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P0C6V2

- R1A_CVPPU

UniProt

P0C6V2 - R1A_CVPPU

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Porcine transmissible gastroenteritis coronavirus (strain Purdue) (TGEV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 49 (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-|-[SAGC]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK.
    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
    Sitei879 – 8802Cleavage; by PL1-PROBy similarity
    Active sitei1093 – 10931For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1244 – 12441For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1588 – 15881For PL2-PRO activityPROSITE-ProRule annotation
    Active sitei1741 – 17411For PL2-PRO activityPROSITE-ProRule annotation
    Sitei2388 – 23892Cleavage; by PL2-PROBy similarity
    Sitei2878 – 28792Cleavage; by 3CL-PROBy similarity
    Active sitei2919 – 29191For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3022 – 30221For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3180 – 31812Cleavage; by 3CL-PROBy similarity
    Sitei3474 – 34752Cleavage; by 3CL-PROBy similarity
    Sitei3557 – 35582Cleavage; by 3CL-PROBy similarity
    Sitei3752 – 37532Cleavage; by 3CL-PROBy similarity
    Sitei3863 – 38642Cleavage; by 3CL-PROBy similarity
    Sitei3998 – 39992Cleavage; by 3CL-PROBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1164 – 119532C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri3937 – 395317By similarityAdd
    BLAST
    Zinc fingeri3979 – 399214By 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
    OrganismiPorcine transmissible gastroenteritis coronavirus (strain Purdue) (TGEV)
    Taxonomic identifieri11151 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
    Virus hostiSus scrofa (Pig) [TaxID: 9823]
    ProteomesiUP000001440: 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 – 40174017Replicase polyprotein 1aPRO_0000338302Add
    BLAST
    Chaini1 – 110110Non-structural protein 1By similarityPRO_0000338303Add
    BLAST
    Chaini111 – 879769Non-structural protein 2By similarityPRO_0000338304Add
    BLAST
    Chaini880 – 23881509Non-structural protein 3By similarityPRO_0000338305Add
    BLAST
    Chaini2389 – 2878490Non-structural protein 4By similarityPRO_0000338306Add
    BLAST
    Chaini2879 – 31803023C-like proteinasePRO_0000338307Add
    BLAST
    Chaini3181 – 3474294Non-structural protein 6By similarityPRO_0000338308Add
    BLAST
    Chaini3475 – 355783Non-structural protein 7By similarityPRO_0000338309Add
    BLAST
    Chaini3558 – 3752195Non-structural protein 8By similarityPRO_0000338310Add
    BLAST
    Chaini3753 – 3863111Non-structural protein 9PRO_0000338311Add
    BLAST
    Chaini3864 – 3998135Non-structural protein 10By similarityPRO_0000338312Add
    BLAST
    Chaini3999 – 401719Non-structural protein 11Sequence AnalysisPRO_0000338313Add
    BLAST

    Post-translational modificationi

    Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO is autocatalytically processed.1 Publication

    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
    4017
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107
    Helixi23 – 3614
    Beta strandi41 – 455
    Helixi46 – 516
    Beta strandi59 – 7517
    Beta strandi84 – 907
    Beta strandi96 – 1049
    Beta strandi1077 – 10804
    Beta strandi1083 – 10864
    Helixi1093 – 110210
    Helixi1111 – 11166
    Turni1117 – 11193
    Helixi1122 – 113211
    Helixi1142 – 11509
    Beta strandi1156 – 11649
    Beta strandi1167 – 118014
    Beta strandi1183 – 11853
    Beta strandi1187 – 11915
    Turni1193 – 11953
    Beta strandi1198 – 121720
    Helixi1223 – 12253
    Beta strandi1226 – 12283
    Beta strandi1231 – 12388
    Turni1240 – 12423
    Beta strandi1244 – 12496
    Turni1250 – 12534
    Beta strandi1254 – 12574
    Beta strandi1260 – 12623
    Beta strandi1269 – 128012
    Turni2889 – 28913
    Helixi2892 – 28943
    Beta strandi2895 – 29006
    Beta strandi2903 – 29108
    Beta strandi2913 – 29175
    Helixi2918 – 29214
    Helixi2931 – 29366
    Helixi2940 – 29423
    Beta strandi2943 – 29486
    Beta strandi2950 – 29523
    Beta strandi2954 – 29607
    Beta strandi2963 – 29708
    Beta strandi2988 – 29958
    Beta strandi2998 – 30069
    Beta strandi3025 – 30306
    Beta strandi3033 – 304311
    Beta strandi3049 – 30524
    Helixi3059 – 30613
    Helixi3078 – 309013
    Helixi3104 – 31118
    Turni3112 – 31154
    Helixi3123 – 31253
    Helixi3126 – 31327
    Helixi3136 – 314611
    Beta strandi3158 – 31603
    Helixi3167 – 31759

