Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0C6X3

- R1AB_CVHN2

UniProt

P0C6X3 - R1AB_CVHN2

Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Human coronavirus HKU1 (isolate N2) (HCoV-HKU1)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.
    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
    The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) By similarity.By similarity
    The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction.By similarity
    Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter.By similarity
    Nsp9 is a ssRNA-binding protein.By similarity
    NendoU is a Mn2+-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.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

    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
    ATP + H2O = ADP + phosphate.
    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
    Sitei5355 – 53562Cleavage; by 3CL-PROBy similarity
    Sitei6479 – 64802Cleavage; by 3CL-PROBy similarity
    Sitei6853 – 68542Cleavage; 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
    Nucleotide bindingi5636 – 56438ATPBy 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 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 gene expression 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. transcription, DNA-templated Source: InterPro
    8. viral genome replication Source: InterPro
    9. viral protein processing 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, 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 ISG15 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):
    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
    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
    p67
    Exoribonuclease (EC:3.1.13.-)
    Short name:
    ExoN
    Alternative name(s):
    nsp14
    Alternative name(s):
    NendoU
    nsp15
    p35
    Alternative name(s):
    nsp16
    Gene namesi
    Name:rep
    ORF Names:1a-1b
    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.
    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.

    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 – 222222Non-structural protein 1By similarityPRO_0000297773Add
    BLAST
    Chaini223 – 809587Non-structural protein 2By similarityPRO_0000297774Add
    BLAST
    Chaini810 – 28081999Non-structural protein 3By similarityPRO_0000297775Add
    BLAST
    Chaini2809 – 3304496Non-structural protein 4By similarityPRO_0000297776Add
    BLAST
    Chaini3305 – 36073033C-like proteinaseBy similarityPRO_0000297777Add
    BLAST
    Chaini3608 – 3894287Non-structural protein 6By similarityPRO_0000297778Add
    BLAST
    Chaini3895 – 398692Non-structural protein 7By similarityPRO_0000297779Add
    BLAST
    Chaini3987 – 4180194Non-structural protein 8By similarityPRO_0000297780Add
    BLAST
    Chaini4181 – 4290110Non-structural protein 9By similarityPRO_0000297781Add
    BLAST
    Chaini4291 – 4427137Non-structural protein 10By similarityPRO_0000297782Add
    BLAST
    Chaini4428 – 5355928RNA-directed RNA polymeraseBy similarityPRO_0000297783Add
    BLAST
    Chaini5356 – 5958603HelicaseBy similarityPRO_0000297784Add
    BLAST
    Chaini5959 – 6479521ExoribonucleaseBy similarityPRO_0000297785Add
    BLAST
    Chaini6480 – 6853374Uridylate-specific endoribonucleaseBy similarityPRO_0000297786Add
    BLAST
    Chaini6854 – 7152299Putative 2'-O-methyl transferaseBy similarityPRO_0000297787Add
    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

    ProteinModelPortaliP0C6X3.
    SMRiP0C6X3. Positions 4022-4172, 4296-4420, 6480-6848.
    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
    Domaini5035 – 5197163RdRp catalyticAdd
    BLAST
    Domaini5356 – 543984CV MBDAdd
    BLAST
    Domaini5611 – 5792182(+)RNA virus helicase ATP-bindingAdd
    BLAST
    Domaini5793 – 5962170(+)RNA virus helicase C-terminalAdd
    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
    Compositional biasi5360 – 538526Cys-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
    Contains 1 RdRp catalytic domain.Curated

    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

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
    IPR022570. Coronavirus_NSP1.
    IPR009461. Coronavirus_NSP16.
    IPR027352. CV_MBD_dom.
    IPR002589. Macro_dom.
    IPR009466. NSP11.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR027417. P-loop_NTPase.
    IPR002705. Pept_C30/C16_B_coronavir.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR001205. RNA-dir_pol_C.
    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.
    PF11963. DUF3477. 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.
    PF01831. Peptidase_C16. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF00680. RdRP_1. 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.
    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.
    [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: P0C6X3-1) [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.

