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P0C6U4

- R1A_CVHN2

UniProt

P0C6U4 - R1A_CVHN2

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Human coronavirus HKU1 (isolate N2) (HCoV-HKU1)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    The papain-like proteinase 1 (PL1-PRO) and papain-like proteinase 2 (PL2-PRO) 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. 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
    Sitei222 – 2232Cleavage; by PL1-PROBy similarity
    Sitei809 – 8102Cleavage; by PL1-PROBy similarity
    Active sitei1131 – 11311For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1282 – 12821For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1727 – 17271For PL2-PRO activityPROSITE-ProRule annotation
    Active sitei1884 – 18841For PL2-PRO activityPROSITE-ProRule annotation
    Sitei2808 – 28092Cleavage; by PL2-PROBy similarity
    Sitei3304 – 33052Cleavage; by 3CL-PROBy similarity
    Active sitei3345 – 33451For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3449 – 34491For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3607 – 36082Cleavage; by 3CL-PROBy similarity
    Sitei3894 – 38952Cleavage; by 3CL-PROBy similarity
    Sitei3986 – 39872Cleavage; by 3CL-PROBy similarity
    Sitei4180 – 41812Cleavage; by 3CL-PROBy similarity
    Sitei4290 – 42912Cleavage; by 3CL-PROBy similarity
    Sitei4427 – 44282Cleavage; by 3CL-PROBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1208 – 123629C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1805 – 184137C4-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4364 – 438017By similarityAdd
    BLAST
    Zinc fingeri4406 – 441914By similarityAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

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

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Replicase polyprotein 1a
    Short name:
    pp1a
    Alternative name(s):
    ORF1a polyprotein
    Cleaved into the following 11 chains:
    Non-structural protein 1
    Short name:
    nsp1
    Alternative name(s):
    p28
    Non-structural protein 2
    Short name:
    nsp2
    Alternative name(s):
    p65
    Alternative name(s):
    PL1-PRO/PL2-PRO
    PL1/PL2
    Papain-like proteinases 1/2
    p210
    Non-structural protein 4
    Short name:
    nsp4
    Alternative name(s):
    Peptide HD2
    p44
    3C-like proteinase (EC:3.4.22.-)
    Short name:
    3CL-PRO
    Short name:
    3CLp
    Alternative name(s):
    M-PRO
    nsp5
    p27
    Non-structural protein 6
    Short name:
    nsp6
    Non-structural protein 7
    Short name:
    nsp7
    Alternative name(s):
    p10
    Non-structural protein 8
    Short name:
    nsp8
    Alternative name(s):
    p22
    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
    p15
    Non-structural protein 11
    Short name:
    nsp11
    Gene namesi
    ORF Names:1a
    OrganismiHuman coronavirus HKU1 (isolate N2) (HCoV-HKU1)
    Taxonomic identifieri443240 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000006551: 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.
    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.
    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.
    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.

    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 – 44414441Replicase polyprotein 1aPRO_0000338206Add
    BLAST
    Chaini1 – 222222Non-structural protein 1By similarityPRO_0000338207Add
    BLAST
    Chaini223 – 809587Non-structural protein 2By similarityPRO_0000338208Add
    BLAST
    Chaini810 – 28081999Non-structural protein 3By similarityPRO_0000338209Add
    BLAST
    Chaini2809 – 3304496Non-structural protein 4By similarityPRO_0000338210Add
    BLAST
    Chaini3305 – 36073033C-like proteinaseBy similarityPRO_0000338211Add
    BLAST
    Chaini3608 – 3894287Non-structural protein 6By similarityPRO_0000338212Add
    BLAST
    Chaini3895 – 398692Non-structural protein 7By similarityPRO_0000338213Add
    BLAST
    Chaini3987 – 4180194Non-structural protein 8By similarityPRO_0000338214Add
    BLAST
    Chaini4181 – 4290110Non-structural protein 9By similarityPRO_0000338215Add
    BLAST
    Chaini4291 – 4427137Non-structural protein 10By similarityPRO_0000338216Add
    BLAST
    Chaini4428 – 444114Non-structural protein 11Sequence AnalysisPRO_0000338217Add
    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

