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P0C6X6

- R1AB_CVHOC

UniProt

P0C6X6 - R1AB_CVHOC

Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Human coronavirus OC43 (HCoV-OC43)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (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.
    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).PROSITE-ProRule annotation
    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
    Sitei246 – 2472Cleavage; by PL1-PROBy similarity
    Sitei851 – 8522Cleavage; by PL1-PROBy similarity
    Active sitei1074 – 10741For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1225 – 12251For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1671 – 16711For PL2-PRO activityPROSITE-ProRule annotation
    Active sitei1828 – 18281For PL2-PRO activityPROSITE-ProRule annotation
    Sitei2750 – 27512Cleavage; by PL2-PROBy similarity
    Sitei3246 – 32472Cleavage; by 3CL-PROBy similarity
    Active sitei3287 – 32871For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3391 – 33911For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3549 – 35502Cleavage; by 3CL-PROBy similarity
    Sitei3836 – 38372Cleavage; by 3CL-PROBy similarity
    Sitei3925 – 39262Cleavage; by 3CL-PROBy similarity
    Sitei4122 – 41232Cleavage; by 3CL-PROBy similarity
    Sitei4232 – 42332Cleavage; by 3CL-PROBy similarity
    Sitei4369 – 43702Cleavage; by 3CL-PROBy similarity
    Sitei5297 – 52982Cleavage; by 3CL-PROBy similarity
    Sitei5900 – 59012Cleavage; by 3CL-PROBy similarity
    Sitei6421 – 64222Cleavage; by 3CL-PROBy similarity
    Sitei6796 – 67972Cleavage; by 3CL-PROBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1151 – 117929C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1749 – 178537C4-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4306 – 432217By similarityAdd
    BLAST
    Zinc fingeri4348 – 436114By similarityAdd
    BLAST
    Nucleotide bindingi5578 – 55858ATPBy 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 protein processing Source: InterPro
    9. 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, 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

    Protein family/group databases

    MEROPSiC16.006.

    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 OC43 (HCoV-OC43)
    Taxonomic identifieri31631 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007552: 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 – 246246Non-structural protein 1By similarityPRO_0000283826Add
    BLAST
    Chaini247 – 851605Non-structural protein 2By similarityPRO_0000283827Add
    BLAST
    Chaini852 – 27501899Non-structural protein 3By similarityPRO_0000283828Add
    BLAST
    Chaini2751 – 3246496Non-structural protein 4By similarityPRO_0000283829Add
    BLAST
    Chaini3247 – 35493033C-like proteinaseBy similarityPRO_0000283830Add
    BLAST
    Chaini3550 – 3836287Non-structural protein 6By similarityPRO_0000283831Add
    BLAST
    Chaini3837 – 392589Non-structural protein 7By similarityPRO_0000283832Add
    BLAST
    Chaini3926 – 4122197Non-structural protein 8By similarityPRO_0000283833Add
    BLAST
    Chaini4123 – 4232110Non-structural protein 9By similarityPRO_0000283834Add
    BLAST
    Chaini4233 – 4369137Non-structural protein 10By similarityPRO_0000283835Add
    BLAST
    Chaini4370 – 5297928RNA-directed RNA polymeraseBy similarityPRO_0000037308Add
    BLAST
    Chaini5298 – 5900603HelicaseBy similarityPRO_0000283836Add
    BLAST
    Chaini5901 – 6421521ExoribonucleaseBy similarityPRO_0000283837Add
    BLAST
    Chaini6422 – 6796375Uridylate-specific endoribonucleaseBy similarityPRO_0000283838Add
    BLAST
    Chaini6797 – 7095299Putative 2'-O-methyl transferaseBy similarityPRO_0000283839Add
    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

