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P0C6F6

- R1A_BC512

UniProt

P0C6F6 - R1A_BC512

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Bat coronavirus 512/2005 (BtCoV) (BtCoV/512/2005)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the 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

    Catalytic activityi

    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
    Sitei110 – 1112Cleavage; by PL1-PROBy similarity
    Sitei897 – 8982Cleavage; by PL1-PROBy similarity
    Active sitei1103 – 11031For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1252 – 12521For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1737 – 17371For PL2-PRO activityPROSITE-ProRule annotation
    Active sitei1902 – 19021For PL2-PRO activityPROSITE-ProRule annotation
    Sitei2530 – 25312Cleavage; by PL2-PROBy similarity
    Sitei3012 – 30132Cleavage; by 3CL-PROBy similarity
    Active sitei3053 – 30531For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3156 – 31561For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3314 – 33152Cleavage; by 3CL-PROBy similarity
    Sitei3590 – 35912Cleavage; by 3CL-PROBy similarity
    Sitei3673 – 36742Cleavage; by 3CL-PROBy similarity
    Sitei3868 – 38692Cleavage; by 3CL-PROBy similarity
    Sitei3976 – 39772Cleavage; by 3CL-PROBy similarity
    Sitei4111 – 41122Cleavage; by 3CL-PROBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1174 – 120532C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4050 – 406617By similarityAdd
    BLAST
    Zinc fingeri4092 – 410514By 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 host autophagy Source: UniProtKB-KW
    2. modulation by virus of host protein ubiquitination Source: UniProtKB-KW
    3. suppression by virus of host IRF3 activity Source: UniProtKB-KW
    4. viral genome replication Source: InterPro
    5. viral protein processing Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Activation of host autophagy by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host IRF3 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):
    p9
    Non-structural protein 2
    Short name:
    nsp2
    Alternative name(s):
    p87
    Alternative name(s):
    PL1-PRO/PL2-PRO
    PLP1/PLP2
    Papain-like proteinases 1/2
    p195
    Non-structural protein 4
    Short name:
    nsp4
    Alternative name(s):
    Peptide HD2
    3C-like proteinase (EC:3.4.22.-)
    Short name:
    3CL-PRO
    Short name:
    3CLp
    Alternative name(s):
    M-PRO
    nsp5
    p34
    Non-structural protein 6
    Short name:
    nsp6
    Non-structural protein 7
    Short name:
    nsp7
    Alternative name(s):
    p5
    Non-structural protein 8
    Short name:
    nsp8
    Alternative name(s):
    p23
    Non-structural protein 9
    Short name:
    nsp9
    Alternative name(s):
    p12
    Non-structural protein 10
    Short name:
    nsp10
    Alternative name(s):
    Growth factor-like peptide
    Short name:
    GFL
    p14
    Non-structural protein 11
    Short name:
    nsp11
    Gene namesi
    ORF Names:1a
    OrganismiBat coronavirus 512/2005 (BtCoV) (BtCoV/512/2005)
    Taxonomic identifieri693999 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
    Virus hostiScotophilus kuhlii (Lesser asiatic yellow bat) [TaxID: 153297]

    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 – 41284128Replicase polyprotein 1aPRO_0000338050Add
    BLAST
    Chaini1 – 110110Non-structural protein 1By similarityPRO_0000338051Add
    BLAST
    Chaini111 – 897787Non-structural protein 2By similarityPRO_0000338052Add
    BLAST
    Chaini898 – 25301633Non-structural protein 3By similarityPRO_0000338053Add
    BLAST
    Chaini2531 – 3012482Non-structural protein 4By similarityPRO_0000338054Add
    BLAST
    Chaini3013 – 33143023C-like proteinaseBy similarityPRO_0000338055Add
    BLAST
    Chaini3315 – 3590276Non-structural protein 6By similarityPRO_0000338056Add
    BLAST
    Chaini3591 – 367383Non-structural protein 7By similarityPRO_0000338057Add
    BLAST
    Chaini3674 – 3868195Non-structural protein 8By similarityPRO_0000338058Add
    BLAST
    Chaini3869 – 3976108Non-structural protein 9By similarityPRO_0000338059Add
    BLAST
    Chaini3977 – 4111135Non-structural protein 10By similarityPRO_0000338060Add
    BLAST
    Chaini4112 – 412817Non-structural protein 11Sequence AnalysisPRO_0000338061Add
    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

