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P0C6T4

- R1A_BCHK4

UniProt

P0C6T4 - R1A_BCHK4

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Bat coronavirus HKU4 (BtCoV) (BtCoV/HKU4/2004)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    The papain-like proteinase (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
    Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter.By similarity
    Nsp9 is a ssRNA-binding protein.By similarity
    Non-structural protein 1: binds to the 40S ribosomal subunit and inhibits host translation. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response By similarity.By similarity

    Catalytic activityi

    TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei195 – 1962CleavageSequence Analysis
    Sitei847 – 8482Cleavage; by PL-PROSequence Analysis
    Active sitei1634 – 16341For PL-PRO activityPROSITE-ProRule annotation
    Active sitei1800 – 18001For PL-PRO activityPROSITE-ProRule annotation
    Sitei2784 – 27852Cleavage; by PL-PROSequence Analysis
    Sitei3291 – 32922Cleavage; by 3CL-PROSequence Analysis
    Active sitei3332 – 33321For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3439 – 34391For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3597 – 35982Cleavage; by 3CL-PROSequence Analysis
    Sitei3889 – 38902Cleavage; by 3CL-PROSequence Analysis
    Sitei3972 – 39732Cleavage; by 3CL-PROSequence Analysis
    Sitei4171 – 41722Cleavage; by 3CL-PROSequence Analysis
    Sitei4281 – 42822Cleavage; by 3CL-PROSequence Analysis
    Sitei4420 – 44212Cleavage; by 3CL-PROSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1714 – 175138C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4355 – 437117By similarityAdd
    BLAST
    Zinc fingeri4397 – 441014By similarityAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: InterPro
    2. omega peptidase activity Source: InterPro
    3. RNA binding Source: UniProtKB-KW
    4. RNA-directed RNA polymerase activity Source: InterPro
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. induction by virus of catabolism of host mRNA Source: UniProtKB-KW
    2. induction by virus of host autophagy Source: UniProtKB-KW
    3. modulation by virus of host protein ubiquitination Source: UniProtKB-KW
    4. suppression by virus of host IRF3 activity Source: UniProtKB-KW
    5. suppression by virus of host ISG15 activity Source: UniProtKB-KW
    6. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
    7. viral genome replication Source: InterPro
    8. viral protein processing Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Activation of host autophagy by virus, Decay of host mRNAs by virus, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host IRF3 by virus, Inhibition of host ISG15 by virus, Inhibition of host RLR pathway by virus, Modulation of host ubiquitin pathway by viral deubiquitinase, Modulation of host ubiquitin pathway by virus, Ubl conjugation pathway, Viral immunoevasion

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Replicase polyprotein 1a
    Short name:
    pp1a
    Alternative name(s):
    ORF1a polyprotein
    Cleaved into the following 11 chains:
    Non-structural protein 1
    Short name:
    nsp1
    Alternative name(s):
    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
    Non-structural protein 11
    Short name:
    nsp11
    Gene namesi
    ORF Names:1a
    OrganismiBat coronavirus HKU4 (BtCoV) (BtCoV/HKU4/2004)
    Taxonomic identifieri694007 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
    Virus hostiTylonycteris pachypus (Lesser bamboo bat) [TaxID: 258959]
    ProteomesiUP000006574: Genome

    Subcellular locationi

    Chain Non-structural protein 7 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity
    Chain Non-structural protein 8 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity
    Chain Non-structural protein 9 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity
    Chain Non-structural protein 10 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity

    GO - Cellular componenti

    1. host cell membrane Source: UniProtKB-SubCell
    2. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Host cytoplasm, Host membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 44344434Replicase polyprotein 1aPRO_0000338086Add
    BLAST
    Chaini1 – 195195Non-structural protein 1Sequence AnalysisPRO_0000338087Add
    BLAST
    Chaini196 – 847652Non-structural protein 2Sequence AnalysisPRO_0000338088Add
    BLAST
    Chaini848 – 27841937Non-structural protein 3Sequence AnalysisPRO_0000338089Add
    BLAST
    Chaini2785 – 3291507Non-structural protein 4Sequence AnalysisPRO_0000338090Add
    BLAST
    Chaini3292 – 35973063C-like proteinaseSequence AnalysisPRO_0000338091Add
    BLAST
    Chaini3598 – 3889292Non-structural protein 6Sequence AnalysisPRO_0000338092Add
    BLAST
    Chaini3890 – 397283Non-structural protein 7Sequence AnalysisPRO_0000338093Add
    BLAST
    Chaini3973 – 4171199Non-structural protein 8Sequence AnalysisPRO_0000338094Add
    BLAST
    Chaini4172 – 4281110Non-structural protein 9Sequence AnalysisPRO_0000338095Add
    BLAST
    Chaini4281 – 4434154Non-structural protein 11Sequence AnalysisPRO_0000338097Add
    BLAST
    Chaini4282 – 4420139Non-structural protein 10Sequence AnalysisPRO_0000338096Add
    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
    4434
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3302 – 33054
    Beta strandi3308 – 33136
    Beta strandi3316 – 33238
    Beta strandi3326 – 33305
    Helixi3331 – 33344
    Helixi3337 – 33393
    Helixi3345 – 33506
    Helixi3354 – 33563
    Beta strandi3358 – 33603
    Beta strandi3363 – 33653
    Beta strandi3367 – 33693
    Beta strandi3371 – 33777
    Beta strandi3380 – 33878
    Beta strandi3394 – 33974
    Beta strandi3405 – 34128
    Beta strandi3415 – 34239
    Beta strandi3442 – 34476
    Beta strandi3450 – 346213
    Beta strandi3465 – 34695
    Helixi3476 – 34783
    Beta strandi3481 – 34844
    Helixi3495 – 350713
    Helixi3521 – 353010
    Helixi3540 – 354910
    Helixi3553 – 356513
    Beta strandi3575 – 35773
    Helixi3584 – 35918

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YNAX-ray1.50A/B3292-3597[»]
    2YNBX-ray1.96A/B3292-3597[»]
    ProteinModelPortaliP0C6T4.
    SMRiP0C6T4. Positions 3889-3972, 4221-4281, 4291-4411.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2145 – 216521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2222 – 224221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2326 – 234621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2350 – 237021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2375 – 239521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2800 – 282021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3072 – 309221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3105 – 312521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3149 – 316921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3603 – 362321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3637 – 365721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3662 – 368221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3707 – 372721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3735 – 375521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3784 – 380421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3808 – 382821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1152 – 1321170MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1593 – 1864272Peptidase C16PROSITE-ProRule annotationAdd
    BLAST
    Domaini3292 – 3597306Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2112 – 2395284HD1By similarityAdd
    BLAST
    Regioni2800 – 3169370HD2By similarityAdd
    BLAST
    Regioni3603 – 3828226HD3By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi960 – 104990Glu-richAdd
    BLAST
    Compositional biasi4161 – 41666Poly-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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1714 – 175138C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4355 – 437117By similarityAdd
    BLAST
    Zinc fingeri4397 – 441014By similarityAdd
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    InterProiIPR002589. Macro_dom.
    IPR024375. Nsp3_coronavir.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view]
    PfamiPF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF11633. SUD-M. 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.
    PROSITEiPS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 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 1a (identifier: P0C6T4-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1a, ORF1a polyprotein

