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P0C6X5

- R1AB_CVHNL

UniProt

P0C6X5 - R1AB_CVHNL

Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Human coronavirus NL63 (HCoV-NL63)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.1 Publication
    The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 By similarity.By similarity
    The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function By similarity.PROSITE-ProRule annotation
    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).1 Publication
    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
    NendoU is a Mn2+-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.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).
    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
    ATP + H2O = ADP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei110 – 1112Cleavage; by PL1-PROBy similarity
    Sitei898 – 8992Cleavage; by PL1-PROBy similarity
    Active sitei1062 – 10621For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1212 – 12121For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1678 – 16781For PL2-PRO activityPROSITE-ProRule annotation
    Active sitei1836 – 18361For PL2-PRO activityPROSITE-ProRule annotation
    Sitei2462 – 24632Cleavage; by PL2-PROBy similarity
    Sitei2939 – 29402Cleavage; by 3CL-PROBy similarity
    Active sitei2980 – 29801For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3083 – 30831For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3242 – 32432Cleavage; by 3CL-PROBy similarity
    Sitei3521 – 35222Cleavage; by 3CL-PROBy similarity
    Sitei3604 – 36052Cleavage; by 3CL-PROBy similarity
    Sitei3799 – 38002Cleavage; by 3CL-PROBy similarity
    Sitei3908 – 39092Cleavage; by 3CL-PROBy similarity
    Sitei4043 – 40442Cleavage; by 3CL-PROBy similarity
    Sitei4970 – 49712Cleavage; by 3CL-PROBy similarity
    Sitei6085 – 60862Cleavage; by 3CL-PROBy similarity
    Sitei6429 – 64302Cleavage; by 3CL-PROBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1134 – 116532C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1757 – 178832C4-type 2; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri3982 – 399817By similarityAdd
    BLAST
    Zinc fingeri4024 – 403714By similarityAdd
    BLAST
    Nucleotide bindingi5253 – 52608ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cysteine-type endopeptidase activity Source: InterPro
    3. endonuclease activity Source: UniProtKB-KW
    4. exoribonuclease activity, producing 5'-phosphomonoesters Source: InterPro
    5. helicase activity Source: UniProtKB-KW
    6. methyltransferase activity Source: InterPro
    7. omega peptidase activity Source: InterPro
    8. RNA binding Source: UniProtKB-KW
    9. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    10. 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. transcription, DNA-templated Source: InterPro
    5. viral protein processing Source: InterPro
    6. viral RNA genome replication Source: InterPro

    Keywords - Molecular functioni

    Endonuclease, Exonuclease, Helicase, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase

    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, Viral RNA replication

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Replicase polyprotein 1ab
    Short name:
    pp1ab
    Alternative name(s):
    ORF1ab polyprotein
    Cleaved into the following 15 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
    RNA-directed RNA polymerase (EC:2.7.7.48)
    Short name:
    Pol
    Short name:
    RdRp
    Alternative name(s):
    nsp12
    p100
    Helicase (EC:3.6.4.12, EC:3.6.4.13)
    Short name:
    Hel
    Alternative name(s):
    nsp13
    p66
    p66-HEL
    Exoribonuclease (EC:3.1.13.-)
    Short name:
    ExoN
    Alternative name(s):
    nsp14
    Alternative name(s):
    NendoU
    nsp15
    p41
    Alternative name(s):
    nsp16
    Gene namesi
    Name:rep
    ORF Names:1a-1b
    OrganismiHuman coronavirus NL63 (HCoV-NL63)
    Taxonomic identifieri277944 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000008573: 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
    Chain Helicase : Host endoplasmic reticulum-Golgi intermediate compartment Curated
    Note: The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA.By similarity

