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K9N638

- R1A_CVEMC

UniProt

K9N638 - R1A_CVEMC

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Human coronavirus EMC (isolate United Kingdom/H123990006/2012) (HCoV-EMC)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 16 (01 Oct 2014)
      Sequence version 1 (06 Mar 2013)
      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.By similarity
    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) 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
    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

    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).
    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei193 – 1942CleavageBy similarity
    Sitei853 – 8542Cleavage; by PL-PROBy similarity
    Active sitei1592 – 15921For PL-PRO activityPROSITE-ProRule annotation
    Active sitei1759 – 17591For PL-PRO activityPROSITE-ProRule annotation
    Sitei2740 – 27412Cleavage; by PL-PROBy similarity
    Sitei3247 – 32482Cleavage; by 3CL-PROBy similarity
    Active sitei3288 – 32881For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3395 – 33951For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3553 – 35542Cleavage; by 3CL-PROBy similarity
    Sitei3845 – 38462Cleavage; by 3CL-PROBy similarity
    Sitei3928 – 39292Cleavage; by 3CL-PROBy similarity
    Sitei4127 – 41282Cleavage; by 3CL-PROBy similarity
    Sitei4237 – 42382Cleavage; by 3CL-PROBy similarity
    Metal bindingi4311 – 43111Zinc
    Metal bindingi4314 – 43141Zinc
    Metal bindingi4320 – 43201Zinc
    Metal bindingi4327 – 43271Zinc
    Metal bindingi4354 – 43541Zinc
    Metal bindingi4357 – 43571Zinc
    Metal bindingi4365 – 43651Zinc
    Sitei4377 – 43782Cleavage; by 3CL-PROBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1672 – 170938C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4311 – 432717Add
    BLAST
    Zinc fingeri4354 – 436714Add
    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
    SARS coronavirus main proteinase
    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
    OrganismiHuman coronavirus EMC (isolate United Kingdom/H123990006/2012) (HCoV-EMC)
    Taxonomic identifieri1263720 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirusunclassified Betacoronavirus

    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 – 193193Non-structural protein 1By similarityPRO_0000422454Add
    BLAST
    Chaini194 – 853660Non-structural protein 2By similarityPRO_0000422455Add
    BLAST
    Chaini854 – 27401887Non-structural protein 3By similarityPRO_0000422456Add
    BLAST
    Chaini2741 – 3247507Non-structural protein 4Sequence AnalysisPRO_0000422457Add
    BLAST
    Chaini3248 – 35533063C-like proteinaseBy similarityPRO_0000422458Add
    BLAST
    Chaini3554 – 3845292Non-structural protein 6By similarityPRO_0000422459Add
    BLAST
    Chaini3846 – 392883Non-structural protein 7By similarityPRO_0000422460Add
    BLAST
    Chaini3929 – 4127199Non-structural protein 8By similarityPRO_0000422461Add
    BLAST
    Chaini4128 – 4237110Non-structural protein 9By similarityPRO_0000422462Add
    BLAST
    Chaini4238 – 4377140Non-structural protein 10By similarityPRO_0000422463Add
    BLAST
    Chaini4378 – 439114Non-structural protein 11By similarityPRO_0000422464Add
    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

    Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer.

    Structurei

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2105 – 212521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2177 – 219721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2281 – 230121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2305 – 232521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2330 – 235021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2757 – 277721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3028 – 304821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3062 – 308221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3104 – 312421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3125 – 314521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3559 – 357921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3593 – 361321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3618 – 363821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3664 – 368421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3691 – 371121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3740 – 376021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3765 – 378521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1110 – 1276167MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1552 – 1823272Peptidase C16PROSITE-ProRule annotationAdd
    BLAST
    Domaini3248 – 3553306Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2040 – 2363324HD1Add
    BLAST
    Regioni2761 – 3171411HD2Add
    BLAST
    Regioni3571 – 3785215HD3Add
    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.

