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P0C6F5

- R1A_BC279

UniProt

P0C6F5 - R1A_BC279

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Bat coronavirus 279/2005 (BtCoV) (BtCoV/279/2005)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    The papain-like proteinase (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
    Sitei179 – 1802CleavageBy similarity
    Sitei818 – 8192Cleavage; by PL-PROBy similarity
    Active sitei1657 – 16571For PL-PRO activityPROSITE-ProRule annotation
    Active sitei1818 – 18181For PL-PRO activityPROSITE-ProRule annotation
    Sitei3246 – 32472Cleavage; by PL-PROBy similarity
    Active sitei3287 – 32871For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3391 – 33911For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3552 – 35532Cleavage; by 3CL-PROBy similarity
    Sitei3842 – 38432Cleavage; by 3CL-PROBy similarity
    Sitei3925 – 39262Cleavage; by 3CL-PROBy similarity
    Sitei4123 – 41242Cleavage; by 3CL-PROBy similarity
    Sitei4236 – 42372Cleavage; by 3CL-PROBy similarity
    Sitei4375 – 43762Cleavage; by 3CL-PROBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1735 – 177238C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4310 – 432617By similarityAdd
    BLAST
    Zinc fingeri4353 – 436614By similarityAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: InterPro
    2. hydrolase activity, acting on acid anhydrides Source: InterPro
    3. hydrolase activity, acting on ester bonds Source: InterPro
    4. omega peptidase activity Source: InterPro
    5. RNA binding Source: UniProtKB-KW
    6. RNA-directed RNA polymerase activity Source: InterPro
    7. 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 279/2005 (BtCoV) (BtCoV/279/2005)
    Taxonomic identifieri389167 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
    Virus hostiRhinolophus macrotis (Big-eared horseshoe bat) [TaxID: 196889]
    ProteomesiUP000006573: 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 – 43884388Replicase polyprotein 1aPRO_0000338038Add
    BLAST
    Chaini1 – 179179Non-structural protein 1By similarityPRO_0000338039Add
    BLAST
    Chaini180 – 818639Non-structural protein 2By similarityPRO_0000338040Add
    BLAST
    Chaini819 – 27461928Non-structural protein 3By similarityPRO_0000338041Add
    BLAST
    Chaini2747 – 3246500Non-structural protein 4By similarityPRO_0000338042Add
    BLAST
    Chaini3247 – 35523063C-like proteinaseBy similarityPRO_0000338043Add
    BLAST
    Chaini3553 – 3842290Non-structural protein 6By similarityPRO_0000338044Add
    BLAST
    Chaini3843 – 392583Non-structural protein 7By similarityPRO_0000338045Add
    BLAST
    Chaini3926 – 4123198Non-structural protein 8By similarityPRO_0000338046Add
    BLAST
    Chaini4124 – 4236113Non-structural protein 9By similarityPRO_0000338047Add
    BLAST
    Chaini4237 – 4375139Non-structural protein 10By similarityPRO_0000338048Add
    BLAST
    Chaini4376 – 438813Non-structural protein 11Sequence AnalysisPRO_0000338049Add
    BLAST

    Post-translational modificationi

    Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed By similarity.By similarity

    Interactioni

    Subunit structurei

    3CL-PRO exists as monomer and homodimer. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP0C6F5.
    SMRiP0C6F5. Positions 13-127, 819-930, 1000-1174, 1337-1475, 1547-1860, 3247-3552, 3842-3925, 3927-4117, 4124-4236, 4246-4368.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2209 – 222921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2310 – 233021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2357 – 237721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2761 – 278121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2998 – 301821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3028 – 304821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3060 – 308021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3083 – 310321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3111 – 313121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3148 – 316821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3570 – 359021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3592 – 361221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3618 – 363821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3665 – 368420HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3691 – 371020HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3734 – 375421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3762 – 378221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1001 – 1167167MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1617 – 1881265Peptidase C16PROSITE-ProRule annotationAdd
    BLAST
    Domaini3247 – 3552306Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2098 – 2377280HD1By similarityAdd
    BLAST
    Regioni2761 – 3168408HD2By similarityAdd
    BLAST
    Regioni3570 – 3782213HD3By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi930 – 99970Glu-richAdd
    BLAST
    Compositional biasi2216 – 22194Poly-Leu
    Compositional biasi3772 – 37754Poly-Cys

