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P0C6X1

- R1AB_CVH22

UniProt

P0C6X1 - R1AB_CVH22

Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Human coronavirus 229E (HCoV-229E)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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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 (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).
    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
    Sitei111 – 1122Cleavage; by PL1-PRO
    Sitei897 – 8982Cleavage; by PL1-PRO
    Active sitei1054 – 10541For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1205 – 12051For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1701 – 17011For PL2-PRO activityPROSITE-ProRule annotation
    Active sitei1863 – 18631For PL2-PRO activityPROSITE-ProRule annotation
    Sitei2484 – 24852Cleavage; by PL2-PRO
    Sitei2965 – 29662Cleavage; by 3CL-PRO
    Active sitei3006 – 30061For 3CL-PRO activity
    Active sitei3109 – 31091For 3CL-PRO activity
    Sitei3267 – 32682Cleavage; by 3CL-PRO
    Sitei3546 – 35472Cleavage; by 3CL-PRO
    Sitei3629 – 36302Cleavage; by 3CL-PRO
    Sitei3824 – 38252Cleavage; by 3CL-PRO
    Sitei3933 – 39342Cleavage; by 3CL-PRO
    Sitei4068 – 40692Cleavage; by 3CL-PRO
    Sitei4995 – 49962Cleavage; by 3CL-PRO
    Sitei5592 – 55932Cleavage; by 3CL-PRO
    Sitei6110 – 61112Cleavage; by 3CL-PRO
    Sitei6458 – 64592Cleavage; by 3CL-PRO

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1126 – 115732C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1780 – 181536C4-type 2; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4007 – 402317By similarityAdd
    BLAST
    Zinc fingeri4049 – 406214By similarityAdd
    BLAST
    Nucleotide bindingi5278 – 52858ATPCurated

    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
    p16
    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 229E (HCoV-229E)
    Taxonomic identifieri11137 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000006716: 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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1048 – 10481K → E: Complete loss of PL1-PRO activity. 1 Publication
    Mutagenesisi1054 – 10541C → A, G or S: Complete loss of PL1-PRO activity. 1 Publication
    Mutagenesisi1099 – 10991G → A: Complete loss of PL1-PRO activity. 1 Publication
    Mutagenesisi1099 – 10991G → P: No effect. 1 Publication
    Mutagenesisi1102 – 11021G → A or S: No effect. 1 Publication
    Mutagenesisi1126 – 11261C → D or H: Complete loss of PL1-PRO activity. 1 Publication
    Mutagenesisi1128 – 11281C → A, D or P: Complete loss of PL1-PRO activity. 1 Publication
    Mutagenesisi1154 – 11541C → A, H or D: Complete loss of PL1-PRO activity. 1 Publication
    Mutagenesisi1155 – 11551Missing: Complete loss of PL1-PRO activity. 1 Publication
    Mutagenesisi1157 – 11571C → A, D, H or P: Complete loss of PL1-PRO activity. 1 Publication
    Mutagenesisi1163 – 11631C → A or D: No effect. 1 Publication
    Mutagenesisi1175 – 11751V → H or P: Complete loss of PL1-PRO activity. 1 Publication
    Mutagenesisi1175 – 11751V → N or T: No effect. 1 Publication
    Mutagenesisi1203 – 12031C → A: Complete loss of PL1-PRO activity. 1 Publication
    Mutagenesisi1203 – 12031C → D: No effect. 1 Publication
    Mutagenesisi1218 – 12181D → A, E, H, K, N or Q: No effect. 1 Publication
    Mutagenesisi1702 – 17021W → L: Complete loss of PL2-PRO activity. 1 Publication
    Mutagenesisi3006 – 30061H → G, S, T or Y: Complete loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3028 – 30281H → G or T: No loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3029 – 30291N → A, D, E or Q: Increase of 3CL-PRO activity. 2 Publications
    Mutagenesisi3029 – 30291N → G: No loss of 3CL-PRO activity. 2 Publications
    Mutagenesisi3029 – 30291N → P: 95% loss of 3CL-PRO activity. 2 Publications
    Mutagenesisi3074 – 30741E → H: No loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3099 – 30991T → D: Complete loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3109 – 31091C → P, S or V: Complete loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3127 – 31271H → S: Complete loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3136 – 31361H → A: 67% loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3136 – 31361H → S: 77% loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3136 – 31361H → T: 93% loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3267 – 32671Q → A: No loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi5284 – 52841K → A: Almost complete loss of helicase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 111111Non-structural protein 1PRO_0000037293Add
    BLAST
    Chaini112 – 897786Non-structural protein 2PRO_0000037294Add
    BLAST
    Chaini898 – 24841587Non-structural protein 3PRO_0000037295Add
    BLAST
    Chaini2485 – 2965481Non-structural protein 4PRO_0000037296Add
    BLAST
    Chaini2966 – 32673023C-like proteinasePRO_0000037297Add
    BLAST
    Chaini3268 – 3546279Non-structural protein 6PRO_0000037298Add
    BLAST
    Chaini3547 – 362983Non-structural protein 7PRO_0000037299Add
    BLAST
    Chaini3630 – 3824195Non-structural protein 8PRO_0000037300Add
    BLAST
    Chaini3825 – 3933109Non-structural protein 9PRO_0000037301Add
    BLAST
    Chaini3934 – 4068135Non-structural protein 10PRO_0000037302Add
    BLAST
    Chaini4069 – 4995927RNA-directed RNA polymerasePRO_0000037303Add
    BLAST
    Chaini4996 – 5592597HelicasePRO_0000037304Add
    BLAST
    Chaini5593 – 6110518ExoribonucleaseBy similarityPRO_0000037305Add
    BLAST
    Chaini6111 – 6458348Uridylate-specific endoribonucleaseBy similarityPRO_0000037306Add
    BLAST
    Chaini6459 – 6758300Putative 2'-O-methyl transferaseBy similarityPRO_0000037307Add
    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.3 Publications