    ProteinModelPortaliP0C6U4.
    SMRiP0C6U4. Positions 4022-4172, 4296-4420.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2196 – 221621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2257 – 227721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2288 – 230821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2371 – 239121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2413 – 243321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2814 – 283421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3089 – 310921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3121 – 314121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3148 – 316821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3173 – 319321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3621 – 364121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3646 – 366621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3671 – 369121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3714 – 373421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3742 – 376221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3770 – 379021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3813 – 383321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati945 – 954101
    Repeati955 – 964102
    Repeati965 – 974103
    Repeati975 – 984104
    Repeati985 – 994105
    Repeati995 – 1004106
    Repeati1005 – 1014107
    Repeati1015 – 1024108
    Repeati1025 – 1034109
    Repeati1035 – 10441010
    Repeati1045 – 10541011
    Domaini1093 – 1343251Peptidase C16 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1321 – 1492172MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1688 – 1948261Peptidase C16 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini3305 – 3607303Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni945 – 105411011 X 10 AA tandem repeat of N-[DN]-D-E-D-V-V-T-G-DAdd
    BLAST
    Regioni2196 – 2433238HD1By similarityAdd
    BLAST
    Regioni2814 – 3193380HD2By similarityAdd
    BLAST
    Regioni3621 – 3833213HD3By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi934 – 1086153Asp-richAdd
    BLAST
    Compositional biasi2199 – 229193Phe-richAdd
    BLAST
    Compositional biasi2586 – 25894Poly-Val

    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 fingeri1208 – 123629C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1805 – 184137C4-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4364 – 438017By similarityAdd
    BLAST
    Zinc fingeri4406 – 441914By similarityAdd
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    InterProiIPR022570. Coronavirus_NSP1.
    IPR002589. Macro_dom.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR002705. Pept_C30/C16_B_coronavir.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view]
    PfamiPF11963. DUF3477. 1 hit.
    PF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF01831. Peptidase_C16. 1 hit.
    PF05409. Peptidase_C30. 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. 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: P0C6U4-1) [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