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LVOX-ray1.96A/B/C/D/E/F2879-3180[»]
    1P9UX-ray2.37A/B/C/D/E/F2879-3180[»]
    2AMPX-ray2.70A/B2879-3180[»]
    3MP2X-ray2.50A1071-1281[»]
    3ZBDX-ray1.49A/B1-105[»]
    4F49X-ray2.25A/B/C/D2879-3181[»]
    ProteinModelPortaliP0C6V2.
    SMRiP0C6V2. Positions 2879-3179, 3869-3994.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C6V2.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1896 – 191621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1995 – 201521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2033 – 205321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2401 – 242121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2467 – 248721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2497 – 251721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2538 – 255821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2666 – 268621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2695 – 271521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2721 – 274121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2746 – 276621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3187 – 320721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3217 – 323721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3242 – 326221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3280 – 330021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3313 – 333321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3347 – 336721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3371 – 339121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3394 – 341421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1055 – 1299245Peptidase C16 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1318 – 1489172MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1550 – 1803254Peptidase C16 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2879 – 3180302Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1896 – 2053158HD1Add
    BLAST
    Regioni2401 – 2766366HD2Add
    BLAST
    Regioni3187 – 3414228HD3Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi932 – 1042111Glu-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.

    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 fingeri1164 – 119532C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri3937 – 395317By similarityAdd
    BLAST
    Zinc fingeri3979 – 399214By 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. 2 hits.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF08715. Viral_protease. 2 hits.
    [Graphical view]
    SMARTiSM00506. A1pp. 1 hit.
    [Graphical view]
    SUPFAMiSSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 2 hits.
    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: P0C6V2-1) [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