    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 fingeri1672 – 170938C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4311 – 432717Add
    BLAST
    Zinc fingeri4354 – 436714Add
    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: K9N638-1) [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

    MSFVAGVTAQ GARGTYRAAL NSEKHQDHVS LTVPLCGSGN LVEKLSPWFM     50
    DGENAYEVVK AMLLKKEPLL YVPIRLAGHT RHLPGPRVYL VERLIACENP 100
    FMVNQLAYSS SANGSLVGTT LQGKPIGMFF PYDIELVTGK QNILLRKYGR 150
    GGYHYTPFHY ERDNTSCPEW MDDFEADPKG KYAQNLLKKL IGGDVTPVDQ 200
    YMCGVDGKPI SAYAFLMAKD GITKLADVEA DVAARADDEG FITLKNNLYR 250
    LVWHVERKDV PYPKQSIFTI NSVVQKDGVE NTPPHYFTLG CKILTLTPRN 300
    KWSGVSDLSL KQKLLYTFYG KESLENPTYI YHSAFIECGS CGNDSWLTGN 350
    AIQGFACGCG ASYTANDVEV QSSGMIKPNA LLCATCPFAK GDSCSSNCKH 400
    SVAQLVSYLS ERCNVIADSK SFTLIFGGVA YAYFGCEEGT MYFVPRAKSV 450
    VSRIGDSIFT GCTGSWNKVT QIANMFLEQT QHSLNFVGEF VVNDVVLAIL 500
    SGTTTNVDKI RQLLKGVTLD KLRDYLADYD VAVTAGPFMD NAINVGGTGL 550
    QYAAITAPYV VLTGLGESFK KVATIPYKVC NSVKDTLTYY AHSVLYRVFP 600
    YDMDSGVSSF SELLFDCVDL SVASTYFLVR LLQDKTGDFM STIITSCQTA 650
    VSKLLDTCFE ATEATFNFLL DLAGLFRIFL RNAYVYTSQG FVVVNGKVST 700
    LVKQVLDLLN KGMQLLHTKV SWAGSNISAV IYSGRESLIF PSGTYYCVTT 750
    KAKSVQQDLD VILPGEFSKK QLGLLQPTDN STTVSVTVSS NMVETVVGQL 800
    EQTNMHSPDV IVGDYVIISE KLFVRSKEED GFAFYPACTN GHAVPTLFRL 850
    KGGAPVKKVA FGGDQVHEVA AVRSVTVEYN IHAVLDTLLA SSSLRTFVVD 900
    KSLSIEEFAD VVKEQVSDLL VKLLRGMPIP DFDLDDFIDA PCYCFNAEGD 950
    ASWSSTMIFS LHPVECDEEC SEVEASDLEE GESECISETS TEQVDVSHEI 1000
    SDDEWAAAVD EAFPLDEAED VTESVQEEAQ PVEVPVEDIA QVVIADTLQE 1050
    TPVVSDTVEV PPQVVKLPSE PQTIQPEVKE VAPVYEADTE QTQSVTVKPK 1100
    RLRKKRNVDP LSNFEHKVIT ECVTIVLGDA IQVAKCYGES VLVNAANTHL 1150
    KHGGGIAGAI NAASKGAVQK ESDEYILAKG PLQVGDSVLL QGHSLAKNIL 1200
    HVVGPDARAK QDVSLLSKCY KAMNAYPLVV TPLVSAGIFG VKPAVSFDYL 1250
    IREAKTRVLV VVNSQDVYKS LTIVDIPQSL TFSYDGLRGA IRKAKDYGFT 1300
    VFVCTDNSAN TKVLRNKGVD YTKKFLTVDG VQYYCYTSKD TLDDILQQAN 1350
    KSVGIISMPL GYVSHGLDLI QAGSVVRRVN VPYVCLLANK EQEAILMSED 1400
    VKLNPSEDFI KHVRTNGGYN SWHLVEGELL VQDLRLNKLL HWSDQTICYK 1450
    DSVFYVVKNS TAFPFETLSA CRAYLDSRTT QQLTIEVLVT VDGVNFRTVV 1500
    LNNKNTYRSQ LGCVFFNGAD ISDTIPDEKQ NGHSLYLADN LTADETKALK 1550
    ELYGPVDPTF LHRFYSLKAA VHKWKMVVCD KVRSLKLSDN NCYLNAVIMT 1600
    LDLLKDIKFV IPALQHAFMK HKGGDSTDFI ALIMAYGNCT FGAPDDASRL 1650