    GO - Cellular componenti

    1. host cell endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
    2. host cell membrane Source: UniProtKB-SubCell
    3. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
    4. 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 – 110110Non-structural protein 1By similarityPRO_0000283874Add
    BLAST
    Chaini111 – 898788Non-structural protein 2By similarityPRO_0000283875Add
    BLAST
    Chaini899 – 24621564Non-structural protein 3By similarityPRO_0000283876Add
    BLAST
    Chaini2463 – 2939477Non-structural protein 4By similarityPRO_0000283877Add
    BLAST
    Chaini2940 – 32423033C-like proteinaseBy similarityPRO_0000283878Add
    BLAST
    Chaini3243 – 3521279Non-structural protein 6By similarityPRO_0000283879Add
    BLAST
    Chaini3522 – 360483Non-structural protein 7By similarityPRO_0000283880Add
    BLAST
    Chaini3605 – 3799195Non-structural protein 8By similarityPRO_0000283881Add
    BLAST
    Chaini3800 – 3908109Non-structural protein 9By similarityPRO_0000283882Add
    BLAST
    Chaini3909 – 4043135Non-structural protein 10By similarityPRO_0000283883Add
    BLAST
    Chaini4044 – 4970927RNA-directed RNA polymeraseBy similarityPRO_0000283884Add
    BLAST
    Chaini4971 – 5567597HelicaseBy similarityPRO_0000283885Add
    BLAST
    Chaini5568 – 6085518ExoribonucleaseBy similarityPRO_0000283886Add
    BLAST
    Chaini6086 – 6429344Uridylate-specific endoribonucleaseBy similarityPRO_0000283887Add
    BLAST
    Chaini6430 – 6729300Putative 2'-O-methyl transferaseBy similarityPRO_0000283888Add
    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.

    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

    ProteinModelPortaliP0C6X5.
    SMRiP0C6X5. Positions 2940-3240, 3802-3907, 3915-4039.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1903 – 192321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1968 – 198821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2050 – 207021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2073 – 209321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2111 – 213121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2468 – 248821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2727 – 274721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2752 – 276918HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2772 – 279221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2800 – 282021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3254 – 327421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3279 – 329921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3303 – 332321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3342 – 336221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3376 – 339621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3397 – 341721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3442 – 346221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1021 – 1262242Peptidase C16 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1263 – 1421159MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1640 – 1886247Peptidase C16 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2940 – 3242303Peptidase C30PROSITE-ProRule annotationAdd
    BLAST
    Domaini4650 – 4812163RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini4971 – 505484CV MBDAdd
    BLAST
    Domaini5228 – 5409182(+)RNA virus helicase ATP-bindingAdd
    BLAST
    Domaini5410 – 5579170(+)RNA virus helicase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1903 – 2131229HD1By similarityAdd
    BLAST
    Regioni2468 – 2820353HD2By similarityAdd
    BLAST
    Regioni3254 – 3462209HD3By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi625 – 6284Poly-Leu
    Compositional biasi1975 – 19784Poly-Leu

    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
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1134 – 116532C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1757 – 178832C4-type 2; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri3982 – 399817By similarityAdd
    BLAST
    Zinc fingeri4024 – 403714By similarityAdd
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
    IPR009461. Coronavirus_NSP16.
    IPR027352. CV_MBD_dom.
    IPR002589. Macro_dom.
    IPR009466. NSP11.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR027417. P-loop_NTPase.
    IPR011050. Pectin_lyase_fold/virulence.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009469. RNA_pol_N_coronovir.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view]
    PfamiPF06478. Corona_RPol_N. 1 hit.
    PF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF06471. NSP11. 1 hit.
    PF06460. NSP13. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF08715. Viral_protease. 2 hits.
    [Graphical view]
    SMARTiSM00506. A1pp. 1 hit.
    [Graphical view]
    SUPFAMiSSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 1 hit.
    SSF50494. SSF50494. 1 hit.
    SSF51126. SSF51126. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF53335. SSF53335. 1 hit.
    PROSITEiPS51653. CV_MBD. 1 hit.
    PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 2 hits.
    PS51657. PSRV_HELICASE. 1 hit.
    PS50507. RDRP_SSRNA_POS. 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 1ab (identifier: P0C6X5-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    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.