    ProteinModelPortaliP0C6X6.
    SMRiP0C6X6. Positions 3964-4114, 4238-4362, 6422-6791.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2138 – 215821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2199 – 221921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2221 – 224121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2313 – 233321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2343 – 236321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2365 – 238521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2752 – 277221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2824 – 284421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3009 – 302921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3031 – 305121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3063 – 308321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3090 – 311021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3115 – 313521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3558 – 357821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3588 – 360821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3615 – 363521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3657 – 367721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3684 – 370421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3711 – 373121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3755 – 377521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1036 – 1274239Peptidase C16 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1275 – 1435161MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1631 – 1892262Peptidase C16 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini3247 – 3549303Peptidase C30PROSITE-ProRule annotationAdd
    BLAST
    Domaini4977 – 5139163RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini5298 – 538184CV MBDAdd
    BLAST
    Domaini5553 – 5734182(+)RNA virus helicase ATP-bindingAdd
    BLAST
    Domaini5735 – 5904170(+)RNA virus helicase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2138 – 2385248HD1By similarityAdd
    BLAST
    Regioni2752 – 3135384HD2By similarityAdd
    BLAST
    Regioni3319 – 3775457HD3By similarityAdd
    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.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1151 – 117929C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1749 – 178537C4-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4306 – 432217By similarityAdd