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLSKASVTTQ GARGKYRAEL YNEKRSDHVA CTVPLCDTDD MACKLTPWFE     50
    DGETAFNQVS SILKEKGKIL FVPMHMQRAM KFLPGPRVYL VERLTGGMLS 100
    KHFLVNQLAY KDQVGAAMMR TTLNAKPLGM FFPYDSSLET GEYTFLLRKN 150
    GLGGQLFRER PWDRKETPYV EILDDLEADP TGKYSQNLLK KLIGGDCIPI 200
    DQYMCGKNGK PIADYAKIVA KEGLTTLADI EVDVKSRMDS DRFIVLNKKL 250
    YRVVWNVTRR NVPYPKQTAF TIVSVVQCDD KDSVPEHTFT IGSQILMVSP 300
    LKATNNKNFN LKQRLLYTFY GKDAVQQPGY IYHSAYVDCN ACGRGTWCTG 350
    NAIQGFACDC GANYSANDVD LQSSGLVPRN ALFLANCPCA NNGACSHSAA 400
    QVYNILDGKA CVEVGGKSFT LTFGGVVYAY MGCCDGTMYF VPRAKSCVSR 450
    IGDAIFTGCT GTWDKVVETA NLFLEKAQRS LNFCQQFALT EVVLAILSGT 500
    TSTFEELRDL CHNASYEKVR DHLVNHGFVV TIGDYIRDAI NIGANGVCNA 550
    TINAPFIAFT GLGESFKKVS AIPWKICSNL KSALDYYSSN IMFRVFPYDI 600
    PCDVSNFVEL LLDCGKLTVA TSYFVLRYLD EKFDTVLGTV SSACQTALSS 650
    FLNACVAASR ATAGFINDMF KLFKVLMHKL YVYTSCGYVA VAEHSSKIVQ 700
    QVLDIMSKAM KLLHTNVSWA GTKLSAIIYE GREALLFNSG TYFCLSTKAK 750
    TLQGQMNLVL PGDYNKKTLG ILDPVPNADT IDVNANSTVV DVVHGQLEPT 800
    NEHGPSMIVG NYVLVSDKLF VRTEDEEFYP LCTNGKVVST LFRLKGGMPS 850
    KKVTFGDVNT VEVTAYRSVS ITYDIHPVLD ALLSSSKLAT FTVEKDLLVE 900
    DFVDVIKDEV LTLLTPLLRG YDIDGFDVED FIDVPCYVYN QDGDCAWSSN 950
    MTFSINPVED VEEVEEFIED DYLSDELPIA DDEEAWARAV EEVMPLDDIL 1000
    VAEIELEEDP PLETALESVE AEVVETAEAQ EPSVESIDST PSTSTVVGEN 1050
    DLSVKPMSRV AETDDVLELE TAVVGGPVSD VTAIVTNDIV SVEQAQQCGV 1100
    SSLPIQDEAS ENQVHQVSDL QGNELLCSET KVEIVQPRQD LKPRRSRKSK 1150
    VDLSKYKHTV INNSVTLVLG DAIQIASLLP KCILVNAANR HLKHGGGIAG 1200
    VINKASGGDV QEESDEYISN NGPLHVGDSV LLKGHGLADA ILHVVGPDAR 1250
    NNEDAALLKR CYKAFNKHTI VVTPLISAGI FSVDPKVSFE YLLANVTTTT 1300
    YVVVNNEDIY NTLATPSKPD GLVYSFEGWR GTVRTAKNYG FTCFICTEYS 1350
    ANVKFLRTKG VDTTKKIQTV DGVSYYLYSA RDALTDVIAA ANGCSGICAM 1400
    PFGYVTHGLD LAQSGNYVRQ VKVPYVCLLA SKEQIPIMNS DVAIQTPETA 1450
    FINNVTSNGG YHSWHLVSGD LIVKDVCYKK LLHWSGQTIC YADNKFYVVK 1500
    NDVALPFSDL EACRAYLTSR AAQQVNIEVL VTIDGVNFRT VILNDTTTFR 1550
    KQLGATFYKG VDISDAFPTV KMGGESLFVA DNLSESEKVV LKEYYGTSDV 1600
    TFLQRYYSLQ PLVQQWKFVV HDGVKSLKLS NYNCYINATI MMIDMLHDIK 1650
    FVVPALQNAY LRYKGGDPYD FLALIMAYGD CTFDNPDDEA KLLHTLLAKA 1700
    ELTVSAKMVW REWCTVCGIR DIEYTGMRAC VYAGVNSMEE LQSVFNETCV 1750
    CGSVKHRQLV EHSAPWLLVS GLNEVKVSTS TDPIYRAFNV FQGVETSVGH 1800
    YVHIRVKDGL FYKYDSGSLT KTSDMKCKMT SVWYPTVRYT ADCNVVVYDL 1850
    DGVTKVEVNP DLSNYYMKDG KYYTSKPTIK YSPATILPGS VYSNSCLVGV 1900