    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

    Secondary structure

    1
    6758
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1275 – 12784
    Beta strandi1281 – 12855
    Helixi1288 – 12947
    Beta strandi1298 – 13047
    Helixi1313 – 13219
    Turni1322 – 13243
    Helixi1325 – 133713
    Beta strandi1345 – 13506
    Beta strandi1353 – 13597
    Helixi1367 – 138014
    Beta strandi1381 – 13833
    Beta strandi1385 – 13873
    Helixi1393 – 13953
    Helixi1399 – 140911
    Beta strandi1415 – 14195
    Helixi1422 – 143312
    Helixi3829 – 38313
    Beta strandi3834 – 38429
    Helixi3843 – 38453
    Beta strandi3847 – 38559
    Beta strandi3858 – 38603
    Beta strandi3862 – 38698
    Beta strandi3873 – 38786
    Beta strandi3881 – 38833
    Beta strandi3885 – 38895
    Beta strandi3893 – 38975
    Beta strandi3904 – 39118
    Helixi3916 – 393015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P9SX-ray2.54A/B2966-3265[»]
    2J97X-ray1.75A3825-3933[»]
    2J98X-ray1.80A3825-3933[»]
    B3830-3933[»]
    3EJGX-ray1.78A1270-1434[»]
    ProteinModelPortaliP0C6X1.
    SMRiP0C6X1. Positions 2966-3265, 3827-3932, 3940-4064.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C6X1.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1925 – 194521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1998 – 201821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2068 – 208821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2095 – 211521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2491 – 251121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2731 – 275121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2755 – 277521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2782 – 280221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2809 – 282921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2834 – 285421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3281 – 330121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3304 – 332421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3328 – 334821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3367 – 338721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3401 – 342121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3422 – 344221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3467 – 348721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1016 – 1268253Peptidase C16 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1269 – 1436168MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1663 – 1914252Peptidase C16 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2966 – 3267302Peptidase C30PROSITE-ProRule annotationAdd
    BLAST
    Domaini4675 – 4837163RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini4996 – 507984CV MBDAdd
    BLAST
    Domaini5253 – 5434182(+)RNA virus helicase ATP-bindingAdd
    BLAST
    Domaini5435 – 5607173(+)RNA virus helicase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1925 – 2115191HD1Add
    BLAST
    Regioni2491 – 2854364HD2Add
    BLAST
    Regioni3281 – 3487207HD3Add
    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 fingeri1126 – 115732C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1780 – 181536C4-type 2; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4007 – 402317By similarityAdd
    BLAST
    Zinc fingeri4049 – 406214By 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.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    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.
    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.
    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: P0C6X1-1) [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

