHAQRLS 4600
    LRELLVYAAD PAMHVAASNA LADKRTVCMS VAAMTTGVTF QTVKPGQFNE 4650
    DFYNFAVKCG FFKEGSTISF KHFFYAQDGN AAISDYDYYR YNLPTMCDIK 4700
    QLLFSLEVVD KYFDCYDGGC LQASQVVVAN YDKSAGFPFN KFGKARLYYE 4750
    SLSYADQDEL FAYTKRNVLP TITQMNLKYA ISAKNRARTV AGVSIASTMT 4800
    NRQFHQKMLK SIAAARGASV VIGTTKFYGG WNRMLRTLCE GVENPHLMGW 4850
    DYPKCDRAMP NLLRIFASLI LARKHATCCN ASERFYRLAN ECAQVLSEMV 4900
    LCGGGFYVKP GGTSSGDSTT AYANSVFNIC QAVSANLNTF LSIDGNKIYT 4950
    TYVQELQRRL YLGIYRSNTV DNELVLDYYN YLRKHFSMMI LSDDGVVCYN 5000
    ADYAQKGYVA DIQGFKELLY FQNNVFMSES KCWVEPDITK GPHEFCSQHT 5050
    MLVDMKGEQV YLPYPDPSRI LGAGCFVDDL LKTDGTLMME RYVSLAIDAY 5100
    PLTKHPDPEY QNVFWCYLQY IKKLHEELTG HLLDTYSVML ASDNASKYWE 5150
    VEFYENMYME SATLQSVGTC VVCNSQTSLR CGGCIRRPFL CCKCCYDHVV 5200
    STTHKLVLSV TPYVCNNPSC DVADVTQLYL GGMSYYCRDH RPPISFPLCA 5250
    NGQVFGLYKN ICTGSPDVAD FNSLATCDWS NSKDYVLANT ATERLKLFAA 5300
    ETLRATEENA KQAYASAVVK EVLSDRELVL SWETGKTRPP LNRNYVFTGF 5350
    HITKNSKVQL GEYIFEKGDY GDVVNYRSST TYKLQVGDYF VLTSHSVQPL 5400
    SSPTLLPQER YTKLVGLYPA MNVPESFASN VVHYQRVGMS RYTTVQGPPG 5450
    TGKSHLSIGL ALYYPSAKIV YTACSHAAVD ALCEKAHKNL PINRCSRIVP 5500
    AKARVECFSK FKVNDVGAQY VFSTINALPE TTADILVVDE VSMCTNYDLS 5550
    MINARVRAKH IVYVGDPAQL PAPRTLLTKG TLAPEHFNSV CRLMVAVGPD 5600
    IFLATCYRCP KEIVDTVSAL VYDKKLKANK VTTGECYKCY YKGSVTHDSS 5650
    SAINKPQLGL VKEFLIKNPK WQSAVFISPY NSQNSVARRM LGLQTQTVDS 5700
    SQGSEFDYVI YCQTSDTAHA LNVNRFNVAI TRAKKGILCV MSDSTLYESL 5750
    EFTPLDVNDY VKPKMQSEVT VGLFKDCAKA EPLGPAYAPT FVSVNDKFKL 5800
    NESLCVHFDT TELQMPYNRL ISKMGFKFDL NIPGYSKLFI TREQAIREVR 5850
    GWVGFDVEGA HACGPNIGTN LPLQIGFSTG VNFVVTPSGY IDTESGSRLA 5900
    NVVSKAPPGD QFKHLIPLMR KGEPWSVVRK RIVEMLCDTL DGVSDTVTFV 5950
    TWAHGFELTT LHYFAKVGPE RKCFMCPRRA TLFSSVYGAY SCWSHHRHIG 6000
    GADFVYNPFL VDVQQWGYVG NLQVNHDNVC DVHKGAHVAS CDAIMTRCLA 6050
    IHDCFCGEVN WDVEYPIIAN ELAINRACRS VQRVVLKAAV KALHIETIYD 6100
    IGNPKAIKVY GVNVNNWNFY DTNPVVEGVK QLHYVYDVHR DQFKDGLAMF 6150
    WNCNVDCYPH NALVCRFDTR VLSKLNLAGC NGGSLYVNQH AFHTDAFNKN 6200
    AFVNLKPLPF FYYSDTACEN ATGVSTNYVS EVDYVPLKSN VCITRCNLGG 6250
    AVCKKHADEY RNFLESYNTM VSAGFTLWVD KTFDVFNLWS TFVKLQSLEN 6300
    VAYNVLKSGH FTAVAGELPV AILNDRLYIK EDGADKLLFT NNTCLPTNVA 6350
    FELWAKRSVN VVPEVKLLRN LGVTCTYNLV IWDYESNAPL VPNTVGICTY 6400
    TDLTKLDDQV VLVDGRQLDA YSKFCQLKNA IYFSPSKPKC VCTRGPTHAS 6450
    INGVVVEAPD RGTAFWYAMR KDGAFVQPTD GYFTQSRTVD DFQPRTQLEI 6500
    DFLDLEQSCF LDKYDLHDLG LEHIVYGQFD GTIGGLHLLI GAVRRKRTAH 6550
    LVMETVLGTD TVTSYAVIDQ PTASSKQVCS VVDIILDDFI ALIKAQDRSV 6600
    VSKVVQCCLD FKVFRFMLWC KGGKISTFYP QLQAKQDWKP GYSMPALYKV 6650
    QNAVLEPCLL HNYGQAARLP SGTLMNVAKY TQLCQYLNTC SLAVPAKMRV 6700
    MHFGAGSDKG VCPGTAVLKQ WLPADAYLVD NDLCYCASDA DSTYVGSCET 6750
    FFSVNKWDFI FSDMYDARTK NTSGDNTSKE GFFTYLTGFI RSKLALGGSI 6800
    AIKITEHSWS ADLYAIMGHF NWWTCFCTSV NSSSSEAFLI GVNYIGVGAL 6850
    LDGWQMHANY VFWRNSTVMQ LSSYSLYDLQ RFPLRLKGTP VMSLKEDQLN 6900
    ELVLNLIRAG RLIVRDAVDI GVRGVACSGV 6930