    BLAST
    Zinc fingeri4348 – 436114By 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.
    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.
    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.
    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: P0C6X6-1) [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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    MSKINKYGLE LHWAPEFPWM FEDAEEKLDN PSSSEVDMIC STTAQKLETD     50
    GICPENHVMV DCRRLLKQEC CVQSSLIREI VMNASPYHLE VLLQDALQSR 100
    EAVLVTTPLG MSLEACYVRG CNPKGWTMGL FRRRSVCNTG RCTVNKHVAY 150
    QLYMIDPAGV CLGAGQFVGW VIPLAFMPVQ SRKFIVPWVM YLRKRGEKGA 200
    YNKDHGCGGF GHVYDFKVED AYDQVHDEPK GKFSKKAYAL IRGYRGVKPL 250
    LYVDQYGCDY TGSLADGLEA YADKTLQEMK ALFPTWSQEL PFDVIVAWHV 300
    VRDPRYVMRL QSAATICSVA YVANPTEDLC DGSVVIKEPV HVYADDSIIL 350
    RQYNLFDIMS HFYMEADTVV NAFYGVALKD CGFVMQFGYI DCEQDSCDFK 400
    GWIPGNMIDG FACTTCGHVY EVGDLIAQSS GVLPVNPVLH TKSAAGYGGF 450
    GCKDSFTLYG QTVVYFGGCV YWSPARNIWI PILKSSVKSY DSLVYTGVLG 500
    CKAIVKETNL ICKALYLDYV QHKCGNLHQR ELLGVSDVWH KQLLINRGVY 550
    KPLLENIDYF NMRRAKFSLE TFTVCADGFM PFLLDDLVPR AYYLAVSGQA 600
    FCDYADKLCH AVVSKSKELL DVSLDSLGAA IHYLNSKIVD LAQHFSDFGT 650
    SFVSKIVHFF KTFTTSTALA FAWVLFHVLH GAYIVVESDI YFVKNIPRYA 700
    SAVAQAFQSV AKVVLDSLRV TFIDGLSCFK IGRRRICLSG RKIYEVERGL 750
    LHSSQLPLDV YDLTMPSQVQ KAKQKPIYLK GSGSDFSLAD SVVEVVTTSL 800
    TPCGYSEPPK VADKICIVDN VYMAKAGDKY YPVVVDDHVG LLDQAWRVPC 850
    AGRRVTFKEQ PTVKEIISMP KIIKVFYELD NDFNTILNTA CGVFEVDDTV 900
    DMEEFYAVVI DAIEEKLSPC KELEGVGAKV SAFLQKLEDN PLFLFDEAGE 950
    EVFAPKLYCA FTAPEDDDFL EESDVEEDDV EGEETDLTIT SAGQPCVASE 1000
    QEESSEVLED TLDDGPSVET SDSQVEEDVE MSDFVDLESV IQDYENVCFE 1050
    FYTTEPEFVK VLGLYVPKAT RNNCWLRSVL AVMQKLPCQF KDKNLQDLWV 1100
    LYKQQYSQLF VDTLVNKIPA NIVLPQGGYV ADFAYWFLTL CDWQCVAYWK 1150
    CIKCDLALKL KGLDAMFFYG DVVSHICKCG ESMVLIDVDV PFTAHFALKD 1200
    KLFCAFITKR IVYKAACVVD VNDSHSMAVV DGKQIDDHRI TSITSDKFDF 1250
    IIGHGMSFSM TTFEIAQLYG SCITPNVCFV KGDIIKVSKL VKAEVVVNPA 1300
    NGHMVHGGGV AKAIAVAAGQ QFVKETTNMV KSKGVCATGD CYVSTGGKLC 1350
    KTVLNVVGPD ARTQGKQSYV LLERVYKHFN NYDCVVTTLI SAGIFSVPSD 1400
    VSLTYLLGTA KKQVVLVSNN QEDFDLISKC QITAVEGTKK LAARLSFNVG 1450
    RSIVYETDAN KLILINDVAF VSTFNVLQDV LSLRHDIALD DDARTFVQSN 1500