    MACNRVTLAV ASDSEISANG CSTIAQAVRR YSEAASNGFR ACRFVSLDLQ     50
    DCIVGIADDT YVMGLHGNQT LFCNIMKFSD RPFMLHGWLV FSNSNYLLEE 100
    FDVVFGKRGG GNVTYTDQYL CGADGKPVMS EDLWQFVDHF GENEEIIING 150
    HTYVCAWLTK RKPLDYKRQN NLAIEEIEYV HGDALHTLRN GSVLEMAKEV 200
    KTSSKVVLSD ALDKLYKVFG SPVMTNGSNI LEAFTKPVFI SALVQCTCGT 250
    KSWSVGDWTG FKSSCCNVIS NKLCVVPGNV KPGDAVITTQ QAGAGIKYFC 300
    GMTLKFVANI EGVSVWRVIA LQSVDCFVAS STFVEEEHVN RMDTFCFNVR 350
    NSVTDECRLA MLGAEMTSNV RRQVASGVID ISTGWFDVYD DIFAESKPWF 400
    VRKAEDIFGP CWSALASALK QLKVTTGELV RFVKSICNSA VAVVGGTIQI 450
    LASVPEKFLN AFDVFVTAIQ TVFDCAVETC TIAGKAFDKV FDYVLLDNAL 500
    VKLVTTKLKG VRERGLNKVK YATVVVGSTE EVKSSRVERS TAVLTIANNY 550
    SKLFDEGYTV VIGDVAYFVS DGYFRLMASP NSVLTTAVYK PLFAFNVNVM 600
    GTRPEKFPTT VTCENLESAV LFVNDKITEF QLDYSIDVID NEIIVKPNIS 650
    LCVPLYVRDY VDKWDDFCRQ YSNESWFEDD YRAFISVLDI TDAAVKAAES 700
    KAFVDTIVPP CPSILKVIDG GKIWNGVIKN VNSVRDWLKS LKLNLTQQGL 750
    LGTCAKRFKR WLGILLEAYN AFLDTVVSTV KIGGLTFKTY AFDKPYIVIR 800
    DIVCKVENKT EAEWIELFPH NDRIKSFSTF ESAYMPIADP THFDIEEVEL 850
    LDAEFVEPGC GGILAVIDEH VFYKKDGVYY PSNGTNILPV AFTKAAGGKV 900
    SFSDDVEVKD IEPVYRVKLC FEFEDEKLVD VCEKAIGKKI KHEGDWDSFC 950
    KTIQSALSVV SCYVNLPTYY IYDEEGGNDL SLPVMISEWP LSVQQAQQEA 1000
    TLPDIAEDVV DQVEEVNSIF DIETVDVKHD VSPFEMPFEE LNGLKILKQL 1050
    DNNCWVNSVM LQIQLTGILD GDYAMQFFKM GRVAKMIERC YTAEQCIRGA 1100
    MGDVGLCMYR LLKDLHTGFM VMDYKCSCTS GRLEESGAVL FCTPTKKAFP 1150
    YGTCLNCNAP RMCTIRQLQG TIIFVQQKPE PVNPVSFVVK PVCSSIFRGA 1200
    VSCGHYQTNI YSQNLCVDGF GVNKIQPWTN DALNTICIKD ADYNAKVEIS 1250
    VTPIKNTVDT TPKEEFVVKE KLNAFLVHDN VAFYQGDVDT VVNGVDFDFI 1300
    VNAANENLAH GGGLAKALDV YTKGKLQRLS KEHIGLAGKV KVGTGVMVEC 1350