    ProteinModelPortaliP0C6F6.
    SMRiP0C6F6. Positions 3013-3311, 3871-3975, 3982-4107.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1973 – 199321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2036 – 205621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2119 – 213921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2141 – 216121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2164 – 218421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2543 – 256321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2634 – 265421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2669 – 268921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2769 – 278921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2802 – 282221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2829 – 284921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2878 – 289821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3351 – 337121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3376 – 339621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3414 – 343421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3443 – 346321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3466 – 348621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3488 – 350720HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3511 – 353121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1069 – 1302234Peptidase C16 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1303 – 1467165MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1699 – 1965267Peptidase C16 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini3013 – 3314302Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1973 – 2184212HD1By similarityAdd
    BLAST
    Regioni2543 – 2898356HD2By similarityAdd
    BLAST
    Regioni3351 – 3531181HD3By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1827 – 1946120Val-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 2 peptidase C16 domains.PROSITE-ProRule annotation
    Contains 1 peptidase C30 domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1174 – 120532C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4050 – 406617By similarityAdd
    BLAST
    Zinc fingeri4092 – 410514By similarityAdd
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    InterProiIPR002589. Macro_dom.
    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.
    PF08715. Viral_protease. 2 hits.
    [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. 2 hits.
    [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: P0C6F6-1) [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