    VDVLPEGWRV VNKFYQINGV RTVKYFECTG GIDICSQDKV FGYVQQGIFN 1550
    KATVAQIKAL FLDKVDILLT VDGVNFTNRF VPVGESFGKS LGNVFCDGVN 1600
    VTKHKCDINY KGKVFFQFDN LSSEDLKAVR SSFNFDQKEL LAYYNMLVNC 1650
    FKWQVVVNGK YFTFKQANNN CFVNVSCLML QSLHLTFKIV QWQEAWLEFR 1700
    SGRPARFVAL VLAKGGFKFG DPADSRDFLR VVFSQVDLTG AICDFEIACK 1750
    CGVKQEQRTG LDAVMHFGTL SREDLEIGYT VDCSCGKKLI HCVRFDVPFL 1800
    ICSNTPASVK LPKGVGSANI FIGDNVGHYV HVKCEQSYQL YDASNVKKVT 1850
    DVTGKLSDCL YLKNLKQTFK SVLTTYYLDD VKKIEYKPDL SQYYCDGGKY 1900
    YTQRIIKAQF KTFEKVDGVY TNFKLIGHTV CDSLNSKLGF DSSKEFVEYK 1950
    ITEWPTATGD VVLANDDLYV KRYERGCITF GKPVIWLSHE KASLNSLTYF 2000
    NRPLLVDDNK FDVLKVDDVD DSGDSSESGA KETKEINIIK LSGVKKPFKV 2050
    EDSVIVNDDT SETKYVKSLS IVDVYDMWLT GCKYVVRTAN ALSRAVNVPT 2100
    IRKFIKFGMT LVSIPIDLLN LREIKPAVNV VKAVRNKTSA CFNFIKWLFV 2150
    LLFGWIKISA DNKVIYTTEI ASKLTCKLVA LAFKNAFLTF KWSMVARGAC 2200
    IIATIFLLWF NFIYANVIFS DFYLPKIGFL PTFVGKIAQW IKNTFSLVTI 2250
    CDLYSIQDVG FKNQYCNGSI ACQFCLAGFD MLDNYKAIDV VQYEADRRAF 2300
    VDYTGVLKIV IELIVSYALY TAWFYPLFAL ISIQILTTWL PELFMLSTLH 2350
    WSFRLLVALA NMLPAHVFMR FYIIIASFIK LFSLFKHVAY GCSKSGCLFC 2400
    YKRNRSLRVK CSTIVGGMIR YYDVMANGGT GFCSKHQWNC IDCDSYKPGN 2450
    TFITVEAALD LSKELKRPIQ PTDVAYHTVT DVKQVGCSMR LFYDRDGQRI 2500
    YDDVNASLFV DYSNLLHSKV KSVPNMHVVV VENDADKANF LNAAVFYAQS 2550
    LFRPILMVDK NLITTANTGT SVTETMFDVY VDTFLSMFDV DKKSLNALIA 2600
    TAHSSIKQGT QIYKVLDTFL SCARKSCSID SDVDTKCLAD SVMSAVSAGL 2650
    ELTDESCNNL VPTYLKSDNI VAADLGVLIQ NSAKHVQGNV AKIAGVSCIW 2700
    SVDAFNQFSS DFQHKLKKAC CKTGLKLKLT YNKQMANVSV LTTPFSLKGG 2750
    AVFSYFVYVC FVLSLVCFIG LWCLMPTYTV HKSDFQLPVY ASYKVLDNGV 2800
    IRDVSVEDVC FANKFEQFDQ WYESTFGLSY YSNSMACPIV VAVIDQDFGS 2850
    TVFNVPTKVL RYGYHVLHFI THALSADGVQ CYTPHSQISY SNFYASGCVL 2900
    SSACTMFTMA DGSPQPYCYT DGLMQNASLY SSLVPHVRYN LANAKGFIRF 2950
    PEVLREGLVR VVRTRSMSYC RVGLCEEADE GICFNFNGSW VLNNDYYRSL 3000
    PGTFCGRDVF DLIYQLFKGL AQPVDFLALT ASSIAGAILA VIVVLVFYYL 3050
    IKLKRAFGDY TSVVFVNVIV WCVNFMMLFV FQVYPTLSCV YAICYFYATL 3100
    YFPSEISVIM HLQWLVMYGT IMPLWFCLLY IAVVVSNHAF WVFSYCRKLG 3150
    TSVRSDGTFE EMALTTFMIT KDSYCKLKNS LSDVAFNRYL SLYNKYRYYS 3200
    GKMDTAAYRE AACSQLAKAM DTFTNNNGSD VLYQPPTASV STSFLQSGIV 3250
    KMVNPTSKVE PCVVSVTYGN MTLNGLWLDD KVYCPRHVIC SASDMTNPDY 3300
    TNLLCRVTSS DFTVLFDRLS LTVMSYQMRG CMLVLTVTLQ NSRTPKYTFG 3350
