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P0C6U5

- R1A_CVHN5

UniProt

P0C6U5 - R1A_CVHN5

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Human coronavirus HKU1 (isolate N5) (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 sitei1111 – 11111For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1262 – 12621For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1707 – 17071For PL2-PRO activityPROSITE-ProRule annotation
    Active sitei1864 – 18641For PL2-PRO activityPROSITE-ProRule annotation
    Sitei2788 – 27892Cleavage; by PL2-PROBy similarity
    Sitei3284 – 32852Cleavage; by 3CL-PROBy similarity
    Active sitei3325 – 33251For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3429 – 34291For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3587 – 35882Cleavage; by 3CL-PROBy similarity
    Sitei3874 – 38752Cleavage; by 3CL-PROBy similarity
    Sitei3966 – 39672Cleavage; by 3CL-PROBy similarity
    Sitei4160 – 41612Cleavage; by 3CL-PROBy similarity
    Sitei4270 – 42712Cleavage; by 3CL-PROBy similarity
    Sitei4407 – 44082Cleavage; by 3CL-PROBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1188 – 121629C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1785 – 182137C4-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4344 – 436017By similarityAdd
    BLAST
    Zinc fingeri4386 – 439914By 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 N5) (HCoV-HKU1)
    Taxonomic identifieri443241 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000001985: 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 – 44214421Replicase polyprotein 1aPRO_0000338218Add
    BLAST
    Chaini1 – 222222Non-structural protein 1By similarityPRO_0000338219Add
    BLAST
    Chaini223 – 809587Non-structural protein 2By similarityPRO_0000338220Add
    BLAST
    Chaini810 – 27881979Non-structural protein 3By similarityPRO_0000338221Add
    BLAST
    Chaini2789 – 3284496Non-structural protein 4By similarityPRO_0000338222Add
    BLAST
    Chaini3285 – 35873033C-like proteinaseBy similarityPRO_0000338223Add
    BLAST
    Chaini3588 – 3874287Non-structural protein 6By similarityPRO_0000338224Add
    BLAST
    Chaini3875 – 396692Non-structural protein 7By similarityPRO_0000338225Add
    BLAST
    Chaini3967 – 4160194Non-structural protein 8By similarityPRO_0000338226Add
    BLAST
    Chaini4161 – 4270110Non-structural protein 9By similarityPRO_0000338227Add
    BLAST
    Chaini4271 – 4407137Non-structural protein 10By similarityPRO_0000338228Add
    BLAST
    Chaini4408 – 442114Non-structural protein 11Sequence AnalysisPRO_0000338229Add
    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