    DGTPGSDTIS KFFNDLLGFD ETKPISKKLT YSLLPNEDGD VLLSEFSNYN 1950
    PVYKKGVMLK GKPILWVNNG VCDSALNKPN RASLRQLYDV APIVLDNKYT 2000
    VLQDNTSQLV EHNVPVVDDV PITTRKLIEV KCKGLNKPFV KGNFSFVNDP 2050
    NGVTVVDTLG LTELRALYVD INTRYIVLRD NNWSSLFKLH TVESGDLQIV 2100
    AAGGSVTRRA RVLLGASSLF ASFAKITVTA TTAACKTAGR GFCKFVVNYG 2150
    VLQNMFVFLK MLFFLPFNYL WPKKQPTVDI GVSGLRTAGI VTTNIVKQCG 2200
    TAAYYMLLGK FKRVDWKATL RLFLLLCTTI LLLSSIYHLV LFNQVLSSDV 2250
    MLEDATGILA IYKEVRSYLG IRTLCDGLVV EYRNTSFDVM EFCSNRSVLC 2300
    QWCLIGQDSL TRYSALQMLQ THITSYVLNI DWIWFALEFF LAYVLYTSSF 2350
    NVLLLVVTAQ YFFAYTSAFV NWRAYNYIVS GLFFLVTHIP LHGLVRVYNF 2400
    LACLWFLRKF YSHVINGCKD TACLLCYKRN RLTRVEASTI VCGTKRTFYI 2450
    AANGGTSYCC KHNWNCVECD TAGVGNTFIC TEVANDLTTT LRRLIKPTDQ 2500
    SHYYVDSVVV KDAVVELHYN RDGSSCYERY PLCYFTNLEK LKFKEVCKTP 2550
    TGIPEHNFLI YDTNDRGQEN LARSACVYYS QVLCKPMLLV DVNLVTTVGD 2600
    SREIAIKMLD SFINSFISLF SVSRDKLEKL INTARDCVRR GDDFQNVLKT 2650
    FTDAARGHAG VESDVETTMV VDALQYAHKN DIQLTTECYN NYVPGYIKPD 2700
    SINTLDLGCL IDLKAASVNQ TSMRNANGAC VWNSGDYMKL SDSFKRQIRI 2750
    ACRKCNIPFR LTTSKLRAAD NILSVKFSAT KIVGGAPSWL LRVRDLTVKG 2800
    YCILTLFVFT VAVLSWFCLP SYSIATVNFN DDRILTYKVI ENGIVRDIAP 2850
    NDVCFANKYG HFSKWFNENH GGVYRNSMDC PITIAVIAGV AGARVANVPA 2900
    NLAWVGKQIV LFVSRVFANT NVCFTPINEI PYDTFSDSGC VLSSECTLFR 2950
    DAEGNLNPFC YDPTVLPGAS SYADMKPHVR YDMYDSDMYI KFPEVIVEST 3000
    LRITKTLATQ YCRFGSCEES AAGVCISTNG SWALYNQNYS TRPGIYCGDD 3050
    YFDIVRRLAI SLFQPVTYFQ LSTSLAMGLV LCVFLTAAFY YINKVKRALA 3100
    DYTQCAVVAV VAALLNSLCL CFIVANPLLV APYTAMYYYA TFYLTGEPAF 3150
    IMHISWYVMF GAVVPIWMLA SYTVGVMLRH LFWVLAYFSK KHVDVFTDGK 3200
    LNCSFQDAAS NIFVIGKDTY VALRNAITQD SFVRYLSLFN KYKYYSGAMD 3250
    TASYREACAA HLCKALQTYS ETGSDILYQP PNCSVTSSVL QSGLVKMSAP 3300
    SGAVENCIVQ VTCGSMTLNG LWLDNTVWCP RHIMCPADQL TDPNYDALLI 3350
    SKTNHSFIVQ KHIGAQANLR VVAHSMVGVL LKLTVDVANP STPAYTFSTV 3400
    KPGASFSVLA CYNGKPTGVF TVNLRHNSTI KGSFLCGSCG SVGYTENGGV 3450
    INFVYMHQME LSNGTHTGSS FDGVMYGAFE DKQTHQLQLT DKYCTINVVA 3500
    WLYAAVLNGC KWFVKPTRVG IVTYNEWALS NQFTEFVGTQ SIDMLAHRTG 3550
    VSVEQMLAAI QSLHAGFQGK TILGQSTLED EFTPDDVNMQ VMGVVMQSGV 3600
    KRISYGFIHW LISTFVLAYV SVMQLTKFTM WTYLFETIPT QMTPLLLGFM 3650
    ACVMFTVKHK HTFMSLFLLP VALCLTYANI VYEPQTLISS TLIAVANWLT 3700
    PTSVYMRTTH FDFGLYISLS FVLAIIVRRL YRPSMSNLAL ALCSGVMWFY 3750
    TYVIGDHSSP ITYLMFITTL TSDYTITVFA TVNLAKFISG LVFFYAPHLG 3800