    VVKPGETFTV LAAYNGKPQG AFHVTMRSSY TIKGSFLCGS CGSVGYVIMG 3400
    DCVKFVYMHQ LELSTGCHTG TDFNGDFYGP YKDAQVVQLP IQDYIQSVNF 3450
    LAWLYAAILN NCNWFIQSDK CSVEDFNVWA LSNGFSQVKS DLVIDALASM 3500
    TGVSLETLLA AIKRLKNGFQ GRQIMGSCSF EDELTPSDVY QQLAGIKLQS 3550
    KRTRLFKGTV CWIMASTFLF SCIITAFVKW TMFMYVTTNM FSITFCALCV 3600
    ISLAMLLVKH KHLYLTMYIT PVLFTLLYNN YLVVYKHTFR GYVYAWLSYY 3650
    VPSVEYTYTD EVIYGMLLLV GMVFVTLRSI NHDLFSFIMF VGRLISVFSL 3700
    WYKGSNLEEE ILLMLASLFG TYTWTTVLSM AVAKVIAKWV AVNVLYFTDI 3750
    PQIKIVLLCY LFIGYIISCY WGLFSLMNSL FRMPLGVYNY KISVQELRYM 3800
    NANGLRPPKN SFEALMLNFK LLGIGGVPII EVSQFQSKLT DVKCANVVLL 3850
    NCLQHLHVAS NSKLWHYCST LHNEILATSD LSVAFEKLAQ LLIVLFANPA 3900
    AVDSKCLTSI EEVCDDYAKD NTVLQALQSE FVNMASFVEY EVAKKNLDEA 3950
    RFSGSANQQQ LKQLEKACNI AKSAYERDRA VAKKLERMAD LALTNMYKEA 4000
    RINDKKSKVV SALQTMLFSM VRKLDNQALN SILDNAVKGC VPLNAIPSLA 4050
    ANTLNIIVPD KSVYDQIVDN IYVTYAGNVW QIQTIQDSDG TNKQLNEISD 4100
    DCNWPLVIIA NRYNEVSATV LQNNELMPAK LKIQVVNSGP DQTCNTPTQC 4150
    YYNNSNNGKI VYAILSDVDG LKYTKILKDD GNFVVLELDP PCKFTVQDAK 4200
    GLKIKYLYFV KGCNTLARGW VVGTISSTVR LQAGTATEYA SNSSILSLCA 4250
    FSVDPKKTYL DFIQQGGTPI ANCVKMLCDH AGTGMAITVK PDATTSQDSY 4300
    GGASVCIYCR ARVEHPDVDG LCKLRGKFVQ VPVGIKDPVS YVLTHDVCRV 4350
    CGFWRDGSCS CVSTDTTVQS KDTNFLNRVR GASVDARLVP CASGLSTDVQ 4400
    LRAFDIYNAS VAGIGLHLKV NCCRFQRVDE NGDKLDQFFV VKRTDLTIYN 4450
    REMKCYERVK DCKFVAEHDF FTFDVEGSRV PHIVRKDLTK YTMLDLCYAL 4500
    RHFDRNDCML LCDILSIYAG CEQSYFTKKD WYDFVENPDI INVYKKLGPI 4550
    FNRALVSATE FADKLVEVGL VGVLTLDNQD LNGKWYDFGD YVIAAPGCGV 4600
    AIADSYYSYI MPMLTMCHAL DCELYVNNAY RLFDLVQYDF TDYKLELFNK 4650
    YFKHWSMPYH PNTVDCQDDR CIIHCANFNI LFSMVLPNTC FGPLVRQIFV 4700
    DGVPFVVSIG YHYKELGIVM NMDVDTHRYR LSLKDLLLYA ADPALHVASA 4750
    SALYDLRTCC FSVAAITSGV KFQTVKPGNF NQDFYDFVLS KGLLKEGSSV 4800
    DLKHFFFTQD GNAAITDYNY YKYNLPTMVD IKQLLFVLEV VYKYFEIYDG 4850
    GCIPASQVIV NNYDKSAGYP FNKFGKARLY YEALSFEEQD EIYAYTKRNV 4900
    LPTLTQMNLK YAISAKNRAR TVAGVSILST MTGRMFHQKC LKSIAATRGV 4950
    PVVIGTTKFY GGWDDMLRRL IKDVDNPVLM GWDYPKCDRA MPNILRIVSS 5000
    LVLARKHETC CSQSDRFYRL ANECAQVLSE IVMCGGCYYV KPGGTSSGDA 5050
    TTAFANSVFN ICQAVSANVC ALMSCNGNKI EDLSIRALQK RLYSHVYRSD 5100
    KVDSTFVTEY YEFLNKHFSM MILSDDGVVC YNSDYASKGY IANISAFQQV 5150
    LYYQNNVFMS ESKCWVEHDI NNGPHEFCSQ HTMLVKMDGD DVYLPYPNPS 5200
    RILGAGCFVD DLLKTDSVLL IERFVSLAID AYPLVYHENE EYQKVFRVYL 5250