    MSSKQFKILV NEDYQVNVPS LPIRDVLQEI KYCYRNGFEG YVFVPEYCRD     50
    LVDCDRKDHY VIGVLGNGVS DLKPVLLTEP SVMLQGFIVR ANCNGVLEDF 100
    DLKIARTGRG AIYVDQYMCG ADGKPVIEGD FKDYFGDEDI IEFEGEEYHC 150
    AWTTVRDEKP LNQQTLFTIQ EIQYNLDIPH KLPNCATRHV APPVKKNSKI 200
    VLSEDYKKLY DIFGSPFMGN GDCLSKCFDT LHFIAATLRC PCGSESSGVG 250
    DWTGFKTACC GLSGKVKGVT LGDIKPGDAV VTSMSAGKGV KFFANCVLQY 300
    AGDVEGVSIW KVIKTFTVDE TVCTPGFEGE LNDFIKPESK SLVACSVKRA 350
    FITGDIDDAV HDCIITGKLD LSTNLFGNVG LLFKKTPWFV QKCGALFVDA 400
    WKVVEELCGS LTLTYKQIYE VVASLCTSAF TIVNYKPTFV VPDNRVKDLV 450
    DKCVKVLVKA FDVFTQIITI AGIEAKCFVL GAKYLLFNNA LVKLVSVKIL 500
    GKKQKGLECA FFATSLVGAT VNVTPKRTET ATISLNKVDD VVAPGEGYIV 550
    IVGDMAFYKS GEYYFMMSSP NFVLTNNVFK AVKVPSYDIV YDVDNDTKSK 600
    MIAKLGSSFE YDGDIDAAIV KVNELLIEFR QQSLCFRAFK DDKSIFVEAY 650
    FKKYKMPACL AKHIGLWNII KKDSCKRGFL NLFNHLNELE DIKETNIQAI 700
    KNILCPDPLL DLDYGAIWYN CMPGCSDPSV LGSVQLLIGN GVKVVCDGCK 750
    GFANQLSKGY NKLCNAARND IEIGGIPFST FKTPTNTFIE MTDAIYSVIE 800
    QGKALSFRDA DVPVVDNGTI STADWSEPIL LEPAEYVKPK NNGNVIVIAG 850
    YTFYKDEDEH FYPYGFGKIV QRMYNKMGGG DKTVSFSEEV DVQEIAPVTR 900
    VKLEFEFDNE IVTGVLERAI GTRYKFTGTT WEEFEESISE ELDAIFDTLA 950
    NQGVELEGYF IYDTCGGFDI KNPDGIMISQ YDINITADEK SEVSASSEEE 1000
    EVESVEEDPE NEIVEASEGA EGTSSQEEVE TVEVADITST EEDVDIVEVS 1050
    AKDDPWAAAV DVQEAEQFNP SLPPFKTTNL NGKIILKQGD NNCWINACCY 1100
    QLQAFDFFNN EAWEKFKKGD VMDFVNLCYA ATTLARGHSG DAEYLLELML 1150
    NDYSTAKIVL AAKCGCGEKE IVLERAVFKL TPLKESFNYG VCGDCMQVNT 1200
    CRFLSVEGSG VFVHDILSKQ TPEAMFVVKP VMHAVYTGTT QNGHYMVDDI 1250
    EHGYCVDGMG IKPLKKRCYT STLFINANVM TRAEKPKQEF KVEKVEQQPI 1300
    VEENKSSIEK EEIQSPKNDD LILPFYKAGK LSFYQGALDV LINFLEPDVI 1350
    VNAANGDLKH MGGVARAIDV FTGGKLTERS KDYLKKNKSI APGNAVFFEN 1400
    VIEHLSVLNA VGPRNGDSRV EAKLCNVYKA IAKCEGKILT PLISVGIFNV 1450
    RLETSLQCLL KTVNDRGLNV FVYTDQERQT IENFFSCSIP VNVTEDNVNH 1500
    ERVSVSFDKT YGEQLKGTVV IKDKDVTNQL PSAFDVGQKV IKAIDIDWQA 1550
    HYGFRDAAAF SASSHDAYKF EVVTHSNFIV HKQTDNNCWI NAICLALQRL 1600
    KPQWKFPGVR GLWNEFLERK TQGFVHMLYH ISGVKKGEPG DAELMLHKLG 1650
    DLMDNDCEII VTHTTACDKC AKVEKFVGPV VAAPLAIHGT DETCVHGVSV 1700
    NVKVTQIKGT VAITSLIGPI IGEVLEATGY ICYSGSNRNG HYTYYDNRNG 1750
    LVVDAEKAYH FNRDLLQVTT AIASNFVVKK PQAEERPKNC AFNKVAASPK 1800
    IVQEQKLLAI ESGANYALTE FGRYADMFFM AGDKILRLLL EVFKYLLVLF 1850
    MCLRSTKMPK VKVKPPLAFK DFGAKVRTLN YMRQLNKPSV WRYAKLVLLL 1900
    IAIYNFFYLF VSIPVVHKLT CNGAVQAYKN SSFIKSAVCG NSILCKACLA 1950
    SYDELADFQH LQVTWDFKSD PLWNRLVQLS YFAFLAVFGN NYVRCFLMYF 2000