    DSLRIFNVVG PRKGKHERDL LIKAYNTINN EQGTPLTPIL SCGIFGIKLE 1400
    TSLEVLLDVC NTKEVKVFVY TDTEVCKVKD FVSGLVNVQK VEQPKIEPKP 1450
    VSVIKVAPKP YRVDGKFSYF TEDLLCVADD KPIVLFTDSM LTLDDRGLAL 1500
    DNALSGVLSA AIKDCVDINK AIPSGNLIKF DIGSVVVYMC VVPSEKDKHL 1550
    DNNVQRCTRK LNRLMCDIVC TIPADYILPL VLSSLTCNVS FVGELKAAEA 1600
    KVITIKVTED GVNVHDVTVT TDKSFEQQVG VIADKDKDLS GAVPSDLNTS 1650
    ELLTKAIDVD WVEFYGFKDA VTFATVDHSA FAYESAVVNG IRVLKTSDNN 1700
    CWVNAVCIAL QYSKPHFISQ GLDAAWNKFV LGDVEIFVAF VYYVARLMKG 1750
    DKGDAEDTLT KLSKYLANEA QVQLEHYSSC VECDAKFKNS VASINSAIVC 1800
    ASVKRDGVQV GYCVHGIKYY SRVRSVRGRA IIVSVEQLEP CAQSRLLSGV 1850
    AYTAFSGPVD KGHYTVYDTA KKSMYDGDRF VKHDLSLLSV TSVVMVGGYV 1900
    APVNTVKPKP VINQLDEKAQ KFFDFGDFLI HNFVIFFTWL LSMFTLCKTA 1950
    VTTGDVKIMA KAPQRTGVVL KRSLKYNLKA SAAVLKSKWW LLAKFTKLLL 2000
    LIYTLYSVVL LCVRFGPFNF CSETVNGYAK SNFVKDDYCD GSLGCKMCLF 2050
    GYQELSQFSH LDVVWKHITD PLFSNMQPFI VMVLLLIFGD NYLRCFLLYF 2100
    VAQMISTVGV FLGYKETNWF LHFIPFDVIC DELLVTVIVI KVISFVRHVL 2150
    FGCENPDCIA CSKSARLKRF PVNTIVNGVQ RSFYVNANGG SKFCKKHRFF 2200
    CVDCDSYGYG STFITPEVSR ELGNITKTNV QPTGPAYVMI DKVEFENGFY 2250
    RLYSCETFWR YNFDITESKY SCKEVFKNCN VLDDFIVFNN NGTNVTQVKN 2300
    ASVYFSQLLC RPIKLVDSEL LSTLSVDFNG VLHKAYIDVL RNSFGKDLNA 2350
    NMSLAECKRA LGLSISDHEF TSAISNAHRC DVLLSDLSFN NFVSSYAKPE 2400
    EKLSAYDLAC CMRAGAKVVN ANVLTKDQTP IVWHAKDFNS LSAEGRKYIV 2450
    KTSKAKGLTF LLTINENQAV TQIPATSIVA KQGAGDAGHS LTWLWLLCGL 2500
    VCLIQFYLCF FMPYFMYDIV SSFEGYDFKY IENGQLKNFE APLKCVRNVF 2550
    ENFEDWHYAK FGFTPLNKQS CPIVVGVSEI VNTVAGIPSN VYLVGKTLIF 2600
    TLQAAFGNAG VCYDIFGVTT PEKCIFTSAC TRLEGLGGNN VYCYNTALME 2650
    GSLPYSSIQA NAYYKYDNGN FIKLPEVIAQ GFGFRTVRTI ATKYCRVGEC 2700