    MIKTSKYGLG FKWAPEFRWL LPDAAEELAS PMKSDEGGLC PSTGQAMESV     50
    GFVYDNHVKI DCRCILGQEW HVQSNLIRDI FVHEDLHVVE VLTKTAVKSG 100
    TAILIKSPLH SLGGFPKGYV MGLFRSYKTK RYVVHHLSMT TSTTNFGEDF 150
    LGWIVPFGFM PSYVHKWFQF CRLYIEESDL IISNFKFDDY DFSVEDAYAE 200
    VHAEPKGKYS QKAYALLRQY RGIKPVLFVD QYGCDYSGKL ADCLQAYGHY 250
    SLQDMRQKQS VWLANCDFDI VVAWHVVRDS RFVMRLQTIA TICGIKYVAQ 300
    PTEDVVDGAV VIREPVHLLS ADAIVLKLPS LMKVMTHMDD FSIKSIYNVD 350
    LCDCGFVMQY GYVDCFNDNC DFYGWVSGNM MDGFSCPLCC TVYDSSEVKA 400
    QSSGVIPENP VLFTNSTDTV NPDSFNLYGY SVTPFGSCIY WSPRPGLWIP 450
    IIKSSVKSYD DLVYSGVVGC KSIVKETALI THALYLDYVQ CKCGNLEQNH 500
    ILGVNNSWCR QLLLNRGDYN MLLKNIDLFV KRRADFACKF AVCGDGFVPF 550
    LLDGLIPRSY YLIQSGIFFT SLMSQFSQEV SDMCLKMCIL FMDRVSVATF 600
    YIEHYVNRLV TQFKLLGTTL VNKMVNWFNT MLDASAPATG WLLYQLLNGL 650
    FVVSQANFNF VALIPDYAKI LVNKFYTFFK LLLECVTVDV LKDMPVLKTI 700
    NGLVCIVGNK FYNVSTGLIP GFVLPCNAQE QQIYFFEGVA ESVIVEDDVI 750
    ENVKSSLSSY EYCQPPKSVE KICIIDNMYM GKCGDKFFPI VMNDKNICLL 800
    DQAWRFPCAG RKVNFNEKPV VMEIPSLMTV KVMFDLDSTF DDILGKVCSE 850
    FEVEKGVTVD DFVAVVCDAI ENALNSCKDH PVVGYQVRAF LNKLNENVVY 900
    LFDEAGDEAM ASRMYCTFAI EDVEDVISSE AVEDTIDGVV EDTINDDEDV 950
    VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV 1000
    VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV 1050
    VTGDNDDEEI VTGDNDDQIV VTGDDVDDIE SVYDFDTYKA LLVFNDVYND 1100
    ALFVSYGSSV ETETYFKVNG LWSPTITHTN CWLRSVLLVM QKLPFKFKDL 1150
    AIENMWLSYK VGYNQSFVDY LLTTIPKAIV LPQGGYVADF AYWFLNQFDI 1200
    NAYANWCCLK CGFSFDLNGL DAVFFYGDIV SHVCKCGHNM TLIAADLPCT 1250
    LHFSLFDDNF CAFCTPKKIF IAACAVDVNV CHSVAVIGDE QIDGKFVTKF 1300
    SGDKFDFIVG YGMSFSMSSF ELAQLYGLCI TPNVCFVKGD IINVARLVKA 1350
    DVIVNPANGH MLHGGGVAKA IAVAAGKKFS KETAAMVKSK GVCQVGDCYV 1400
    STGGKLCKTI LNIVGPDARQ DGRQSYVLLA RAYKHLNNYD CCLSTLISAG 1450
    IFSVPADVSL TYLLGVVDKQ VILVSNNKED FDIIQKCQIT SVVGTKALAV 1500
    RLTANVGRVI KFETDAYKLF LSGDDCFVSN SSVIQEVLLL RHDIQLNNDV 1550
    RDYLLSKMTS LPKDWRLINK FDVINGVKTV KYFECPNSIY ICSQGKDFGY 1600
    VCDGSFYKAT VNQVCVLLAK KIDVLLTVDG VNFKSISLTV GEVFGKILGN 1650
    VFCDGIDVTK LKCSDFYADK ILYQYENLSL ADISAVQSSF GFDQQQLLAY 1700
    YNFLTVCKWS VVVNGPFFSF EQSHNNCYVN VACLMLQHIN LKFNKWQWQE 1750
    AWYEFRAGRP HRLVALVLAK GHFKFDEPSD ATDFIRVVLK QADLSGAICE 1800
    LELICDCGIK QESRVGVDAV MHFGTLAKTD LFNGYKIGCN CAGRIVHCTK 1850
    LNVPFLICSN TPLSKDLPDD VVAANMFMGV GVGHYTHLKC GSPYQHYDAC 1900
    SVKKYTGVSG CLTDCLYLKN LTQTFTSMLT NYFLDDVEMV AYNPDLSQYY 1950
    CDNGKYYTKP IIKAQFKPFA KVDGVYTNFK LVGHDICAQL NDKLGFNVDL 2000
    PFVEYKVTVW PVATGDVVLA SDDLYVKRYF KGCETFGKPV IWLCHDEASL 2050
    NSLTYFNKPS FKSENRYSVL SVDSVSEESQ GNVVTSVMES QISTKEVKLK 2100
    GVRKTVKIED AIIVNDENSS IKVVKSLSLV DVWDMYLTGC DYVVWVANEL 2150
    SRLVKSPTVR EYIRYGIKPI TIPIDLLCLR DDNQTLLVPK IFKARAIEFY 2200
    GFLKWLFIYV FSLLHFTNDK TIFYTTEIAS KFTFNLFCLA LKNAFQTFRW 2250
    SIFIKGFLVV ATVFLFWFNF LYINVIFSDF YLPNISVFPI FVGRIVMWIK 2300
    ATFGLVTICD FYSKLGVGFT SHFCNGSFIC ELCYSGFDML DTYAAIDFVQ 2350
    YEVDRRVLFD YVSLVKLIVE LVIGYSLYTV WFYPLFCLIG LQLFTTWLPD 2400
    LFMLETMHWL IRFIVFVANM LPAFVLLRFY IVVTAMYKVV GFIRHIVYGC 2450
    NKAGCLFCYK RNCSVRVKCS TIVGGVIRYY DITANGGTGF CVKHQWNCFN 2500
    CHSFKPGNTF ITVEAAIELS KELKRPVNPT DASHYVVTDI KQVGCMMRLF 2550
    YDRDGQRVYD DVDASLFVDI NNLLHSKVKV VPNLYVVVVE SDADRANFLN 2600
    AVVFYAQSLY RPILLVDKKL ITTACNGISV TQTMFDVYVD TFMSHFDVDR 2650
    KSFNNFVNIA HASLREGVQL EKVLDTFVGC VRKCCSIDSD VETRFITKSM 2700
    ISAVAAGLEF TDENYNNLVP TYLKSDNIVA ADLGVLIQNG AKHVQGNVAK 2750
    AANISCIWFI DTFNQLTADL QHKLKKACVK TGLKLKLTFN KQEASVPILT 2800
    TPFSLKGGVV LSNLLYILFF ISLICFILLW ALLPTYSVYK SDIHLPAYAS 2850
    FKVIDNGVVR DISVNDLCFA NKFFQFDQWY ESTFGSFYYH NSMDCPIVVA 2900
    VMDEDIGSTM FNVPTKVLRH GFHVLHFLTY AFASDSVQCY TPHIQISYND 2950
    FYASGCVLSS LCTMFKRGDG TPHPYCYSDG VMKNASLYTS LVPHTRYSLA 3000
    NSNGFIRFPD VISEGIVRIV RTRSMTYCRV GACEYAEEGI CFNFNSSWVL 3050
    NNDYYRSMPG TFCGRDLFDL FYQFFSSLIR PIDFFSLTAS SIFGAILAIV 3100
    VVLVFYYLIK LKRAFGDYTS VVVINVIVWC INFLMLFVFQ VYPICACVYA 3150
    CFYFYVTLYF PSEISVIMHL QWIVMYGAIM PFWFCVTYVA MVIANHVLWL 3200
    FSYCRKIGVN VCNDSTFEET SLTTFMITKD SYCRLKNSVS DVAYNRYLSL 3250
    YNKYRYYSGK MDTAAYREAA CSQLAKAMET FNHNNGNDVL YQPPTASVST 3300
    SFLQSGIVKM VSPTSKIEPC IVSVTYGSMT LNGLWLDDKV YCPRHVICLS 3350
    SNMNEPDYSA LLCRVTLGDF TIMSGRMSLT VVSYQMQGCQ LVLTVSLQNP 3400
    YTPKYTFGVV KPGETFTVLA AYNGRPQGAF HVTMRSSYTI KGSFLCGSCG 3450
    SVGYVLTGDS VKFVYMHQLE LSTGCHTGTD FTGNFYGPYR DAQVVQLPVK 3500
    DYVQTVNVIA WLYAAILNNC AWFVQNDVCS IEDFNVWAMT NGFSQVKADL 3550
    VLDALASMTG VSIETLLAAI KRLYMGFQGR QILGSCTFED ELAPSDVYQQ 3600
    LAGVKLQSKT KRFIKETIYW ILISTFLFSC IISAFVKWTI FMYINTHMIG 3650
    VTLCVLCFVS FMMLLVKHKH FYLTMYIIPV LCTLFYVNYL VVYKEGFRGL 3700
    TYVWLSYFVP AVNFTYVYEV FYGCILCVFA IFITMHSINH DIFSLMFLVG 3750
    RIVTLISMWY FGSNLEEDVL LFITAFLGTY TWTTILSLAI AKIVANWLSV 3800
    NIFYFTDVPY IKLILLSYLF IGYILSCYWG FFSLLNSVFR MPMGVYNYKI 3850
    SVQELRYMNA NGLRPPRNSF EAILLNLKLL GIGGVPVIEV SQIQSKLTDV 3900
    KCANVVLLNC LQHLHVASNS RLWQYCSILH NEILSTSDLS VAFDKLAQLL 3950
    IVLFANPAAV DTKCLASIDE VSDDYVQDST VLQALQSEFV NMASFVEYEV 4000
    AKKNLADAKN SGSVNQQQIK QLEKACNIAK SVYERDKAVA RKLERMADLA 4050
    LTNMYKEARI NDKKSKVVSA LQTMLFSMVR KLDNQALNSI LDNAVKGCVP 4100
    LNAIPALAAN TLTIIIPDKQ VFDKVVDNVY VAYAGSVWHI QTVQDADGIN 4150
    KQLTDISVDS NWPLVIIANR YNEVANAVMQ NNELMPHKLK IQVVNSGSDM 4200
    NCNIPTQCYY NNGSSGRIVY AVLSDVDGLK YTKIIKDDGN CVVLELDPPC 4250
    KFSIQDVKGL KIKYLYFIKG CNTLARGWVV GTLSSTIRLQ AGVATEYAAN 4300
    SSILSLCAFS VDPKKTYLDY IQQGGVPIIN CVKMLCDHAG TGMAITIKPE 4350
    ATINQDSYGG ASVCIYCRAR VEHPDVDGLC KLRGKFVQVP LGIKDPILYV 4400
    LTHDVCQVCG FWRDGSCSCV GSGVAVQSKD LNFLNGFGVL V 4441