    ProteinModelPortaliP0C6U5.
    SMRiP0C6U5. Positions 4002-4152, 4276-4400.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2176 – 219621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2237 – 225721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2268 – 228821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2351 – 237121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2393 – 241321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2794 – 281421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3069 – 308921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3101 – 312121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3128 – 314821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3153 – 317321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3601 – 362121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3626 – 364621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3651 – 367121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3694 – 371421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3722 – 374221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3750 – 377021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3793 – 381321HelicalSequence 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
    Domaini1073 – 1323251Peptidase C16 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1301 – 1472172MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1668 – 1928261Peptidase C16 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini3285 – 3587303Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni945 – 1034909 X 10 AA tandem repeat of N-[DN]-D-E-D-V-V-T-G-DAdd
    BLAST
    Regioni2176 – 2413238HD1By similarityAdd
    BLAST
    Regioni2794 – 3173380HD2By similarityAdd
    BLAST
    Regioni3601 – 3813213HD3By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi934 – 1066133Asp-richAdd
    BLAST
    Compositional biasi2179 – 227193Phe-richAdd
    BLAST
    Compositional biasi2566 – 25694Poly-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 fingeri1188 – 121629C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1785 – 182137C4-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4344 – 436017By similarityAdd
    BLAST
    Zinc fingeri4386 – 439914By 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: P0C6U5-1) [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
    FGWIVPFGFM PSYVHKWFQF CRLYIEESDL IISNFKFDDY DFSVEAAYAE 200
    VHAEPKGKYS QKAYALLRQY RGIKPVLFVD QYGCDYSGKL ADCLQAYGHY 250
    SLQDMRQKQS VWLANCDFDI VVAWHVVRDS RFVMRLQTIA TICGIKYVAQ 300
    PTEDVVDGDV 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 WLLYQLLNGF 650
    FVVSQANLNF VALIPDYAKI LVNKFYTFFK LLLECVTVDV LKDMPVLKTI 700
    NGLVCIVGNK FYNVSTGLIP GFVLPCNAQE QQIYFFEGVA ESVIVEDDVI 750
    ENVKSSLSSY EYCQPPKSVE KICIIDNMYM GKCGDKFFPI VMNDKNICLL 800
    DHAWRFPCAG RKVNFNEKPV VMEIPSLMTV KVMFDLDSTF DDILGKVCSE 850
    FEVEKGVTVD DFVAVVCDAI ENALNSCKEH PVVGYQVRAF LNKLNENVVY 900
    LFDEAGDEAM ASRMYCTFAI EDVEDVISSE AVEDTIDGVV EDTINDDEDV 950
    VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV VTGDNDDEDV 1000
    VTGDNDDEDV VTGDNDDEDV VTGDNNDEDV VTGDNNDEES VTGDNDDQIV 1050
    VTGDDVDDIE SIYDFDTYKA LLVFNDVYND ALFVSYGSSV ETETYFKVNG 1100
    LWSPTITHTN CWLRSVLLVM QKLPFKFKDL AIENMWLSYK VGYNQSFVDY 1150
    LLTTIPKAIV LPQGGYVADF AYWFLNQFDI NAYANWCCLK CGFSFDLNGL 1200
    DAVFFYGDIV SHVCKCGHNM TLIAADLPCT LHFSLFDDNF CAFCTPKKIF 1250
    IAACAVDVNV CHSVAVIGDE QIDGKFVTKF SGDKFDFIVG YGMSFSMSSF 1300
    ELAQLYGLCI TPNVCFVKGD IINVARLVKA DVIVNPANGH MLHGGGVAKA 1350
    IAVAAGKKFS KETAAMVKSK GVCQVGDCYV STGGKLCKTI LNIVGPDARQ 1400
    DGRQSYVLLA RAYKHLNNYD CCLSTLISAG IFSVPADVSL TYLLGVVDKQ 1450
    VILVSNNKED FDIIQKCQIT SVVGTKALAV RLTANVGRVI KFETDAYKLF 1500
    LSGDDCFVSN SSVIQEVLLL RHDIQLNNDV RDYLLSKMTS LPKDWRLINK 1550
    FDVINGVKTV KYFECPNSIY ICSQGKDFGY VCDGSFYKAT VNQVCVLLAK 1600
    KIDVLLTVDG VNFKSISLTV GEVFGKILGN VFCDGIDVTK LKCSDFYADK 1650
    ILYQYENLSL ADISAVQSSF GFDQQQLLAY YNFLTVCKWS VVVNGPFFSF 1700
    EQSHNNCYVN VACLMLQHIN LKFNKWQWQE AWYEFRAGRP HRLVALVLAK 1750
    GHFKFDEPSD ATDFIRVVLK QADLSGAICE LELICDCGIK QESRVGVDAV 1800
    MHFGTLAKTD LFNGYKIGCN CAGRIVHCTK LNVPFLICSN TPLSKDLPDD 1850
    VVAANMFMGV GVGHYTHLKC GSPYQHYDAC SVKKYTGVSG CLTDCLYLKN 1900