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    MFYNQVTLAV ASDSEISGFG FAIPSVAVRT YSEAAAQGFQ ACRFVAFGLQ     50
    DCVTGINDDD YVIALTGTNQ LCAKILPFSD RPLNLRGWLI FSNSNYVLQD 100
    FDVVFGHGAG SVVFVDKYMC GFDGKPVLPK NMWEFRDYFN NNTDSIVIGG 150
    VTYQLAWDVI RKDLSYEQQN VLAIESIHYL GTTGHTLKSG CKLTNAKPPK 200
    YSSKVVLSGE WNAVYRAFGS PFITNGMSLL DIIVKPVFFN AFVKCNCGSE 250
    SWSVGAWDGY LSSCCGTPAK KLCVVPGNVV PGDVIITSTS AGCGVKYYAG 300
    LVVKHITNIT GVSLWRVTAV HSDGMFVASS SYDALLHRNS LDPFCFDVNT 350
    LLSNQLRLAF LGASVTEDVK FAASTGVIDI SAGMFGLYDD ILTNNKPWFV 400
    RKASGLFDAI WDAFVAAIKL VPTTTGVLVR FVKSIASTVL TVSNGVIIMC 450
    ADVPDAFQSV YRTFTQAICA AFDFSLDVFK IGDVKFKRLG DYVLTENALV 500
    RLTTEVVRGV RDARIKKAMF TKVVVGPTTE VKFSVIELAT VNLRLVDCAP 550
    VVCPKGKIVV IAGQAFFYSG GFYRFMVDPT TVLNDPVFTG DLFYTIKFSG 600
    FKLDGFNHQF VTASSATDAI IAVELLLLDF KTAVFVYTCV VDGCSVIVRR 650
    DATFATHVCF KDCYNVWEQF CIDNCGEPWF LTDYNAILQS NNPQCAIVQA 700
    SESKVLLERF LPKCPEILLS IDDGHLWNLF VEKFNFVTDW LKTLKLTLTS 750
    NGLLGNCAKR FRRVLVKLLD VYNGFLETVC SVAYTAGVCI KYYAVNVPYV 800
    VISGFVSRVI RRERCDMTFP CVSCVTFFYE FLDTCFGVSK PNAIDVEHLE 850
    LKETVFVEPK DGGQFFVSGD YLWYVVDDIY YPASCNGVLP VAFTKLAGGK 900
    ISFSDDVIVH DVEPTHKVKL IFEFEDDVVT SLCKKSFGKS IIYTGDWEGL 950
    HEVLTSAMNV IGQHIKLPQF YIYDEEGGYD VSKPVMISQW PISNDSNGCV 1000
    VEASTDFHQL ECIVDDSVRE EVDIIEQPFE EVEHVLSIKQ PFSFSFRDEL 1050
    GVRVLDQSDN NCWISTTLVQ LQLTKLLDDS IEMQLFKVGK VDSIVQKCYE 1100
    LSHLISGSLG DSGKLLSELL KEKYTCSITF EMSCDCGKKF DDQVGCLFWI 1150
    MPYTKLFQKG ECCICHKMQT YKLVSMKGTG VFVQDPAPID IDAFPVKPIC 1200
    SSVYLGVKGS GHYQTNLYSF NKAIDGFGVF DIKNSSVNTV CFVDVDFHSV 1250
    EIEAGEVKPF AVYKNVKFYL GDISHLVNCV SFDFVVNAAN ENLLHGGGVA 1300
    RAIDILTEGQ LQSLSKDYIS SNGPLKVGAG VMLECEKFNV FNVVGPRTGK 1350
    HEHSLLVEAY NSILFENGIP LMPLLSCGIF GVRIENSLKA LFSCDINKPL 1400
    QVFVYSSNEE QAVLKFLDGL DLTPVIDDVD VVKPFRVEGN FSFFDCGVNA 1450
    LDGDIYLLFT NSILMLDKQG QLLDTKLNGI LQQAALDYLA TVKTVPAGNL 1500
    VKLFVESCTI YMCVVPSIND LSFDKNLGRC VRKLNRLKTC VIANVPAIDV 1550
    LKKLLSSLTL TVKFVVESNV MDVNDCFKND NVVLKITEDG INVKDVVVES 1600
    SKSLGKQLGV VSDGVDSFEG VLPINTDTVL SVAPEVDWVA FYGFEKAALF 1650