    FILPEVKLVL LIYLGLGYMC TMYFGVFSLL NLKLRVPLGV YDYSVSTQEF 3850
    RFLTGNGLHA PRNSWEALIL NFKLLGIGGT PCIKVATVQS KLTDLKCTSV 3900
    VLLTVLQQLH LESNSKAWSY CVKLHNEILA AVDPTEAFER FVCLFATLMS 3950
    FSANVDLDAL ANDLFENSSV LQATLTEFSH LATYAELETA QSSYQKALNS 4000
    GDASPQVLKA LQKAVNVAKN AYEKDKAVAR KLERMAEQAM TSMYKQARAE 4050
    DKKAKIVSAM QTMLFGMIKK LDNDVLNGVI ANARNGCVPL SIVPLCASNK 4100
    LRVVIPDISV WNKVVNWPSV SYAGSLWDIT VINNVDNEVV KPTDVVETNE 4150
    SLTWPLVIEC SRSSSSAVKL QNNEIHPKGL KTMVITAGVD QVNCNSSAVA 4200
    YYEPVQGHRM VMGLLSENAH LKWAKVEGKD GFINIELQPP CKFLIAGPKG 4250
    PEIRYLYFVK NLNNLHRGQL LGHIAATVRL QAGANTEFAS NSTVLTLVAF 4300
    AVDPAKAYLD YVGSGGTPLS NYVKMLAPKT GTGVAISVKP EATADQETYG 4350
    GASVCLYCRA HIEHPDVSGV CKYKTRFVQI PAHVRDPVGF LLKNVPCNVC 4400
    QYWVGYGCNC DALRNNTVPQ SKDTNFLNES GVLV 4434

    Note: Produced by conventional translation.

    Length:4,434
    Mass (Da):491,823
    Last modified:June 10, 2008 - v1
    Checksum:i942E92FE623EFBCD
    GO
    Isoform Replicase polyprotein 1ab (identifier: P0C6W3-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry P0C6W3.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

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

    Length:7,119
    Mass (Da):795,200
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF065505 Genomic RNA. No translation available.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF065505 Genomic RNA. No translation available.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YNA X-ray 1.50 A/B 3292-3597 [» ]
    2YNB X-ray 1.96 A/B 3292-3597 [» ]
    ProteinModelPortali P0C6T4.
    SMRi P0C6T4. Positions 3889-3972, 4221-4281, 4291-4411.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR002589. Macro_dom.
    IPR024375. Nsp3_coronavir.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view ]
    Pfami PF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF11633. SUD-M. 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.
    PROSITEi PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 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 HKU4-1.

    Entry informationi

    Entry nameiR1A_BCHK4
    AccessioniPrimary (citable) accession number: P0C6T4
    Secondary accession number(s): A3EX93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 46 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete 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