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

    Length:6,930
    Mass (Da):769,729
    Last modified:June 10, 2008 - v1
    Checksum:i9ED06D0888C7EC7B
    GO
    Isoform Replicase polyprotein 1a (identifier: P0C6T6-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1a, ORF1a polyprotein

    The sequence of this isoform can be found in the external entry P0C6T6.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by conventional translation.

    Length:4,248
    Mass (Da):468,590
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF065513 Genomic RNA. Translation: ABN10910.1.
    RefSeqiYP_001039970.1. NC_009021.1. [P0C6W5-1]

    Genome annotation databases

    GeneIDi4836014.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF065513 Genomic RNA. Translation: ABN10910.1 .
    RefSeqi YP_001039970.1. NC_009021.1. [P0C6W5-1 ]

    3D structure databases

    ProteinModelPortali P0C6W5.
    SMRi P0C6W5. Positions 934-1096, 3106-3403, 3699-3782, 3820-3972, 3985-4094, 4104-4224.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P0C6W5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4836014.

    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.
    PF01443. Viral_helicase1. 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 HKU9-1.
    2. "Suppression of host gene expression by nsp1 proteins of group 2 bat coronaviruses."
      Tohya Y., Narayanan K., Kamitani W., Huang C., Lokugamage K., Makino S.
      J. Virol. 83:5282-5288(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF NSP1.

    Entry informationi

    Entry nameiR1AB_BCHK9
    AccessioniPrimary (citable) accession number: P0C6W5
    Secondary accession number(s): A3EXG5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 55 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