    LTQTFTSMLT NYFLDDVEMV AYNPDLSQYY CDNGKYYTKP IIKAQFKPFA 1950
    KVDGVYTNFK LVGHDICAQL NDKLGFNVDL PFVEYKVTVW PVATGDVVLA 2000
    SDDLYVKRYF KGCETFGKPV IWFCHDEASL NSLTYFNKPS FKSENRYSVL 2050
    SVDSVSEESQ GNVVTSVMES QISTKEVKLK GVRKTVKIED AIIVNDENSS 2100
    IKVVKSLSLV DVWDMYLTGC DYVVWVANEL SRLVKSPTVR EYIRYGIKPI 2150
    TIPIDLLCLR DDNQTLLVPK IFKARAIEFY GFLKWLFIYV FSLLHFTNDK 2200
    TIFYTTEIAS KFTFNLFCLA LKNAFQTFRW SIFIKGFLVV ATVFLFWFNF 2250
    LYINVIFSDF YLPNISVFPI FVGRIVMWIK ATFGLVTICD FYSKLGVGFT 2300
    SHFCNGSFIC ELCHSGFDML DTYAAIDFVQ YEVDRRVLFD YVSLVKLIVE 2350
    LVIGYSLYTV WFYPLFCLIG LQLFTTWLPD LFMLETMHWL IRFIVFVANM 2400
    LPAFVLLRFY IVVTAMYKVV GFIRHIVYGC NKAGCLFCYK RNCSVRVKCS 2450
    TIVGGVIRYY DITANGGTGF CVKHQWNCFN CHSFKPGNTF ITVEAAIELS 2500
    KELKRPVNPT DASHYVVTDI KQVGCMMRLF YDRDGQRVYD DVDASLFVDI 2550
    NNLLHSKVKV VPNLYVVVVE SDADRANFLN AVVFYAQSLY RPILLVDKKL 2600
    ITTACNGISV TQIMFDVYVD TFMSHFDVDR KSFNNFVNIA HASLREGVQL 2650
    EKVLDTFVGC VRKCCSIDSD VETRFITKSM ISAVAAGLEF TDENYNNLVP 2700
    TYLKSDNIVA ADLGVLIQNG AKHVQGNVAK VANISCIWFI DAFNQLTADL 2750
    QHKLKKACVK TGLKLKLTFN KQEASVPILT TPFSLKGGVV LSNLLYILFF 2800
    ISLICFILLW ALLPTYSVYK SDIHLPAYAS FKVIDNGVVR DISVNDLCFA 2850
    NKFFQFDQWY ESTFGSVYYH NSMDCPIVVA VMDEDIGSTM FNVPTKVLRY 2900
    GFHVLHFLTY AFASDSVQCY TPHIQISYND FYASGCVLSS LCTMFKRGDG 2950
    TPHPYCYTDG VMKNASLYTS LVPHTRYSLA NSNGFIRFPD VISEGIVRIV 3000
    RTRSMTYCRV GACEYAEEGI CFNFNSSWVL NNDYYRSMPG TFCGRDFFDL 3050
    FYQFFSSLIR PIDFFSLTAS SIFGAILAIV VVLVFYYLIK LKRAFGDYTS 3100
    VVVINVIVWC INFLMLFVFQ VYPICACVYA CFYFYVTLYF PSEISVIMHL 3150
    QWIVMYGAIM PFWFCVTYVA MVIANHVLWL FSYCRKIGVN VCSDSTFEET 3200
    SLTTFMITKD SYCRLKNSVS DVAYNRYLSL YNKYRYYSGK MDTAAYREAA 3250
    CSQLAKAMET FNHNNGNDVL YQPPTASVST SFLQSGIVKM VSPTSKIEPC 3300
    LVSVTYGSMT LNGLWLDDKV YCPRHVICLS SNMNEPDYSA LLCRVTLGDF 3350
    TIMSGRMSLT VVSYQMQGCQ LVLTVSLQNP YTPKYTFGVV KPGETFTVLA 3400
    AYNGRPQGAF HVTMRSSYTI KGSFLCGSCG SVGYVLTGDS VKFVYMHQLE 3450
    LSTGCHTGTD FNGNFYGPYR DAQVVQLPVK DYVQTVNVIA WLYAAILNNC 3500
    AWFVQNDVCS IEDFNVWAMT NGFSQVKADL VLDALASMTG VSIETLLAAI 3550
    KRLYMGFQGR QILGSCTFED ELAPSDVYQQ LAGVKLQSKT KRFIKETIYW 3600
    ILISTFLFSC IISAFVKWTI FMYINTHMIG VTLCVLCFVS FMMLLVKHKH 3650
    FYLTMYIIPV LCTLFYVNYL VVYKEGFRGF TYVWLSHFVP AVNFTYVYEV 3700
    FYGCILCVFA IFITMHSINH DIFSLMFLVG RIVTLISMWY FGSNLEEDVL 3750
    LFITAFLGTY TWTTILSLAI AKIVANWLSV NIFYFTDVPY IKLILLSYLF 3800
    IGYILSCYWG FFSLLNSVFR MPMGVYNYKI SVQELRYMNA NGLRPPRNSF 3850
    EAILLNLKLL GIGGVPVIEV SQIQSKLTDV KCANVVLLNC LQHLHVASNS 3900
    KLWQYCSVLH NEILSTSDLS VAFDKLAQLL IVLFSNPAAV DTKCLASIDE 3950
    VSDDYVQDST VLQALQSEFV NMASFVEYEV AKKNLADAKN SGSVNQQQIK 4000
    QLEKACNIAK SVYERDKAVA RKLERMADLA LTNMYKEARI NDKKSKVVSA 4050
    LQTMLFSMVR KLDNQALNSI LDNAVKGCVP LSAIPALAAN TLTIIIPDKQ 4100
    VFDKVVDNVY VTYAGSVWHI QTVQDADGIN KQLTDISVDS NWPLVIIANR 4150
    YNEVANAVMQ NNELMPHKLK IQVVNSGSDI NCNIPTQCYY NNVSSGRIVY 4200
    AVLSDVDGLK YTKIMKDDGN CVVLELDPPC KFSIQDVKGL KIKYLYFIKG 4250
    CNTLARGWVV GTLSSTIRLQ AGVATEYAAN SSILSLCAFS VDPKKTYLDY 4300
    IQQGGVPIIN CVKMLCDHAG TGMAITIKPE ATINQDSYGG ASVCIYCRAR 4350
    VEHPDVDGIC KLRGKFVQVP LGIKDPILYV LTHDVCQVCG FWRDGSCSCV 4400
    GSSVAVQSKD LNFLNGLGVL V 4421

    Note: Produced by conventional translation.

    Length:4,421
    Mass (Da):497,400
    Last modified:June 10, 2008 - v1
    Checksum:i19FFC89AAA1E43AB
    GO
    Isoform Replicase polyprotein 1ab (identifier: P0C6X4-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry P0C6X4.
    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:7,132
    Mass (Da):805,783
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ339101 Genomic RNA. No translation available.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ339101 Genomic RNA. No translation available.

    3D structure databases

    ProteinModelPortali P0C6U5.
    SMRi P0C6U5. Positions 4002-4152, 4276-4400.
    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_CVHN5
    AccessioniPrimary (citable) accession number: P0C6U5
    Secondary accession number(s): Q0ZME9
    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 N5 belongs to genotype C. Genotype C probably arose from recombination between genotypes A and 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