    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 fingeri1735 – 177238C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4310 – 432617By similarityAdd
    BLAST
    Zinc fingeri4353 – 436614By similarityAdd
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    InterProiIPR002589. Macro_dom.
    IPR021590. NSP1.
    IPR024375. Nsp3_coronavir.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR024358. SARS-CoV_Nsp3_N.
    IPR022733. SARS_polyprot_cleavage.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view]
    PfamiPF12379. DUF3655. 1 hit.
    PF01661. Macro. 1 hit.
    PF11501. Nsp1. 1 hit.
    PF09401. NSP10. 1 hit.
    PF12124. Nsp3_PL2pro. 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]
    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: P0C6F5-1) [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

    MESLALGVSE KTHVQLSLPV LQVRDVLVRG FGDSVEEALA EAREHLKNGT     50
    CGLVELEKGV LPQLEQPYVF IKRSDAQGTN HGYKVVELVA ELDGIQYGRS 100
    GTTLGVLVPH VGETPVAYRN VLLRKNGNKG AGGHSYGIDL KSYDLGVELG 150
    TDPIEDYEQN WNTKHGGGVL RELIRELNGG AFTRYVDNNF CGPDGYPLEC 200
    IKDLLARAGK SMCTLSEQLD YIESKRGVYC CREHEHEIVW FTERSEKSYE 250
    RQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI 300
    RSVYPVATPQ ECNDMHLSTL MKCNHCDEVS WQTCDFLKAT CEQCGTENLV 350
    CEGPTTCGYL PANAVVKMPC PACQDPEVGP EHSVADYHNH SNIETRLRKG 400
    GRTKCFGGCV FAYVGCYNKR AYWVPRASAN IGASHTGITG DNVETLNEDL 450
    MEILNRDRVN INIVGDFHLN EEVAIILASF SASTCAFVDT VKGLDYKTFK 500
    DIVESCGNFK VTRGRAKKGA WNIGQEKSIL TPLYGFPSQA AGVIRSIFTR 550
    ALDTANHSIP DLQRAAITIL DGISEQSLRL IDAMVYTSDL LTNSVIVMAY 600
    VTGGLVQQIT QWLSNMLGTT VDKLKPVFTW VEAKLSAGIE FLRDAWEILK 650
    FLVTGVFDIV KGQIQVASDN LKECVKAFLD VLNKALEMCI DQVIIAGAKL 700
    RTLNLGEVFI AQSKGLYRQC IRGKEQLQLL MPLRAPKEVT FFEGDSHDTV 750
    FTSEEVVLKN GELEALETPV DSFTNGAVIG TPVCVNGLML LELKDKEQYC 800
    ALSPGLLATN NVFSLKGGAP VKGVTFGEDT VLEVQGYKNV KITFELDERV 850
    DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE 900
    WSVATFYLFD DAGEEKLSSR MYCSFYPPDE EEDCEEYEDE EEIPEETCEH 950
    EYGTEDDYKG LPLEFGASTE IQQVDEEEEE DWLEEAIAAK PEPEPLPEEP 1000
    VNQFTGYLKL TDNVAIKCVD IVKEAQHAKP TVIVNAANVH LKHGGGVAGA 1050
    LNKATNGAMQ QESDDYIKKN GPLTVGGSCL LSGHNLAKKC MHVVGPNLNA 1100
    GEDVQLLKAA YANFNSQDVL LAPLLSAGIF GAKPLQSLKM CVETVRTQVY 1150
    FAVNDQDLYD HVVLGYLDSL KPKVETPTQE NLELKEQPAV ETLTQENLEL 1200
    EELPVIEKPV DVKFKARIEE VNTSLEETKF LTSRLLLFAD INGKLYQDSQ 1250
    NMLRGEDMFF LEKDAPYIVG DVISSGDITC VIIPAKKAGG TTEMLAKALK 1300
    KVPVSEYITT YPGQGCAGYT LEEAKTALRK CKSVFYVLPS KTPNDKEEIL 1350
    GTVSWNLREM LAHAEETRKL MLICMDVKAL MSTIHRRYKG IKVQEGIVDY 1400
    GVRFFFYTSK EPVASIITKL NLLNEPLVTM PIGYVTHGLN LEEAARCMRS 1450
    LKAPAVVSVS SPDAVTTYNG YLTSSSKTSE EHFIETVSLA GMYRDWSYSG 1500
    QRTELGVEFL KRGDKVVYHT VGSPIQFHLD GEVLLLDKLK SLLSLREVRT 1550
    IKVFTTVDNT NLHTQIVDMS MTYGQQFGPT YLDGADVTKI KPHAKHEGKT 1600
    FFVLPSDDTL RSEAFEYYHT LDESFLGRYM SALNHTKKWK FPQIGGLTSI 1650
    KWADNNCYLS SVLLALQQIE VKFNAPALQE AYYRARAGDA ANFCALILAY 1700
    SNRTVGELGD VRETMTHLLQ HANLESAKRV LNVVCKTCGQ KSTTLTGVEA 1750
    VMYMGTLSYE ELKTGVTIPC ICGRDATQYL VQQESSFVMM SAPPSEYTLQ 1800
    QGAFLCANEY TGSYQCGHYT HVTVKETLYR IDGAYLTKMS EYKGPVTDVF 1850