    LHTVLAKAEL CCSARMVWRE WCNVCGIKDV VLQGLKACCY VGVQTVEDLR 1700
    ARMTYVCQCG GERHRQIVEH TTPWLLLSGT PNEKLVTTST APDFVAFNVF 1750
    QGIETAVGHY VHARLKGGLI LKFDSGTVSK TSDWKCKVTD VLFPGQKYSS 1800
    DCNVVRYSLD GNFRTEVDPD LSAFYVKDGK YFTSEPPVTY SPATILAGSV 1850
    YTNSCLVSSD GQPGGDAISL SFNNLLGFDS SKPVTKKYTY SFLPKEDGDV 1900
    LLAEFDTYDP IYKNGAMYKG KPILWVNKAS YDTNLNKFNR ASLRQIFDVA 1950
    PIELENKFTP LSVESTPVEP PTVDVVALQQ EMTIVKCKGL NKPFVKDNVS 2000
    FVADDSGTPV VEYLSKEDLH TLYVDPKYQV IVLKDNVLSS MLRLHTVESG 2050
    DINVVAASGS LTRKVKLLFR ASFYFKEFAT RTFTATTAVG SCIKSVVRHL 2100
    GVTKGILTGC FSFVKMLFML PLAYFSDSKL GTTEVKVSAL KTAGVVTGNV 2150
    VKQCCTAAVD LSMDKLRRVD WKSTLRLLLM LCTTMVLLSS VYHLYVFNQV 2200
    LSSDVMFEDA QGLKKFYKEV RAYLGISSAC DGLASAYRAN SFDVPTFCAN 2250
    RSAMCNWCLI SQDSITHYPA LKMVQTHLSH YVLNIDWLWF AFETGLAYML 2300
    YTSAFNWLLL AGTLHYFFAQ TSIFVDWRSY NYAVSSAFWL FTHIPMAGLV 2350
    RMYNLLACLW LLRKFYQHVI NGCKDTACLL CYKRNRLTRV EASTVVCGGK 2400
    RTFYITANGG ISFCRRHNWN CVDCDTAGVG NTFICEEVAN DLTTALRRPI 2450
    NATDRSHYYV DSVTVKETVV QFNYRRDGQP FYERFPLCAF TNLDKLKFKE 2500
    VCKTTTGIPE YNFIIYDSSD RGQESLARSA CVYYSQVLCK SILLVDSSLV 2550
    TSVGDSSEIA TKMFDSFVNS FVSLYNVTRD KLEKLISTAR DGVRRGDNFH 2600
    SVLTTFIDAA RGPAGVESDV ETNEIVDSVQ YAHKHDIQIT NESYNNYVPS 2650
    YVKPDSVSTS DLGSLIDCNA ASVNQIVLRN SNGACIWNAA AYMKLSDALK 2700
    RQIRIACRKC NLAFRLTTSK LRANDNILSV RFTANKIVGG APTWFNALRD 2750
    FTLKGYVLAT IIVFLCAVLM YLCLPTFSMV PVEFYEDRIL DFKVLDNGII 2800
    RDVNPDDKCF ANKHRSFTQW YHEHVGGVYD NSITCPLTVA VIAGVAGARI 2850
    PDVPTTLAWV NNQIIFFVSR VFANTGSVCY TPIDEIPYKS FSDSGCILPS 2900
    ECTMFRDAEG RMTPYCHDPT VLPGAFAYSQ MRPHVRYDLY DGNMFIKFPE 2950
    VVFESTLRIT RTLSTQYCRF GSCEYAQEGV CITTNGSWAI FNDHHLNRPG 3000
    VYCGSDFIDI VRRLAVSLFQ PITYFQLTTS LVLGIGLCAF LTLLFYYINK 3050
    VKRAFADYTQ CAVIAVVAAV LNSLCICFVA SIPLCIVPYT ALYYYATFYF 3100
    TNEPAFIMHV SWYIMFGPIV PIWMTCVYTV AMCFRHFFWV LAYFSKKHVE 3150
    VFTDGKLNCS FQDAASNIFV INKDTYAALR NSLTNDAYSR FLGLFNKYKY 3200
    FSGAMETAAY REAAACHLAK ALQTYSETGS DLLYQPPNCS ITSGVLQSGL 3250
    VKMSHPSGDV EACMVQVTCG SMTLNGLWLD NTVWCPRHVM CPADQLSDPN 3300
    YDALLISMTN HSFSVQKHIG APANLRVVGH AMQGTLLKLT VDVANPSTPA 3350
    YTFTTVKPGA AFSVLACYNG RPTGTFTVVM RPNYTIKGSF LCGSCGSVGY 3400
    TKEGSVINFC YMHQMELANG THTGSAFDGT MYGAFMDKQV HQVQLTDKYC 3450
    SVNVVAWLYA AILNGCAWFV KPNRTSVVSF NEWALANQFT EFVGTQSVDM 3500