    AYIKKLYNDL GNQILDSYSV ILSTCDGQKF TDESFYKNMY LRSAVMQSVG 5300
    ACVVCSSQTS LRCGSCIRKP LLCCKCCYDH VMATDHKYVL SVSPYVCNAP 5350
    GCDVNDVTKL YLGGMSYYCE DHKPQYSFKL VMNGLVFGLY KQSCTGSPYI 5400
    DDFNRIASCK WTDVDDYILA NECTERLKLF AAETQKATEE AFKQSYASAT 5450
    IQEIVSEREL ILSWEIGKVK PPLNKNYVFT GYHFTKNGKT VLGEYVFDKS 5500
    ELTNGVYYRA TTTYKLSVGD VFVLTSHSVA NLSAPTLVPQ ENYSSIRFAS 5550
    VYSVLETFQN NVVNYQHIGM KRYCTVQGPP GTGKSHLAIG LAVFYCTARV 5600
    VYTAASHAAV DALCEKAYKF LNINDCTRIV PAKVRVECYD KFKINDTTRK 5650
    YVFTTINALP EMVTDIVVVD EVSMLTNYEL SVINARIRAK HYVYIGDPAQ 5700
    LPAPRVLLSK GTLEPKYFNT VTKLMCCLGP DIFLGTCYRC PKEIVDTVSA 5750
    LVYENKLKAK NESSLLCFKV YYKGVTTHES SSAVNMQQIY LINKFLKANP 5800
    LWHKAVFISP YNSQNFAAKR VLGLQTQTVD SAQGSEYDYV IYSQTAETAH 5850
    SVNVNRFNVA ITRAKKGILC VMSNMQLFEA LQFTTLTLDK VPQAVETKVQ 5900
    CSTNLFKDCS KSYSGYHPAH APSFLAVDDK YKATGDLAVC LGIGDSAVTY 5950
    SRLISLMGFK LDVTLDGYCK LFITKEEAVK RVRAWVGFDA EGAHATLDSI 6000
    GTNFPLQLGF STGIDFVVEA TGLFADRDGY SFKKAVAKAP PGEQFKHLIP 6050
    LMTRGHRWDV VRPRIVQMFA DHLIDLSDCV VLVTWAANFE LTCLRYFAKV 6100
    GREISCNVCT KRATVYNSRT GYYGCWRHSV TCDYLYNPLI VDIQQWGYIG 6150
    SLSSNHDLYC SVHKGAHVAS SDAIMTRCLA VYDCFCNNIN WNVEYPIISN 6200
    ELSINTSCRV LQRVILKAAM LCNRYTLCYD IGNPKGIACV KDFDFKFYDA 6250
    QPIVKSVKTL LYSFEAHKDS FKDGLCMFWN CNVDKYPPNA VVCRFDTRVL 6300
    NNLNLPGCNG GSLYVNKHAF HTKPFARAAF EHLKPMPFFY YSDTPCVYMD 6350
    GMDAKQVDYV PLKSATCITR CNLGGAVCLK HAEEYREYLE SYNTATTAGF 6400
    TFWVYKTFDF YNLWNTFTKL QSLENVVYNL VKTGHYTGQA GEMPCAIIND 6450
    KVVTKIDKED VVIFINNTTY PTNVAVELFA KRSVRHHPEL KLFRNLNIDV 6500
    CWKHVIWDYA RESIFCSNTY GVCMYTDLKF IDKLNVLFDG RDNGAFEAFK 6550
    RSNNGVYIST TKVKSLSMIR GPPRAELNGV VVDKVGDTDC VFYFAVRKEG 6600
    QDVIFSQFDS LGVSSNQSPQ GNLGSNGKPG NVGGNDALSI STIFTQSRVI 6650
    SSFTCRTDME KDFIALDQDV FIQKYGLEDY AFEHIVYGNF NQKIIGGLHL 6700
    LIGLYRRQQT SNLVVQEFVS YDSSIHSYFI TDEKSGGSKS VCTVIDILLD 6750
    DFVTLVKSLN LNCVSKVVNV NVDFKDFQFM LWCNDEKVMT FYPRLQAASD 6800
    WKPGYSMPVL YKYLNSPMER VSLWNYGKPV TLPTGCMMNV AKYTQLCQYL 6850
    NTTTLAVPVN MRVLHLGAGS EKGVAPGSAV LRQWLPAGTI LVDNDLYPFV 6900
    SDSVATYFGD CITLPFDCQW DLIISDMYDP ITKNIGEYNV SKDGFFTYIC 6950
    HMIRDKLALG GSVAIKITEF SWNAELYKLM GYFAFWTVFC TNANASSSEG 7000
    FLIGINYLCK PKVEIDGNVM HANYLFWRNS TVWNGGAYSL FDMAKFPLKL 7050
    AGTAVINLRA DQINDMVYSL LEKGKLLIRD TNKEVFVGDS LVNVI 7095