    VESNAGVCFG FDKWFVNDGR VANGYVCGTG LWNLVFNILS MFSSSFSVAA 2750
    MSGQILLNCA LGAFAIFCCF LVTKFRRMFG DLSVGVCTVV VAVLLNNVSY 2800
    IVTQNLVTMI AYAILYFFAT RSLRYAWIWC AAYLIAYISF APWWLCAWYF 2850
    LAMLTGLLPS LLKLKVSTNL FEGDKFVGTF ESAAAGTFVI DMRSYEKLAN 2900
    SISPEKLKSY AASYNRYKYY SGNANEADYR CACYAYLAKA MLDFSRDHND 2950
    ILYTPPTVSY GSTLQAGLRK MAQPSGFVEK CVVRVCYGNT VLNGLWLGDI 3000
    VYCPRHVIAS NTTSAIDYDH EYSIMRLHNF SIISGTAFLG VVGATMHGVT 3050
    LKIKVSQTNM HTPRHSFRTL KSGEGFNILA CYDGCAQGVF GVNMRTNWTI 3100
    RGSFINGACG SPGYNLKNGE VEFVYMHQIE LGSGSHVGSS FDGVMYGGFE 3150
    DQPNLQVESA NQMLTVNVVA FLYAAILNGC TWWLKGEKLF VEHYNEWAQA 3200
    NGFTAMNGED AFSILAAKTG VCVERLLHAI QVLNNGFGGK QILGYSSLND 3250
    EFSINEVVKQ MFGVNLQSGK TTSMFKSISL FAGFFVMFWA ELFVYTTTIW 3300
    VNPGFLTPFM ILLVALSLCL TFVVKHKVLF LQVFLLPSII VAAIQNCAWD 3350
    YHVTKVLAEK FDYNVSVMQM DIQGFVNIFI CLFVALLHTW RFAKERCTHW 3400
    CTYLFSLIAV LYTALYSYDY VSLLVMLLCA ISNEWYIGAI IFRICRFGVA 3450
    FLPVEYVSYF DGVKTVLLFY MLLGFVSCMY YGLLYWINRF CKCTLGVYDF 3500
    CVSPAEFKYM VANGLNAPNG PFDALFLSFK LMGIGGPRTI KVSTVQSKLT 3550
    DLKCTNVVLM GILSNMNIAS NSKEWAYCVE MHNKINLCDD PETAQELLLA 3600
    LLAFFLSKHS DFGLGDLVDS YFENDSILQS VASSFVGMPS FVAYETARQE 3650
    YENAVANGSS PQIIKQLKKA MNVAKAEFDR ESSVQKKINR MAEQAAAAMY 3700
    KEARAVNRKS KVVSAMHSLL FGMLRRLDMS SVDTILNMAR NGVVPLSVIP 3750
    ATSAARLVVV VPDHDSFVKM MVDGFVHYAG VVWTLQEVKD NDGKNVHLKD 3800
    VTKENQEILV WPLILTCERV VKLQNNEIMP GKMKVKATKG EGDGGITSEG 3850
    NALYNNEGGR AFMYAYVTTK PGMKYVKWEH DSGVVTVELE PPCRFVIDTP 3900
    TGPQIKYLYF VKNLNNLRRG AVLGYIGATV RLQAGKQTEF VSNSHLLTHC 3950
    SFAVDPAAAY LDAVKQGAKP VGNCVKMLTN GSGSGQAITC TIDSNTTQDT 4000
    YGGASVCIYC RAHVAHPTMD GFCQYKGKWV QVPIGTNDPI RFCLENTVCK 4050