    ASLDVKPYGY PNDFVGGFRV LGTTDNNCWV NATCIILQYL KPTFKSKGLN 1700
    VLWNKFVTGD VGPFVSFIYF ITMSSKGQKG DAEEALSKLS EYLISDSIVT 1750
    LEQYSTCDIC KSTVVEVKSA IVCASVLKDG CDVGFCPHRH KLRSRVKFVN 1800
    GRVVITNVGE PIISQPSKLL NGIAYTTFSG SFDNGHYVVY DAANNAVYDG 1850
    ARLFSSDLST LAVTAIVVVG GCVTSNVPTI VSEKISVMDK LDTGAQKFFQ 1900
    FGDFVMNNIV LFLTWLLSMF SLLRTSIMKH DIKVIAKAPK RTGVILTRSF 1950
    KYNIRSALFV IKQKWCVIVT LFKFLLLLYA IYALVFMIVQ FSPFNSLLCG 2000
    DIVSGYEKST FNKDIYCGNS MVCKMCLFSY QEFNDLDHTS LVWKHIRDPI 2050
    LISLQPFVIL VILLIFGNMY LRFGLLYFVA QFISTFGSFL GFHQKQWFLH 2100
    FVPFDVLCNE FLATFIVCKI VLFVRHIIVG CNNADCVACS KSARLKRVPL 2150
    QTIINGMHKS FYVNANGGTC FCNKHNFFCV NCDSFGPGNT FINGDIAREL 2200
    GNVVKTAVQP TAPAYVIIDK VDFVNGFYRL YSGDTFWRYD FDITESKYSC 2250
    KEVLKNCNVL ENFIVYNNSG SNITQIKNAC VYFSQLLCEP IKLVNSELLS 2300
    TLSVDFNGVL HKAYVDVLCN SFFKELTANM SMAECKATLG LTVSDDDFVS 2350
    AVANAHRYDV LLSDLSFNNF FISYAKPEDK LSVYDIACCM RAGSKVVNHN 2400
    VLIKESIPIV WGVKDFNTLS QEGKKYLVKT TKAKGLTFLL TFNDNQAITQ 2450
    VPATSIVAKQ GAGFKRTYNF LWYVCLFVVA LFIGVSFIDY TTTVTSFHGY 2500
    DFKYIENGQL KVFEAPLHCV RNVFDNFNQW HEAKFGVVTT NSDKCPIVVG 2550
    VSERINVVPG VPTNVYLVGK TLVFTLQAAF GNTGVCYDFD GVTTSDKCIF 2600
    NSACTRLEGL GGDNVYCYNT DLIEGSKPYS TLQPNAYYKY DAKNYVRFPE 2650
    ILARGFGLRT IRTLATRYCR VGECRDSHKG VCFGFDKWYV NDGRVDDGYI 2700
    CGDGLIDLLV NVLSIFSSSF SVVAMSGHML FNFLFAAFIT FLCFLVTKFK 2750
    RVFGDLSYGV FTVVCATLIN NISYVVTQNL FFMLLYAILY FVFTRTVRYA 2800
    WIWHIAYIVA YFLLIPWWLL TWFSFAAFLE LLPNVFKLKI STQLFEGDKF 2850
    IGTFESAAAG TFVLDMRSYE RLINTISPEK LKNYAASYNK YKYYSGSASE 2900
    ADYRCACYAH LAKAMLDYAK DHNDMLYSPP TISYNSTLQS GLKKMAQPSG 2950
    CVERCVVRVC YGSTVLNGVW LGDTVTCPRH VIAPSTTVLI DYDHAYSTMR 3000
    LHNFSVSHNG VFLGVVGVTM HGSVLRIKVS QSNVHTPKHV FKTLKPGDSF 3050
    NILACYEGIA SGVFGVNLRT NFTIKGSFIN GACGSPGYNV RNDGTVEFCY 3100
    LHQIELGSGA HVGSDFTGSV YGNFDDQPSL QVESANLMLS DNVVAFLYAA 3150
    LLNGCRWWLC STRVNVDGFN EWAMANGYTS VSSVECYSIL AAKTGVSVEQ 3200
    LLASIQHLHE GFGGKNILGY SSLCDEFTLA EVVKQMYGVN LQSGKVIFGL 3250
    KTMFLFSVFF TMFWAELFIY TNTIWINPVI LTPIFCLLLF LSLVLTMFLK 3300
    HKFLFLQVFL LPTVIATALY NCVLDYYIVK FLADHFNYNV SVLQMDVQGL 3350