    VSQYLNLWLS YFGYVEYSWF LHVVNFESIS AEFVIVVIVV KAVLALKHIV 2050
    FACSNPSCKT CSRTARQTRI PIQVVVNGSM KTVYVHANGT GKFCKKHNFY 2100
    CKNCDSYGFE NTFICDEIVR DLSNSVKQTV YATDRSHQEV TKVECSDGFY 2150
    RFYVGDEFTS YDYDVKHKKY SSQEVLKSML LLDDFIVYSP SGSALANVRN 2200
    ACVYFSQLIG KPIKIVNSDL LEDLSVDFKG ALFNAKKNVI KNSFNVDVSE 2250
    CKNLDECYRA CNLNVSFSTF EMAVNNAHRF GILITDRSFN NFWPSKVKPG 2300
    SSGVSAMDIG KCMTSDAKIV NAKVLTQRGK SVVWLSQDFA ALSSTAQKVL 2350
    VKTFVEEGVN FSLTFNAVGS DDDLPYERFT ESVSPKSGSG FFDVITQLKQ 2400
    IVILVFVFIF ICGLCSVYSV ATQSYIESAE GYDYMVIKNG IVQPFDDTIS 2450
    CVHNTYKGFG DWFKAKYGFI PTFGKSCPIV VGTVFDLENM RPIPDVPAYV 2500
    SIVGRSLVFA INAAFGVTNM CYDHTGNAVS KDSYFDTCVF NTACTTLTGL 2550
    GGTIVYCAKQ GLVEGAKLYS DLMPDYYYEH ASGNMVKLPA IIRGLGLRFV 2600
    KTQATTYCRV GECIDSKAGF CFGGDNWFVY DNEFGNGYIC GNSVLGFFKN 2650
    VFKLFNSNMS VVATSGAMLV NIIIACLAIA MCYGVLKFKK IFGDCTFLIV 2700
    MIIVTLVVNN VSYFVTQNTF FMIIYAIVYY FITRKLAYPG ILDAGFIIAY 2750
    INMAPWYVIT AYILVFLYDS LPSLFKLKVS TNLFEGDKFV GNFESAAMGT 2800
    FVIDMRSYET IVNSTSIARI KSYANSFNKY KYYTGSMGEA DYRMACYAHL 2850
    GKALMDYSVN RTDMLYTPPT VSVNSTLQSG LRKMAQPSGL VEPCIVRVSY 2900
    GNNVLNGLWL GDEVICPRHV IASDTTRVIN YENEMSSVRL HNFSVSKNNV 2950
    FLGVVSARYK GVNLVLKVNQ VNPNTPEHKF KSIKAGESFN ILACYEGCPG 3000
    SVYGVNMRSQ GTIKGSFIAG TCGSVGYVLE NGILYFVYMH HLELGNGSHV 3050
    GSNFEGEMYG GYEDQPSMQL EGTNVMSSDN VVAFLYAALI NGERWFVTNT 3100
    SMSLESYNTW AKTNSFTELS STDAFSMLAA KTGQSVEKLL DSIVRLNKGF 3150
    GGRTILSYGS LCDEFTPTEV IRQMYGVNLQ AGKVKSFFYP IMTAMTILFA 3200
    FWLEFFMYTP FTWINPTFVS IVLAVTTLIS TVFVSGIKHK MLFFMSFVLP 3250
    SVILVTAHNL FWDFSYYESL QSIVENTNTM FLPVDMQGVM LTVFCFIVFV 3300
    TYSVRFFTCK QSWFSLAVTT ILVIFNMVKI FGTSDEPWTE NQIAFCFVNM 3350
    LTMIVSLTTK DWMVVIASYR IAYYIVVCVM PSAFVSDFGF MKCISIVYMA 3400
    CGYLFCCYYG ILYWVNRFTC MTCGVYQFTV SAAELKYMTA NNLSAPKNAY 3450
    DAMILSAKLI GVGGKRNIKI STVQSKLTEM KCTNVVLLGL LSKMHVESNS 3500
    KEWNYCVGLH NEINLCDDPE IVLEKLLALI AFFLSKHNTC DLSELIESYF 3550
    ENTTILQSVA SAYAALPSWI ALEKARADLE EAKKNDVSPQ ILKQLTKAFN 3600
    IAKSDFEREA SVQKKLDKMA EQAAASMYKE ARAVDRKSKI VSAMHSLLFG 3650
    MLKKLDMSSV NTIIDQARNG VLPLSIIPAA SATRLVVITP SLEVFSKIRQ 3700
    ENNVHYAGAI WTIVEVKDAN GSHVHLKEVT AANELNLTWP LSITCERTTK 3750
    LQNNEIMPGK LKERAVRASA TLDGEAFGSG KALMASESGK SFMYAFIASD 3800
    NNLKYVKWES NNDIIPIELE APLRFYVDGA NGPEVKYLYF VKNLNTLRRG 3850
    AVLGYIGATV RLQAGKPTEH PSNSSLLTLC AFSPDPAKAY VDAVKRGMQP 3900
    VNNCVKMLSN GAGNGMAVTN GVEANTQQDS YGGASVCIYC RCHVEHPAID 3950
    GLCRYKGKFV QIPTGTQDPI RFCIENEVCV VCGCWLNNGC MCDRTSMQSF 4000
    TVDQSYLNEC GVLVQLD 4017