    YKEISYTTTI KPVSYKLDGV IYTEIQPKLD EYYKKDNAYY TEQPIDLVPT 1900
    QPLPNASFDN FKLTCSNTKF ADDLNQMTGF KKPASRELSV TFFPDLNGDV 1950
    VAIDYRHYSA SFKKGAKLLH KPIIWHINQT TNKTTYKPNT WCLRCLWSTK 2000
    PVETSNSFEV LEVEDTQGMD NLACESQTPT SEEVVENPTI QKEVIECDVK 2050
    TIEVVGNVIL KPSEEGVKVT QELGHEDLMA AYVEETSITI KKPNELSLAL 2100
    GLRTLATHGA AAINSVPWSK ILAYVKPFLG QAAVTTTNCI KRCVQRVFNN 2150
    YMPYVITLLF QLCTFTRSTN SRIRASLPTT IAKNSVKSVA KLCLDVCINY 2200
    VKSPKFSKLF TIAMWLLLLS ICLGSLIYVT AAFGVLLSNL GIPSYCDGVR 2250
    ESYVNSSNVT TMDFCEGSFL CSVCLNGLDS LDSYPALETI QVTISSYKLD 2300
    LTSLGLAAEW FLAYMLFTKF FYLLGLSAIM QVFFGYFASH FISNSWLMWF 2350
    IISIVQMAPV SAMVRMYIFF AFCYYVWKSY VHIMDGCTSS TCMMCYKRNR 2400
    ATRVECTTIV NGMKRSFYVY ANGGRGFCKA HNWNCLNCDT FCAGSTFISD 2450
    EVARDLSLQF KRPINPTDQS SYVVDSVAVK NGALHLYFDK AGQKTYERHP 2500
    LSHFVNLDNL RANNTKGSLP INVIVFDGKS KCDESAAKSA SVYYSQLMCQ 2550
    PILLLDQALV SDVGDSTEVS VKMFDAYVDT FSATFSVPME KLKALVATAH 2600
    SELAKGVALD GVLSTFVSAA RQGVVDTDVD TKDVIECLKL SHHSDLEVTG 2650
    DSCNNFMLTY NKVENMTPRD LGACIDCNAR HINAQVAKSH NVSLIWNVKD 2700
    YMSLSEQLRK QIRSAAKKNN IPFRLTCATT RQVVNAITTK ISLKGGKIVS 2750
    TWFKLMLKAT LLCVLAALFC YIIMPVHSLS VHDGYTNEII GYKAIQDGVT 2800
    RDIMATDDCF ANKHAGFDSW FSQRGGSYRN DKSCPVVAAI ITREIGFIVP 2850
    GLPGTVLRAI NGDFLHFLPR VFSAVGNICY TPSKLIEYSD FATSACVLAA 2900
    ECTIFKDAMG KPVPYCYDTN LLEGSISYSE LRPDTRYVLM DGSIIQFPNT 2950
    YLEGSVRVVT TFDAEYCRHG TCERSEAGVC LSTSGRWVLN NEHYRALPGV 3000
    FCGVDAMNLI ANIFTPLVQP VGALDVSASV VAGGIIAILV TCAAYYFMKF 3050
    RRAFGEYNHV VAANALLFLM SFTILCLAPA YSFLPGVYSI FYLYLTFYFT 3100
    NDVSFLAHLQ WFAMFSPIVP FWITAIYVFC ISLKHCHWFF NNYLRKRVMF 3150
    NGVTFSTFEE AALCTFLLNK EMYLKLRSET LLPLTQYNRY LALYNKYKYF 3200
    SGALDTTSYR EAACCHLAKA LNDFSNSGAD VLYQPPQTSI TSAVLQSGFR 3250
    KMAFPSGKVE GCMVQVTCGT TTLNGLWLDD TVYCPRHVIC TAEDMLNPNY 3300
    EDLLIRKSNH SFLVQAGNVQ LRVIGHSMQN CLLRLKVDTS NPKTPKYKFV 3350
    RIQPGQTFSV LACYNGSPSG VYQCAMRPNY TIKGSFLNGS CGSVGFNIDY 3400
    DCVSFCYMHH MELPTGVHAG TDLEGKFYGP FVDRQTAQAA GTDTTITLNV 3450
    LAWLYAAVIN GDRWFLNRFT TTLNDFNLVA MKYNYEPLTQ DHVDILGPLS 3500
    AQTGIAVLDM CAALKELLQN GMNGRTILGS TILEDEFTPF DVVRQCSGVT 3550
    FQGKFKKIVK GTHHWMLLTF LTSLLILVQS TQWSLFFFVY ENAFLPFTLG 3600
    IMAIAACAML LVKHKHAFLC LFLLPSLATV AYFNMVYMPA SWVMRIMTWL 3650
    ELADTSLSGY RLKDCVMYAS ALVLLVLMTA RTVYDDAARR VWTLMNVITL 3700
    VYKVYYGNSL DQAISMWALV ISVTSNYSGV VTTIMFLARA IVFVCVEYYP 3750
    LLFITGNTLQ CIMLVYCFLG YCCCCYFGLF CLLNRYFRLT LGVYDYLVST 3800
    QEFRYMNSQG LLPPKSSIDA FKLNIKLLGI GGKPCIKVAT VQSKMSDVKC 3850
    TSVVLLSVLQ QLRVESSSKL WAQCVQLHND ILLAKDTTEA FEKMVSLLSV 3900
    LLSMQGAVDI NKLCEEMLDN RATLQAIASE FSSLPSYAAY ATAQEAYEQA 3950
    VANGDSEVVL KKLKKSLNVA KSEFDRDAAM QRKLEKMADQ AMTQMYKQAR 4000
    SEDKRAKVTS AMQTMLFTML RKLDNDALNN IINNARDGCV PLNIIPLTTA 4050
    AKLMVVVPDY GTYKNTCDGN TFTYASALWE IQQVVDADSK IVQLSEINMD 4100
    NSQNLAWPLI VTALRANSAV KLQNNELSPV ALRQMSCAAG TTQTACTDDN 4150
    ALAYYNNSKG GRFVLALLSD HQDLKWARFP KSDGTGTIYT ELEPPCRFVT 4200
    DTPRGPKVKY LYFIKGLNNL NRGMVLGSLA ATVRLQAGNA TEVPANSAVL 4250
    SFCAFAVDPA KAYKDYLASG GQPITNCVKM LCTHTGTGQA ITVTPEANMD 4300
    QESFGGASCC LYCRCHIDHP NPKGFCDLKG KYVQIPATCA NDPVGFTLKN 4350
    TVCTVCGTWK GYGCSCDQLR EPMMQSADAS TFLNGFAV 4388