    VCGCWLNHGC TCDRTAIQSF DNSYLNRVRG SSAARLEPCN GTDIDYCVRA 4100
    FDVYNKDASF IGKNLKSNCV RFKNVDKDDA FYIVKRCIKS VMDHEQSMYN 4150
    LLKGCNAVAK HDFFTWHEGR TIYGNVSRQD LTKYTMMDLC FALRNFDEKD 4200
    CEVFKEILVL TGCCSTDYFE MKNWFDPIEN EDIHRVYAAL GKVVANAMLK 4250
    CVAFCDEMVL KGVVGVLTLD NQDLNGNFYD FGDFVLCPPG MGIPYCTSYY 4300
    SYMMPVMGMT NCLASECFMK SDIFGQDFKT FDLLKYDFTE HKEVLFNKYF 4350
    KYWGQDYHPD CVDCHDEMCI LHCSNFNTLF ATTIPNTAFG PLCRKVFIDG 4400
    VPVVATAGYH FKQLGLVWNK DVNTHSTRLT ITELLQFVTD PTLIVASSPA 4450
    LVDKRTVCFS VAALSTGLTS QTVKPGHFNK EFYDFLRSQG FFDEGSELTL 4500
    KHFFFTQKGD AAIKDFDYYR YNRPTMLDIG QARVAYQVAA RYFDCYEGGC 4550
    ITSREVVVTN LNKSAGWPLN KFGKAGLYYE SISYEEQDAI FSLTKRNILP 4600
    TMTQLNLKYA ISGKERARTV GGVSLLATMT TRQFHQKCLK SIVATRNATV 4650
    VIGTTKFYGG WDNMLKNLMA DVDDPKLMGW DYPKCDRAMP SMIRMLSAMI 4700
    LGSKHVTCCT ASDKFYRLSN ELAQVLTEVV YSNGGFYFKP GGTTSGDATT 4750
    AYANSVFNIF QAVSSNINCV LSVNSSNCNN FNVKKLQRQL YDNCYRNSNV 4800
    DESFVDDFYG YLQKHFSMMI LSDDSVVCYN KTYAGLGYIA DISAFKATLY 4850
    YQNGVFMSTA KCWTEEDLSI GPHEFCSQHT MQIVDENGKY YLPYPDPSRI 4900
    ISAGVFVDDI TKTDAVILLE RYVSLAIDAY PLSKHPKPEY RKVFYALLDW 4950
    VKHLNKTLNE GVLESFSVTL LDEHESKFWD ESFYASMYEK STVLQAAGLC 5000
    VVCGSQTVLR CGDCLRRPML CTKCAYDHVF GTDHKFILAI TPYVCNTSGC 5050
    NVNDVTKLYL GGLNYYCVDH KPHLSFPLCS AGNVFGLYKS SALGSMDIDV 5100
    FNKLSTSDWS DIRDYKLAND AKESLRLFAA ETVKAKEESV KSSYAYATLK 5150
    EIVGPKELLL LWESGKAKPP LNRNSVFTCF QITKDSKFQV GEFVFEKVDY 5200
    GSDTVTYKST ATTKLVPGML FILTSHNVAP LRAPTMANQE KYSTIYKLHP 5250
    SFNVSDAYAN LVPYYQLIGK QRITTIQGPP GSGKSHCSIG IGVYYPGARI 5300
    VFTACSHAAV DSLCAKAVTA YSVDKCTRII PARARVECYS GFKPNNNSAQ 5350
    YVFSTVNALP EVNADIVVVD EVSMCTNYDL SVINQRISYK HIVYVGDPQQ 5400