    Note: Produced by conventional translation.

    Length:4,017
    Mass (Da):447,352
    Last modified:June 10, 2008 - v1
    Checksum:i97ED2B170C4FD248
    GO
    Isoform Replicase polyprotein 1ab (identifier: P0C6Y5-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry P0C6Y5.
    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:6,684
    Mass (Da):748,912
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti572 – 5721F → S in strain: Isolate Purdue-115.
    Natural varianti1041 – 10411E → D in strain: Isolate Purdue-115.
    Natural varianti2375 – 23751P → T in strain: Isolate Purdue-115.
    Natural varianti2381 – 23811E → Q in strain: Isolate Purdue-115.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z34093 mRNA. Translation: CAA83979.1.
    AJ271965 Genomic RNA. Translation: CAB91144.1.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z34093 mRNA. Translation: CAA83979.1 .
    AJ271965 Genomic RNA. Translation: CAB91144.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LVO X-ray 1.96 A/B/C/D/E/F 2879-3180 [» ]
    1P9U X-ray 2.37 A/B/C/D/E/F 2879-3180 [» ]
    2AMP X-ray 2.70 A/B 2879-3180 [» ]
    3MP2 X-ray 2.50 A 1071-1281 [» ]
    3ZBD X-ray 1.49 A/B 1-105 [» ]
    4F49 X-ray 2.25 A/B/C/D 2879-3181 [» ]
    ProteinModelPortali P0C6V2.
    SMRi P0C6V2. Positions 2879-3179, 3869-3994.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P0C6V2.

    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. 2 hits.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF08715. Viral_protease. 2 hits.
    [Graphical view ]
    SMARTi SM00506. A1pp. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 2 hits.
    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. "Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus."
      Eleouet J., Rasschaert D., Lambert P., Levy L., Vende P., Laude H.
      Virology 206:817-822(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Isolate Purdue-115.
    2. "Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome."
      Almazan F., Gonzalez J.M., Penzes Z., Izeta A., Calvo E., Plana-Duran J., Enjuanes L.
      Proc. Natl. Acad. Sci. U.S.A. 97:5516-5521(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate PUR46-MAD.
    3. "Conservation of substrate specificities among coronavirus main proteases."
      Hegyi A., Ziebuhr J.
      J. Gen. Virol. 83:595-599(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
      Strain: Isolate Purdue-115.
    4. "Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain."
      Anand K., Palm G.J., Mesters J.R., Siddell S.G., Ziebuhr J., Hilgenfeld R.
      EMBO J. 21:3213-3224(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 2879-3180.
    5. "Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs."
      Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., Hilgenfeld R.
      Science 300:1763-1767(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 2879-3180 COMPLEXED WITH THE SUBSTRATE-ANALOG HEXAPEPTIDYL CMK.

    Entry informationi

    Entry nameiR1A_CVPPU
    AccessioniPrimary (citable) accession number: P0C6V2
    Secondary accession number(s): Q9IW06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 49 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