    Note: Produced by conventional translation.

    Length:4,388
    Mass (Da):487,709
    Last modified:June 10, 2008 - v1
    Checksum:i1D91B831273D6F2A
    GO
    Isoform Replicase polyprotein 1ab (identifier: P0C6V9-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry P0C6V9.
    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:7,079
    Mass (Da):791,654
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ648857 Genomic RNA. No translation available.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ648857 Genomic RNA. No translation available.

    3D structure databases

    ProteinModelPortali P0C6F5.
    SMRi P0C6F5. Positions 13-127, 819-930, 1000-1174, 1337-1475, 1547-1860, 3247-3552, 3842-3925, 3927-4117, 4124-4236, 4246-4368.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR002589. Macro_dom.
    IPR021590. NSP1.
    IPR024375. Nsp3_coronavir.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR024358. SARS-CoV_Nsp3_N.
    IPR022733. SARS_polyprot_cleavage.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view ]
    Pfami PF12379. DUF3655. 1 hit.
    PF01661. Macro. 1 hit.
    PF11501. Nsp1. 1 hit.
    PF09401. NSP10. 1 hit.
    PF12124. Nsp3_PL2pro. 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 ]
    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiR1A_BC279
    AccessioniPrimary (citable) accession number: P0C6F5
    Secondary accession number(s): Q0Q476
    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

    Miscellaneous

    Bat coronavirus 279/2005 is highly similar to SARS-CoV (SARS-like).

    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