    VNVLVCLFVV FLHTWRFSKE RFTHWFTYVC SLIAVAYTYF YSGDFLSLLV 3400
    MFLCAISSDW YIGAIVFRLS RLIVFFSPES VFSVFGDVKL TLVVYLICGY 3450
    LVCTYWGILY WFNRFFKCTM GVYDFKVSAA EFKYMVANGL HAPHGPFDAL 3500
    WLSFKLLGIG GDRCIKISTV QSKLTDLKCT NVVLLGCLSS MNIAANSSEW 3550
    AYCVDLHNKI NLCDDPEKAQ SMLLALLAFF LSKHSDFGLD GLIDSYFDNS 3600
    STLQSVASSF VSMPSYIAYE NARQAYEDAI ANGSSSQLIK QLKRAMNIAK 3650
    SEFDHEISVQ KKINRMAEQA ATQMYKEARS VNRKSKVISA MHSLLFGMLR 3700
    RLDMSSVETV LNLARDGVVP LSVIPATSAS KLTIVSPDLE SYSKIVCDGS 3750
    VHYAGVVWTL NDVKDNDGRP VHVKEITKEN VETLTWPLIL NCERVVKLQN 3800
    NEIMPGKLKQ KPMKAEGDGG VLGDGNALYN TEGGKTFMYA YISNKADLKF 3850
    VKWEYEGGCN TIELDSPCRF MVETPNGPQV KYLYFVKNLN TLRRGAVLGF 3900
    IGATIRLQAG KQTELAVNSG LLTACAFSVD PATTYLEAVK HGAKPVSNCI 3950
    KMLSNGAGNG QAITTSVDAN TNQDSYGGAS ICLYCRAHVP HPSMDGYCKF 4000
    KGKCVQVPIG CLDPIRFCLE NNVCNVCGCW LGHGCACDRT TIQSVDISYL 4050
    NRARGSSAAR LEPCNGTDID KCVRAFDIYN KNVSFLGKCL KMNCVRFKNA 4100
    DLKDGYFVIK RCTKSVMEHE QSMYNLLNFS GALAEHDFFT WKDGRVIYGN 4150
    VSRHNLTKYT MMDLVYAMRN FDEQNCDVLK EVLVLTGCCD NSYFDSKGWY 4200
    DPVENEDIHR VYASLGKIVA RAMLKCVALC DAMVAKGVVG VLTLDNQDLN 4250
    GNFYDFGDFV VSLPNMGVPC CTSYYSYMMP IMGLTNCLAS ECFVKSDIFG 4300
    SDFKTFDLLK YDFTEHKENL FNKYFKHWSF DYHPNCSDCY DDMCVIHCAN 4350
    FNTLFATTIP GTAFGPLCRK VFIDGVPLVT TAGYHFKQLG LVWNKDVNTH 4400
    SVRLTITELL QFVTDPSLII ASSPALVDQR TICFSVAALS TGLTNQVVKP 4450
    GHFNEEFYNF LRLRGFFDEG SELTLKHFFF AQNGDAAVKD FDFYRYNKPT 4500
    ILDICQARVT YKIVSRYFDI YEGGCIKACE VVVTNLNKSA GWPLNKFGKA 4550
    SLYYESISYE EQDALFALTK RNVLPTMTQL NLKYAISGKE RARTVGGVSL 4600
    LSTMTTRQYH QKHLKSIVNT RNATVVIGTT KFYGGWNNML RTLIDGVENP 4650
    MLMGWDYPKC DRALPNMIRM ISAMVLGSKH VNCCTATDRF YRLGNELAQV 4700
    LTEVVYSNGG FYFKPGGTTS GDASTAYANS IFNIFQAVSS NINRLLSVPS 4750
    DSCNNVNVRD LQRRLYDNCY RLTSVEESFI DDYYGYLRKH FSMMILSDDG 4800
    VVCYNKDYAE LGYIADISAF KATLYYQNNV FMSTSKCWVE EDLTKGPHEF 4850
    CSQHTMQIVD KDGTYYLPYP DPSRILSAGV FVDDVVKTDA VVLLERYVSL 4900
    AIDAYPLSKH PNSEYRKVFY VLLDWVKHLN KNLNEGVLES FSVTLLDNQE 4950
    DKFWCEDFYA SMYENSTILQ AAGLCVVCGS QTVLRCGDCL RKPMLCTKCA 5000
    YDHVFGTDHK FILAITPYVC NASGCGVSDV KKLYLGGLNY YCTNHKPQLS 5050