    MASNHISLAF ANDEEISAIG FGSVEEAVSY YSDAAVNGFD QCRFVSLGLQ     50
    DAVVGVEDDD VVMLITGVTQ LRAYLGTFGD RPLNLRGWLL FSNCNYFLEE 100
    LDLVFGRCGG TTIPVDQFMC GADGAPVIQE GDWTFMDYFQ DSNQFTLNGI 150
    TYVKAWDVDR KPNDYAKQNV TCIRRITYIT DHRHVLADGT TMKTARHPKV 200
    NKSVVLDSPF DQIYKEVGSP FMGNGSTFVE MLKDPAFFHA LITCECGRSE 250
    WTVGDWKGYN SLCCNIKCKP ITIVTPKAVP GAVVITKAGI GAGLKCYNNV 300
    FLKHIIDLVV PGTNLGWGVW RIAKVQSKDD VATSGNVLVD DPEDRLDPCY 350
    FGNDGPFATK FKFQLLANSF DDEVKGAIVQ GVVHVNTAIC DVVKDILGLP 400
    WFVKKLGSLV TVMWDQFVAG VQSMKICTLK VVQLAKALSC ATMSVVKGVI 450
    TLVAEVPEIF KRLFYTLTSA LKSLCTSSCD ALVVAGKSFA KIGDYVLLPS 500
    ALVRLVSSKV KGKAQSGIKQ LQFATVVLGD THKVESDRVE FSSVNLKMVD 550
    EEFPLNPVGH TVAVGNQAFF CSDGLYRFMA DRDLVITSPI FKPELELEPI 600
    FECDAIPGFP KVAASNVAEL CVKVDTLLFN YDKIYKKYST IIKGDRCYIQ 650
    CTHTFKAPSY YFDDDEFVEL CTKYYKLPDF DAFYNAVHAA TDMDQFCALC 700
    TSGFEVFIPR VPDCPPILND IDGGSIWTSF ILSVRSATDF IKTLKIDLGL 750
    NGVVVFVTKK FRKAGALLQK LYNAFLDTVT SFIKVAGVAF KYCATCVPKI 800
    VINGCYHTVT RLFAKDLQIP TEDGVADFNT FNHCVFPVNP TRIETDSLEL 850
    EEVDFVEPGV DGKLVILDDY SFYSDGTNYY PSDGKGVVAS CFKKKGGGVV 900
    TISDEVQVRT IDPVYKVRLE YEFEDETLVK VCEKAIGTKL KVTGDWSNLL 950
    ETLEKAMDVV RQHLDVPDYF VYDEEGGTDL NLTIMVSQWP LSSDSEDDFK 1000
    AVDDEPNANT DETVDTFAED VAETQNVQQD VTQDEVEAVC DLVVKATEEG 1050
    PIEHEELSED QKEVQQALAF IEDKPVVVKP DVFAFSYASY GGLKVLNQSS 1100
    NNCWVSSALV QLQLTGLLDS DEMQLFNAGR VSPMVKRCYE SQRAIFGSLG 1150
    DVSACLESLL KDRDGMSITC TIDCGCGPGV RVYENAIFRF TPLKTAFPMG 1200
    RCLICSKTLM HTITQMKGTG IFCRDATALD VDTLVVKPLC AAVYVGAQDG 1250
    GHYLTNMYDA NMAVDGHGRH PIKFNTINTL CYKDVDWEVS NGSCDVKPFL 1300
    TYKNIEFYQG ELSALLSVNH DFVVNAANEQ LSHGGGIAKA LDDLTKGELQ 1350
    VLSNQYVSRN GSIKVGSGVL IKCKEHSILN VVGPRKGKHA AELLTKAYTF 1400
    VFKQKGVPLM PLLSVGIFKV PITESLAAFL ACVGDRVCKC FCYTDKERLA 1450
    IQNFVTSFQT EQPVEPLPVI QEVKGVQLEK PVPDVKVENP CEPFRIEGDA 1500
    KFYDLTPSMV QSLQVTRLVS FTNSDLCLGS FVRDCDGYVQ GSLGGAIANY 1550
    KKSNPVLPAG NCVTLKCDGF ISFTFVILPK EGDTNYEKNF NRAIAKFLKL 1600
    KGSLLVVVED SSVFNKISHA SVAGYVAKPA LVDTLFEAKP VQVVVTQDQR 1650
    SFHTVELSTS QTYGQQLGDC VVEDKKVTNL KPVSKDKVVS VVPNVDWDKH 1700
    YGFVDAGIFH TLDHTMFVFD NNVVNGKRVL RTSDNNCWIN AVCLQLQFAN 1750
    AKFKPKGLQQ LWESYCTGDV AMFVHWLYWI TGVEKGEPSD AENTLNIISR 1800
    FLKPQGSVEM LRATSTTCDG TCSTKRVVST PVVNASVLKV GLDDGNCVHG 1850
    LPLVDRVVSV NGTVIITNVG DTPGKPVVAT ENLLLDGVSY TVFQDSTTGV 1900
    GHYTVFDKEA KLMFDGDVLK PCDLNVSPVT SVVVCNNKKI VVQDPVKRVE 1950
    LDASKFLDTM NVASEKFFTF GDFVSRNIIV LIVYLFSLLA ICFRALKKRD 2000
    MKVMAGVPER TGIILKRSVK YNYKALKFFF RLKFQYIKVF LKFSLVLYTL 2050
    YALMFMFIRF TPVGTPICKR YTDGYANSTF DKNDYCGNVL CKICLYGYEE 2100
    LSDFTHTRVI WQHLKDPLIG NILPLFYLVF LIIFGGFFVR IGITYFIMQY 2150
    INAAGVALGY QDNVWLLHLL PFNSMGNIIV VAFIVTRILL FLKHVLFGCD 2200
    KPSCIACSKS AKLTRVPLQT ILQGVTKSFY VNANGGKKFC KKHNFFCVDC 2250
    DSYGYGCTFI NDVIAPELSN VTKLNVIPTG PATIIIDKVE FSNGFYYLYS 2300
    GSTFWKYNFD ITEAKYACKD VLKNCNILTD FVVFNNSGSN VTQVKNACVY 2350
    FSQLLCKPIK LVDSALLASL NVDFSANLHK AFVEVLSNSF GKDLSNCSNM 2400
    NECRESLGLS DVPEEEFSAA VSEAHRYDVL ISDVSFNNLI VSYAKPEEKL 2450
    AVHDIANCMR VGAKVVNHNV LTKDNVPVVW LAKDFIALSE EARKYIVRTT 2500
    KTKGINFMLT FNDRRMHLTI PTISVANKKG AGLPSLFTRL YSFFWHLCVL 2550
    IVVLFVATSL LDFSAQVTSD TQYDFKYIEN GVLKVFEKPL DCVHNAFVNF 2600