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

    Length:7,095
    Mass (Da):797,914
    Last modified:June 10, 2008 - v1
    Checksum:i157CDEBD4CE45D4A
    GO
    Isoform Replicase polyprotein 1a (identifier: P0C6U7-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1a, ORF1a polyprotein

    The sequence of this isoform can be found in the external entry P0C6U7.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by conventional translation.

    Length:4,383
    Mass (Da):491,305
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti426 – 4261I → M in AAT84359. (PubMed:15650185)Curated
    Sequence conflicti426 – 4261I → M in AAT84351. (PubMed:15650185)Curated
    Sequence conflicti813 – 8131D → A in AAT84359. (PubMed:15650185)Curated
    Sequence conflicti813 – 8131D → A in AAT84351. (PubMed:15650185)Curated
    Sequence conflicti4376 – 43772LN → FK in AAR01012. (PubMed:15280490)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti88 – 881H → D in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti207 – 2071C → R in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti291 – 2911P → L in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti317 – 3171C → R in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti356 – 3561F → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti545 – 5451I → L in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti762 – 7621D → N in strain: Isolate 87309 Belgium 2003.
    Natural varianti953 – 9531F → L in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
    Natural varianti989 – 9891I → V in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
    Natural varianti1305 – 13051V → A in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
    Natural varianti1328 – 13281N → D in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti1379 – 13791F → L in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti1504 – 15041L → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti1740 – 17401G → E in strain: Isolate 87309 Belgium 2003.
    Natural varianti1825 – 18251N → K in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti1936 – 19361S → A in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
    Natural varianti1965 – 19651N → T in strain: ATCC VR-759, Isolate clinical OC43-Paris.
    Natural varianti2004 – 20041L → S in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
    Natural varianti2022 – 20221S → G in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti2138 – 21403TSA → ISV in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti2256 – 22561I → M in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti2257 – 22571Q → H in strain: Isolate 87309 Belgium 2003.
    Natural varianti2386 – 23861K → R in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti2500 – 25001I → T in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
    Natural varianti2921 – 29211D → E in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti2961 – 29611V → I in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti3086 – 30861T → I in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti3440 – 34401P → L in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti3451 – 34511L → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti3466 – 34661I → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti4067 – 40671I → V in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti4071 – 40711I → V in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
    Natural varianti4382 – 43821A → T in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti4994 – 49941I → L in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate Tulsa 1999 and Isolate 87309 Belgium 2003.
    Natural varianti5014 – 50152SD → RT in strain: Isolate Tulsa 1999.
    Natural varianti5765 – 57651L → S in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
    Natural varianti5997 – 59971L → R in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti6236 – 62361G → A in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti6454 – 64541T → A in strain: ATCC VR-759 and Isolate clinical OC43-Paris.
    Natural varianti6546 – 65461F → L in strain: ATCC VR-759, Isolate clinical OC43-Paris and Isolate 87309 Belgium 2003.
    Natural varianti6636 – 66361D → E in strain: Isolate 87309 Belgium 2003.
    Natural varianti6665 – 66651A → T in strain: Isolate 87309 Belgium 2003.
    Natural varianti6754 – 67541T → A in strain: ATCC VR-759 and Isolate clinical OC43-Paris.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY903459 Genomic RNA. Translation: AAX85666.1.
    AY903460 Genomic RNA. Translation: AAX85675.1.
    AY585228 Genomic RNA. Translation: AAT84351.1.
    AY585229 Genomic RNA. Translation: AAT84359.1.
    AY391777 Genomic RNA. Translation: AAR01012.1.
    AF124989 Genomic RNA. Translation: AAD32993.1.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY903459 Genomic RNA. Translation: AAX85666.1 .
    AY903460 Genomic RNA. Translation: AAX85675.1 .
    AY585228 Genomic RNA. Translation: AAT84351.1 .
    AY585229 Genomic RNA. Translation: AAT84359.1 .
    AY391777 Genomic RNA. Translation: AAR01012.1 .
    AF124989 Genomic RNA. Translation: AAD32993.1 .

    3D structure databases

    ProteinModelPortali P0C6X6.
    SMRi P0C6X6. Positions 3964-4114, 4238-4362, 6422-6791.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C16.006.

    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.
    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.
    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.
    PS50507. RDRP_SSRNA_POS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Circulation of genetically distinct contemporary human coronavirus OC43 strains."
      Vijgen L., Keyaerts E., Lemey P., Moes E., Li S., Vandamme A.M., Van Ranst M.
      Virology 337:85-92(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate 19572 Belgium 2004 and Isolate 87309 Belgium 2003.
    2. "Human respiratory coronavirus OC43: genetic stability and neuroinvasion."
      St Jean J.R., Jacomy H., Desforges M., Vabret A., Freymuth F., Talbot P.J.
      J. Virol. 78:8824-8834(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate ATCC VR-759 and Isolate clinical OC43-Paris.
    3. "Complete genomic sequence of human coronavirus OC43: molecular clock analysis suggests a relatively recent zoonotic coronavirus transmission event."
      Vijgen L., Keyaerts E., Moes E., Thoelen I., Wollants E., Lemey P., Vandamme A.M., Van Ranst M.
      J. Virol. 79:1595-1604(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate ATCC VR-759.
    4. "Phylogenetic analysis of a highly conserved region of the polymerase gene from 11 coronaviruses and development of a consensus polymerase chain reaction assay."
      Stephensen C.B., Casebolt D.B., Gangopadhyay N.N.
      Virus Res. 60:181-189(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 4871-5177.
      Strain: Isolate Tulsa 1999.

    Entry informationi

    Entry nameiR1AB_CVHOC
    AccessioniPrimary (citable) accession number: P0C6X6
    Secondary accession number(s): Q4VID8
    , Q4VIE7, Q696Q1, Q6TNG2, Q9WAC3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The sequence shown is that of isolate 19572 Belgium 2004.

    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