    « 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 LNFLNRVRGT SVNARLVPCA 4450
    SGLSTDVQLR AFDICNTNRA GIGLYYKVNC CRFQRIDDDG NKLDKFFVVK 4500
    RTNLEVYNKE KTYYELTKSC GVVAEHDFFT FDIDGSRVPH IVRKNLSKYT 4550
    MLDLCYALRH FDCNDCSVLC EILCEYADCK ESYFSKKDWY DFVENPDIIN 4600
    IYKKLGPIFN RALLNTVSFA DTLVKVGLVG VLTLDNQDLY GQWYDFGDFI 4650
    QTAPGFGVAV ADSYYSYMMP MLTMCHVLDC ELFVNDSYRQ FDLVQYDFTD 4700
    YKLELFNKYF KYWGMKYHPN TVDCDNDRCI IHCANFNILF SMVLPNTCFG 4750
    PLVRQIFVDG VPFVVSIGYH YKELGVVMNL DVDTHRYRLS LKDLLLYAAD 4800
    PAMHVASASA LLDLRTCCFS VAAITSGIKF QTVKPGNFNQ DFYEFVKSKG 4850
    LFKEGSTVDL KHFFFTQDGN AAITDYNYYK YNLPTMVDIK QLLFVLEVVY 4900
    KYFEIYDGGC IPASQVIVNN YDKSAGYPFN KFGKARLYYE ALSFEEQNEI 4950
    YAYTKRNVLP TLTQMNLKYA ISAKNRARTV AGVSILSTMT GRMFHQKCLK 5000
    SIAATRGVPV VIGTTKFYGG WDDMLRHLIK DVDNPVLMGW DYPKCDRAMP 5050
    NILRIVSSLV LARKHEFCCS HGDRFYRLAN ECAQVLSEIV MCGGCYYVKP 5100
    GGTSSGDATT AFANSVFNIC QAVTANVCSL MACNGHKIED LSIRNLQKRL 5150
    YSNVYRTDYV DYTFVNEYYE FLCKHFSMMI LSDDGVVCYN SDYASKGYIA 5200
    NISVFQQVLY YQNNVFMSES KCWVENDITN GPHEFCSQHT MLVKIDGDYV 5250
    YLPYPDPSRI LGAGCFVDDL LKTDSVLLIE RFVSLAIDAY PLVHHENEEY 5300
    QKVFRVYLEY IKKLYNDLGN QILDSYSVIL STCDGLKFTD ESFYKNMYLK 5350
    SAVMQSVGAC VVCSSQTSLR CGSCIRKPLL CCKCCYDHVM ATNHKYVLSV 5400
    SPYVCNAPNC DVSDVTKLYL GGMSYYCENH KPHYSFKLVM NGMVFGLYKQ 5450
    SCTGSPYIDD FNKIASCKWT EVDDYVLANE CIERLKLFAA ETQKATEEAF 5500
    KQSYASATIQ EIVSDREIIL CWETGKVKPP LNKNYVFTGY HFTSTGKTVL 5550
    GEYVFDKSEL TNGVYYRATT TYKLSIGDVF VLTSHSVANL SAPTLVPQEN 5600
    YASIRFSSVY SVPLLFQTNV ANYQHIGMKR YCTVQGPPGT GKSHLAIGLA 5650
    VYYYTARVVY TAASHAAVDA LCEKAYKFLN INDCTRIIPA KVRVDCYDKF 5700
    KINDTTCKYV FTTINALPEL VTDIVVVDEV SMLTNYELSV INARVKAKHY 5750
    VYIGDPAQLP APRVLLSKGS LEPRHFNSIT KIMCCLGPDI FLGNCYRCPK 5800
    EIVETVSALV YDNKLKAKND NSSLCFKVYF KGQTTHESSS AVNIQQIYLI 5850
    SKFLKANPVW NSAVFISPYN SQNYVAKRIL GVQTQTVDSA QGSEYDYVIY 5900
    SQTAETAHSI NVNRFNVAIT RAKKGIFCVM SNMQLFESLN FITLPLDKIQ 5950
    NQTLSRLHCT TNLFKDCSKN FLGYHPAHAP SFLSVDDKYK VNEDLAVCLN 6000
    ICEPVLTYSR LISLMGFKLD LTLDGYSKFF ITKDEAIKRV RGWVGFDVEG 6050
    AHATRDNIGT NFPLQIGFST GVDFVVEATG LFAERDCYIF KRTVAKAPPG 6100
    DNFKHLIPLM SKGQKWDVVR IRIVQMLSDY LLDLSDSVVF ITWSASFELT 6150
    CLRYFAKLGR ELNCDVCPNR ATCYNSRTGY YGCWRHSYTC DYVYNPLIVD 6200
    IQQWGYTGSL TSNHDIICNV HKGAHVASSD AIMTRCLAIY DCFCKSVNWN 6250
    LEYPIISNEV SINTSCRLLQ RVMLKAAMLC NRYNLCYDIG NPKGIACVKD 6300
    YEFKFYDASP VVKSVKQLFY VYDVHKDNFK DGLCMFWNCN VDKYPSNSIV 6350
    CRFDTRVLNK LNLPGCNGGS LYVNKHAFHT NPFTRTVFEN LKPMPFFYYS 6400
    DTPCVYVDGL ESKQVDYVPL RSATCITRCN LGGAVCSKHA EDYCKYLESY 6450
    NVATTAGFTF WVYKTFDFYN LWNTFTMLQS LENVIYNLVN AGHYDGRIGE 6500
    LPCAIMNDKV VVKINNVDTV IFKNNTSLPT NIAVELFTKR SIRHHPELKI 6550
    LRNLNIDICW KHVLWDYVKD SLFCSSTYGV CKYTDLNFIE NLNVLFDGRD 6600
    NGALEAFRKA RNGVFISTGK LSSLSMIKGP QRADLNGVIV DKVGELNVEF 6650
    WFAMRKDGDD VIFSRADSLS PSHYWSPQGN LGGNCAGNAS GNDALARFTI 6700
    FTQSRVLSTF EPRSDLERDF IDMEDSLFIA KYGLEDYAFD HIVYGSFNYK 6750
    VIGGLHLLIG LFRRLKKSNL VIQEFLQYDS SIHSYFITDQ ECGSSKSVCT 6800
    VIDLLLDDFV VIVKSLNLNC VSKVVNINVD FKDFQFMLWC NDNKIMTFYP 6850
    KMQATSDWKP GYSMPVLYKY LNVPLERVSL WNYGKAINLP TGCMMNVAKY 6900
    TQLCQYLNTT TLAVPVNMRV LHLGAGSDKE VAPGSAVLRQ WLPSGSILVD 6950
    NDLNPFVSDS LVTYFGDCMT LPFDCHWDLI ISDMYDPLTK NIGDYNVSKD 7000
    GFFTYICYLI RDKLSLGGSV AIKITEFSWN ADLYKLMSYF AFWTVFCTNV 7050
    NASSSEGFLI GINYLGKSCF EIDGNVMHAN YLFWRNSTTW NGGAYSLFDM 7100
    SKFSLKLAGT AVVNLRPDQL NDLVYSLIER GKLLVRDTRK EIFVGDSLVN 7150
    TC 7152