    LPAPRVLISK GVMEPIDYNV VTQRMCAIGP DVFLHKCYRC PAEIVNTVSE 5450
    LVYENKFVPV KEASKQCFKI FERGSVQVDN GSSINRRQLD VVKRFIHKNS 5500
    TWSKAVFISP YNSQNYVAAR LLGLQTQTVD SAQGSEYDYV IFAQTSDTAH 5550
    ACNANRFNVA ITRAKKGIFC IMSDRTLFDA LKFFEITMTD LQSESSCGLF 5600
    KDCARNPIDL PPSHATTYLS LSDRFKTSGD LAVQIGNNNV CTYEHVISYM 5650
    GFRFDVSMPG SHSLFCTRDF AMRHVRGWLG MDVEGAHVTG DNVGTNVPLQ 5700
    VGFSNGVDFV AQPEGCVLTN TGSVVKPVRA RAPPGEQFTH IVPLLRKGQP 5750
    WSVLRKRIVQ MIADFLAGSS DVLVFVLWAG GLELTTMRYF VKIGAVKHCQ 5800
    CGTVATCYNS VSNDYCCFKH ALGCDYVYNP YVIDIQQWGY VGSLSTNHHA 5850
    ICNVHRNEHV ASGDAIMTRC LAVYDCFVKN VDWSITYPMI ANENAINKGG 5900
    RTVQSHIMRA AIKLYNPKAI HDIGNPKGIR CAVTDAKWYC YDKNPINSNV 5950
    KTLEYDYMTH GQMDGLCLFW NCNVDMYPEF SIVCRFDTRT RSTLNLEGVN 6000
    GGSLYVNNHA FHTPAYDKRA MAKLKPAPFF YYDDGSCEVV HDQVNYVPLR 6050
    ATNCITKCNI GGAVCSKHAN LYRAYVESYN IFTQAGFNIW VPTTFDCYNL 6100
    WQTFTEVNLQ GLENIAFNVV NKGSFVGADG ELPVAISGDK VFVRDGNTDN 6150
    LVFVNKTSLP TNIAFELFAK RKVGLTPPLS ILKNLGVVAT YKFVLWDYEA 6200
    ERPLTSFTKS VCGYTDFAED VCTCYDNSIQ GSYERFTLST NAVLFSATAV 6250
    KTGGKSLPAI KLNFGMLNGN AIATVKSEDG NIKNINWFVY VRKDGKPVDH 6300
    YDGFYTQGRN LQDFLPRSTM EEDFLNMDIG VFIQKYGLED FNFEHVVYGD 6350
    VSKTTLGGLH LLISQVRLSK MGILKAEEFV AASDITLKCC TVTYLNDPSS 6400
    KTVCTYMDLL LDDFVSVLKS LDLTVVSKVH EVIIDNKPWR WMLWCKDNAV 6450
    ATFYPQLQSA EWKCGYSMPG IYKTQRMCLE PCNLYNYGAG LKLPSGIMFN 6500
    VVKYTQLCQY FNSTTLCVPH NMRVLHLGAG SDYGVAPGTA VLKRWLPHDA 6550
    IVVDNDVVDY VSDADFSVTG DCATVYLEDK FDLLISDMYD GRTKAIDGEN 6600
    VSKEGFFTYI NGFICEKLAI GGSIAIKVTE YSWNKKLYEL VQRFSFWTMF 6650
    CTSVNTSSSE AFVVGINYLG DFAQGPFIDG NIIHANYVFW RNSTVMSLSY 6700
    NSVLDLSKFN CKHKATVVVQ LKDSDINEMV LSLVRSGKLL VRGNGKCLSF 6750
    SNHLVSTK 6758