    NEWHNAKFGS IPTNSRRCPI VVGTSDEVRY IPGVPAGVFL YGKSLIFAMS 2650
    TIFGTSGLCF DDRGLTDPDS CIFNSACTTL SGIGGRNVYC YREGVVDNAK 2700
    LYSSLLPHSY YRLMDGNHIV LPEIITRGFG IRTIKTQAMT YCRTGECIDS 2750
    QAGVCVGLDR FFVYSKTPGS DYVCGTGFFS LLFNVIGMFS NSIPVTVMSG 2800
    QILLNCVVAF TAVMACFAFT KFKRLFGDMS FGVLSVGLCT VVNNLSYVVT 2850
    QNSIGMLAYA TLYFLCTKGV RYSWVWHVGF AISYCFLAPW WVVLAYLICA 2900
    LLEFLPNLFK LKVSTQLFEG DKFVGSFESA ASGTFVLDMH SYQKLANSIS 2950
    TEKLKQYCAS YNRYKYYSGS ASEADYRLAC FAHLAKAMSD FANDHMDKLY 3000
    TPPTVSYNST LQAGLRKMAQ PSGIVEGCIV RVSYGNLTLN GLWLGDTVIC 3050
    PRHVIASNTT NVIDYDHAMS LVRLHNFSIS SGNMFLGVIS ASMRGTLLHI 3100
    KVNQSNVNTP NYTYKVLKPG DSFNILACYD GSAAGVYGVN MRTNYTIRGS 3150
    FISGACGSPG YNINNGVVEF CYMHHLELGS GCHVGSDMDG TMYGKYEDQP 3200
    TLQIEGASNL VTENVCSWLY GALINGDRWW LSSVSVGVDT YNEWALRNGM 3250
    TALKNVDCFS LLVAKTGVDV GRLLASIQKL HGNFGGKSIL GCTSLCDEFT 3300
    LSEVVKQMYG VTLQSGKVSR AFRNASIVCC LLFLFLSEML NHSKLFWINP 3350
    GYITPVFLAI IVASSALMLL VKHKLLFLQL YLLPSLCIVS GYNIFKDYHF 3400
    YTYMLEEFDY KVPFGGFNVT GVLNISLCCF VMGLHTFRFL QTPNKIFSYV 3450
    VAVLTVLYTY YYSTDVLGLI LTSMSGFTNY WFIGTATYKL ATYVLPHTSL 3500
    LDSFDAIKAV VFLYLLLGYC NCVYYGSLYW INRFCKLTLG CYEFKVSAAE 3550
    FKYMVANGLR APTGVFDALI LSLKLIGVGG RKTIKISSVQ SKLTDLKCTN 3600
    VVLLGCLSNM NIAANSREWA YCVDLHNKIN LCNDAEAAQE MLLALLAFFL 3650
    SKNSAFGVDE LLDSYFNDSS VLQSVAATYV NLPSYLAYET ARQSYEDALA 3700
    NGSPPQLVKQ LRHAMNVAKS EFDREASTQR KLDRMAEQAA SQMYKEARAV 3750
    NRKSKVVSAM HSLLFGMLRR LDMSSVDTIL SLAKDGVVPL SIIPAVSATK 3800
    LNIVVSDIES YSKIQREGCV HYAGVIWSVV DIKDNDGKPV HAKEVVTSNV 3850
    ESLAWPLFLN CERIIKLQNN EIIPSKIKQR PIKAEGEGVV ADGNALYSNE 3900
    GGRTFMYAFI SDKPDLKVVK WEFDGGSNAI ELEPPCKFLV EAPSGPVVKY 3950
    LYFVRNLNNL RRGAVLGFIG ATVRLQAGKQ TEQATNSSLL TLCAFAVDPP 4000
    KTYLDAVKSG HRPVGNCVKM LANGSGNGQA ITNGVEASTN QDSYGGASVC 4050
    LYCRAHVEHP DMDGFCKLRG KYVQVPLGTL DPIRFVLENT VCKVCGCWQA 4100
    NGCTCDRAVI QSVDSGYLNE CGALVQLD 4128

    Note: Produced by conventional translation.

    Length:4,128
    Mass (Da):456,581
    Last modified:June 10, 2008 - v1
    Checksum:i550324DCD9D1820F
    GO
    Isoform Replicase polyprotein 1ab (identifier: P0C6W0-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry P0C6W0.
    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:6,793
    Mass (Da):757,262
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ648858 Genomic RNA. No translation available.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ648858 Genomic RNA. No translation available.

    3D structure databases

    ProteinModelPortali P0C6F6.
    SMRi P0C6F6. Positions 3013-3311, 3871-3975, 3982-4107.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR002589. Macro_dom.
    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.
    PF08715. Viral_protease. 2 hits.
    [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. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiR1A_BC512
    AccessioniPrimary (citable) accession number: P0C6F6
    Secondary accession number(s): Q0Q467
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 42 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 512/2005 is highly similar to porcine epidemic diarrhea virus (PEDV).

    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