    Note: Produced by conventional translation.

    Length:4,441
    Mass (Da):499,423
    Last modified:June 10, 2008 - v1
    Checksum:i9BED41AF10453162
    GO
    Isoform Replicase polyprotein 1ab (identifier: P0C6X3-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry P0C6X3.
    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:7,152
    Mass (Da):807,495
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY884001 Genomic RNA. No translation available.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY884001 Genomic RNA. No translation available.

    3D structure databases

    ProteinModelPortali P0C6U4.
    SMRi P0C6U4. Positions 4022-4172, 4296-4420.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR022570. Coronavirus_NSP1.
    IPR002589. Macro_dom.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR002705. Pept_C30/C16_B_coronavir.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view ]
    Pfami PF11963. DUF3477. 1 hit.
    PF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF01831. Peptidase_C16. 1 hit.
    PF05409. Peptidase_C30. 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. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Comparative analysis of 22 coronavirus HKU1 genomes reveals a novel genotype and evidence of natural recombination in coronavirus HKU1."
      Woo P.C.Y., Lau S.K.P., Yip C.C.Y., Huang Y., Tsoi H.-W., Chan K.-H., Yuen K.-Y.
      J. Virol. 80:7136-7145(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiR1A_CVHN2
    AccessioniPrimary (citable) accession number: P0C6U4
    Secondary accession number(s): Q14EB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 45 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Isolate N2 belongs to genotype B.

    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