    FPLCSAGNIF GLYKNSATGS LDVEVFNRLA TSDWTDVRDY KLANDVKDTL 5100
    RLFAAETIKA KEESVKSSYA FATLKEVVGP KELLLSWESG KVKPPLNRNS 5150
    VFTCFQISKD SKFQIGEFIF EKVEYGSDTV TYKSTVTTKL VPGMIFVLTS 5200
    HNVQPLRAPT IANQEKYSSI YKLHPAFNVS DAYANLVPYY QLIGKQKITT 5250
    IQGPPGSGKS HCSIGLGLYY PGARIVFVAC AHAAVDSLCA KAMTVYSIDK 5300
    CTRIIPARAR VECYSGFKPN NTSAQYIFST VNALPECNAD IVVVDEVSMC 5350
    TNYDLSVINQ RLSYKHIVYV GDPQQLPAPR VMITKGVMEP VDYNVVTQRM 5400
    CAIGPDVFLH KCYRCPAEIV NTVSELVYEN KFVPVKPASK QCFKVFFKGN 5450
    VQVDNGSSIN RKQLEIVKLF LVKNPSWSKA VFISPYNSQN YVASRFLGLQ 5500
    IQTVDSSQGS EYDYVIYAQT SDTAHACNVN RFNVAITRAK KGIFCVMCDK 5550
    TLFDSLKFFE IKHADLHSSQ VCGLFKNCTR TPLNLPPTHA HTFLSLSDQF 5600
    KTTGDLAVQI GSNNVCTYEH VISFMGFRFD ISIPGSHSLF CTRDFAIRNV 5650
    RGWLGMDVES AHVCGDNIGT NVPLQVGFSN GVNFVVQTEG CVSTNFGDVI 5700
    KPVCAKSPPG EQFRHLIPLL RKGQPWLIVR RRIVQMISDY LSNLSDILVF 5750
    VLWAGSLELT TMRYFVKIGP IKYCYCGNSA TCYNSVSNEY CCFKHALGCD 5800
    YVYNPYAFDI QQWGYVGSLS QNHHTFCNIH RNEHDASGDA VMTRCLAVHD 5850
    CFVKNVDWTV TYPFIANEKF INGCGRNVQG HVVRAALKLY KPSVIHDIGN 5900
    PKGVRCAVTD AKWYCYDKQP VNSNVKLLDY DYATHGQLDG LCLFWNCNVD 5950
    MYPEFSIVCR FDTRTRSVFN LEGVNGGSLY VNKHAFHTPA YDKRAFVKLK 6000
    PMPFFYFDDS DCDVVQEQVN YVPLRASSCV TRCNIGGAVC SKHANLYQKY 6050
    VEAYNTFTQA GFNIWVPHSF DVYNLWQIFI ETNLQSLENI AFNVVKKGCF 6100
    TGVDGELPVA VVNDKVFVRY GDVDNLVFTN KTTLPTNVAF ELFAKRKMGL 6150
    TPPLSILKNL GVVATYKFVL WDYEAERPFT SYTKSVCKYT DFNEDVCVCF 6200
    DNSIQGSYER FTLTTNAVLF STVVIKNLTP IKLNFGMLNG MPVSSIKGDK 6250
    GVEKLVNWYI YVRKNGQFQD HYDGFYTQGR NLSDFTPRSD MEYDFLNMDM 6300
    GVFINKYGLE DFNFEHVVYG DVSKTTLGGL HLLISQFRLS KMGVLKADDF 6350
    VTASDTTLRC CTVTYLNELS SKVVCTYMDL LLDDFVTILK SLDLGVISKV 6400
    HEVIIDNKPY RWMLWCKDNH LSTFYPQLQS AEWKCGYAMP QIYKLQRMCL 6450
    EPCNLYNYGA GIKLPSGIML NVVKYTQLCQ YLNSTTMCVP HNMRVLHYGA 6500
    GSDKGVAPGT TVLKRWLPPD AIIIDNDIND YVSDADFSIT GDCATVYLED 6550
    KFDLLISDMY DGRIKFCDGE NVSKDGFFTY LNGVIREKLA IGGSVAIKIT 6600
    EYSWNKYLYE LIQRFAFWTL FCTSVNTSSS EAFLIGINYL GDFIQGPFIA 6650
    GNTVHANYIF WRNSTIMSLS YNSVLDLSKF ECKHKATVVV TLKDSDVNDM 6700
    VLSLIKSGRL LLRNNGRFGG FSNHLVSTK 6729