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

    Length:7,152
    Mass (Da):807,495
    Last modified:June 10, 2008 - v1
    Checksum:i1B6E93484EF69631
    GO
    Isoform Replicase polyprotein 1a (identifier: P0C6U4-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1a, ORF1a polyprotein

    The sequence of this isoform can be found in the external entry P0C6U4.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by conventional translation.

    Length:4,441
    Mass (Da):499,423
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY884001 Genomic RNA. Translation: AAX76519.1.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY884001 Genomic RNA. Translation: AAX76519.1 .

    3D structure databases

    ProteinModelPortali P0C6X3.
    SMRi P0C6X3. Positions 4022-4172, 4296-4420, 6480-6848.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR027351. (+)RNA_virus_helicase_core_dom.
    IPR022570. Coronavirus_NSP1.
    IPR009461. Coronavirus_NSP16.
    IPR027352. CV_MBD_dom.
    IPR002589. Macro_dom.
    IPR009466. NSP11.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR027417. P-loop_NTPase.
    IPR002705. Pept_C30/C16_B_coronavir.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR001205. RNA-dir_pol_C.
    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.
    PF11963. DUF3477. 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.
    PF01831. Peptidase_C16. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF00680. RdRP_1. 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.
    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.
    [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 nameiR1AB_CVHN2
    AccessioniPrimary (citable) accession number: P0C6X3
    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 56 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