    LAVKTGVAIE QLLYAIQQLY TGFQGKQILG STMLEDEFTP EDVNMQIMGV 3550
    VMQSGVRKVT YGTAHWLFAT LVSTYVIILQ ATKFTLWNYL FETIPTQLFP 3600
    LLFVTMAFVM LLVKHKHTFL TLFLLPVAIC LTYANIVYEP TTPISSALIA 3650
    VANWLAPTNA YMRTTHTDIG VYISMSLVLV IVVKRLYNPS LSNFALALCS 3700
    GVMWLYTYSI GEASSPIAYL VFVTTLTSDY TITVFVTVNL AKVCTYAIFA 3750
    YSPQLTLVFP EVKMILLLYT CLGFMCTCYF GVFSLLNLKL RAPMGVYDFK 3800
    VSTQEFRFMT ANNLTAPRNS WEAMALNFKL IGIGGTPCIK VAAMQSKLTD 3850
    LKCTSVVLLS VLQQLHLEAN SRAWAFCVKC HNDILAATDP SEAFEKFVSL 3900
    FATLMTFSGN VDLDALASDI FDTPSVLQAT LSEFSHLATF AELEAAQKAY 3950
    QEAMDSGDTS PQVLKALQKA VNIAKNAYEK DKAVARKLER MADQAMTSMY 4000
    KQARAEDKKA KIVSAMQTML FGMIKKLDND VLNGIISNAR NGCIPLSVIP 4050
    LCASNKLRVV IPDFTVWNQV VTYPSLNYAG ALWDITVINN VDNEIVKSSD 4100
    VVDSNENLTW PLVLECTRAS TSAVKLQNNE IKPSGLKTMV VSAGQEQTNC 4150
    NTSSLAYYEP VQGRKMLMAL LSDNAYLKWA RVEGKDGFVS VELQPPCKFL 4200
    IAGPKGPEIR YLYFVKNLNN LHRGQVLGHI AATVRLQAGS NTEFASNSSV 4250
    LSLVNFTVDP QKAYLDFVNA GGAPLTNCVK MLTPKTGTGI AISVKPESTA 4300
    DQETYGGASV CLYCRAHIEH PDVSGVCKYK GKFVQIPAQC VRDPVGFCLS 4350
    NTPCNVCQYW IGYGCNCDSL RQAALPQSKD SNFLNESGVL L 4391

    Note: Produced by conventional translation.

    Length:4,391
    Mass (Da):486,059
    Last modified:March 6, 2013 - v1
    Checksum:iD0A87AE59773BBB8
    GO
    Isoform Replicase polyprotein 1ab (identifier: K9N7C7-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry K9N7C7.
    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:7,078
    Mass (Da):789,563
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    KC164505 Genomic RNA. Translation: AFY13305.1.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    KC164505 Genomic RNA. Translation: AFY13305.1 .

    3D structure databases

    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. "The phylogenetic status and pathogenicity of a new isolate of Metarhizium sp. from a fruit beetle larvae in Japan."
      Nishi O., Iiyama K., Yasunaga-Aoki C., Shimizu S.
      Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiR1A_CVEMC
    AccessioniPrimary (citable) accession number: K9N638
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2013
    Last sequence update: March 6, 2013
    Last modified: October 1, 2014
    This is version 16 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    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