    Note: Produced by -1 ribosomal frameshifting at the 1a-1b genes boundary.

    Length:6,729
    Mass (Da):752,702
    Last modified:June 10, 2008 - v1
    Checksum:i86F9F04C687A65FA
    GO
    Isoform Replicase polyprotein 1a (identifier: P0C6U6-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1a, ORF1a polyprotein

    The sequence of this isoform can be found in the external entry P0C6U6.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by conventional translation.

    Length:4,060
    Mass (Da):451,388
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY567487 Genomic RNA. Translation: AAS58176.2.
    RefSeqiYP_003766.2. NC_005831.2. [P0C6X5-1]

    Genome annotation databases

    GeneIDi2943501.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY567487 Genomic RNA. Translation: AAS58176.2 .
    RefSeqi YP_003766.2. NC_005831.2. [P0C6X5-1 ]

    3D structure databases

    ProteinModelPortali P0C6X5.
    SMRi P0C6X5. Positions 2940-3240, 3802-3907, 3915-4039.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2943501.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR027351. (+)RNA_virus_helicase_core_dom.
    IPR009461. Coronavirus_NSP16.
    IPR027352. CV_MBD_dom.
    IPR002589. Macro_dom.
    IPR009466. NSP11.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR027417. P-loop_NTPase.
    IPR011050. Pectin_lyase_fold/virulence.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009469. RNA_pol_N_coronovir.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view ]
    Pfami PF06478. Corona_RPol_N. 1 hit.
    PF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF06471. NSP11. 1 hit.
    PF06460. NSP13. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF00680. RdRP_1. 1 hit.
    PF08715. Viral_protease. 2 hits.
    [Graphical view ]
    SMARTi SM00506. A1pp. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 1 hit.
    SSF50494. SSF50494. 1 hit.
    SSF51126. SSF51126. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF53335. SSF53335. 1 hit.
    PROSITEi PS51653. CV_MBD. 1 hit.
    PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 2 hits.
    PS51657. PSRV_HELICASE. 1 hit.
    PS50507. RDRP_SSRNA_POS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Amsterdam I.
    2. "Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases."
      Clementz M.A., Chen Z., Banach B.S., Wang Y., Sun L., Ratia K., Baez-Santos Y.M., Wang J., Takayama J., Ghosh A.K., Li K., Mesecar A.D., Baker S.C.
      J. Virol. 84:4619-4629(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiR1AB_CVHNL
    AccessioniPrimary (citable) accession number: P0C6X5
    Secondary accession number(s): Q6Q1S3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 52 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

    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