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

    Length:6,758
    Mass (Da):754,163
    Last modified:June 10, 2008 - v1
    Checksum:iB7EC2ABD7FE4EC1A
    GO
    Isoform Replicase polyprotein 1a (identifier: P0C6U2-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1a, ORF1a polyprotein

    The sequence of this isoform can be found in the external entry P0C6U2.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by conventional translation.

    Length:4,085
    Mass (Da):454,215
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1982 – 19821A → Q Ref (PubMed:11369870)Curated
    Sequence conflicti1982 – 19821A → Q 1 (PubMed:11369870)Curated
    Sequence conflicti4042 – 40421F → S Ref (PubMed:11369870)Curated
    Sequence conflicti4042 – 40421F → S 1 (PubMed:11369870)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF304460 Genomic RNA. Translation: AAG48591.1.
    PIRiS28600.
    RefSeqiNP_073549.1. NC_002645.1. [P0C6X1-1]

    Genome annotation databases

    GeneIDi918764.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Proteic grace - Issue 77 of December 2006

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF304460 Genomic RNA. Translation: AAG48591.1 .
    PIRi S28600.
    RefSeqi NP_073549.1. NC_002645.1. [P0C6X1-1 ]

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P9S X-ray 2.54 A/B 2966-3265 [» ]
    2J97 X-ray 1.75 A 3825-3933 [» ]
    2J98 X-ray 1.80 A 3825-3933 [» ]
    B 3830-3933 [» ]
    3EJG X-ray 1.78 A 1270-1434 [» ]
    ProteinModelPortali P0C6X1.
    SMRi P0C6X1. Positions 2966-3265, 3827-3932, 3940-4064.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 918764.

    Miscellaneous databases

    EvolutionaryTracei P0C6X1.

    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.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    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.
    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.
    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. "Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus."
      Thiel V., Herold J., Schelle B., Siddell S.G.
      J. Gen. Virol. 82:1273-1281(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Nucleotide sequence of the human coronavirus 229E RNA polymerase locus."
      Herold J., Raabe T., Schelle-Prinz B., Siddell S.G.
      Virology 195:680-691(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-4085.
    3. "Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase."
      Ziebuhr J., Heusipp G., Siddell S.G.
      J. Virol. 71:3992-3997(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF 3CL-PRO, MUTAGENESIS OF HIS-3006; HIS-3028; ASN-3029; GLU-3074; THR-3099; CYS-3109; HIS-3127; HIS-3136 AND GLN-3267.
    4. "Identification and subcellular localization of a 41 kDa, polyprotein 1ab processing product in human coronavirus 229E-infected cells."
      Heusipp G., Groetzinger C., Herold J., Siddell S.G., Ziebuhr J.
      J. Gen. Virol. 78:2789-2794(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF P41, SUBCELLULAR LOCATION.
    5. "The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5'-to-3' polarity."
      Seybert A., Hegyi A., Siddell S.G., Ziebuhr J.
      RNA 6:1056-1068(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF HELICASE, MUTAGENESIS OF LYS-5284.
    6. "A human RNA viral cysteine proteinase that depends upon a unique Zn2+-binding finger connecting the two domains of a papain-like fold."
      Herold J., Siddell S.G., Gorbalenya A.E.
      J. Biol. Chem. 274:14918-14925(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ZINC-FINGER DOMAIN OF PL1-PRO, MUTAGENESIS OF LYS-1048; GLY-1099; GLY-1102; CYS-1126; CYS-1128; CYS-1154; LEU-1155; CYS-1157; CYS-1163; VAL-1175; CYS-1203 AND ASP-1218.
    7. Erratum
      Herold J., Siddell S.G., Gorbalenya A.E.
      J. Biol. Chem. 274:21490-21490(1999)
    8. "Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: identification of proteolytic products and cleavage sites common to pp1a and pp1ab."
      Ziebuhr J., Siddell S.G.
      J. Virol. 73:177-185(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    9. "The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond."
      Ziebuhr J., Thiel V., Gorbalenya A.E.
      J. Biol. Chem. 276:33220-33232(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF CYS-1054 AND TRP-1702.
    10. "Conservation of substrate specificities among coronavirus main proteases."
      Hegyi A., Ziebuhr J.
      J. Gen. Virol. 83:595-599(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    11. "Mutational analysis of the active centre of coronavirus 3C-like proteases."
      Hegyi A., Friebe A., Gorbalenya A.E., Ziebuhr J.
      J. Gen. Virol. 83:581-593(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASN-3029.
    12. "Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs."
      Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., Hilgenfeld R.
      Science 300:1763-1767(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 2966-3265.

    Entry informationi

    Entry nameiR1AB_CVH22
    AccessioniPrimary (citable) accession number: P0C6X1
    Secondary accession number(s): Q05002, Q9DLN0, Q9DLN1
    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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3