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P0C6U8

- R1A_CVHSA

UniProt

P0C6U8 - R1A_CVHSA

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Human SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome coronavirus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO 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.
    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 By similarity. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function.PROSITE-ProRule annotation
    Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter.
    Nsp9 is a ssRNA-binding protein.
    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. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.

    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).
    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei180 – 1812CleavageBy similarity
    Sitei818 – 8192Cleavage; by PL-PROBy similarity
    Active sitei1651 – 16511For PL-PRO activityPROSITE-ProRule annotation
    Active sitei1812 – 18121For PL-PRO activityPROSITE-ProRule annotation
    Sitei2740 – 27412Cleavage; by PL-PROBy similarity
    Sitei3240 – 32412Cleavage; by 3CL-PROBy similarity
    Active sitei3281 – 32811For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3385 – 33851For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3546 – 35472Cleavage; by 3CL-PROBy similarity
    Sitei3836 – 38372Cleavage; by 3CL-PROBy similarity
    Sitei3919 – 39202Cleavage; by 3CL-PROBy similarity
    Sitei4117 – 41182Cleavage; by 3CL-PROBy similarity
    Sitei4230 – 42312Cleavage; by 3CL-PROBy similarity
    Metal bindingi4304 – 43041Zinc
    Metal bindingi4307 – 43071Zinc
    Metal bindingi4313 – 43131Zinc
    Metal bindingi4320 – 43201Zinc
    Metal bindingi4347 – 43471Zinc
    Metal bindingi4350 – 43501Zinc
    Metal bindingi4358 – 43581Zinc
    Sitei4369 – 43702Cleavage; by 3CL-PROBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1729 – 176638C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4304 – 432017Add
    BLAST
    Zinc fingeri4347 – 436014Add
    BLAST

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: InterPro
    2. endonuclease activity Source: UniProtKB-KW
    3. hydrolase activity, acting on acid anhydrides Source: InterPro
    4. omega peptidase activity Source: InterPro
    5. RNA binding Source: UniProtKB-KW
    6. RNA-directed RNA polymerase activity Source: InterPro
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. induction by virus of catabolism of host mRNA Source: UniProtKB-KW
    2. induction by virus of host autophagy Source: UniProtKB-KW
    3. modulation by virus of host protein ubiquitination Source: UniProtKB-KW
    4. suppression by virus of host IRF3 activity Source: UniProtKB-KW
    5. suppression by virus of host ISG15 activity Source: UniProtKB-KW
    6. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
    7. viral genome replication Source: InterPro
    8. viral protein processing Source: InterPro

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease, Protease, Thiol protease

    Keywords - Biological processi

    Activation of host autophagy by virus, Decay of host mRNAs by virus, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host IRF3 by virus, Inhibition of host ISG15 by virus, Inhibition of host RLR pathway by virus, Modulation of host ubiquitin pathway by viral deubiquitinase, Modulation of host ubiquitin pathway by virus, Ubl conjugation pathway, Viral immunoevasion

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Replicase polyprotein 1a
    Short name:
    pp1a
    Alternative name(s):
    ORF1a polyprotein
    Cleaved into the following 11 chains:
    Non-structural protein 1
    Short name:
    nsp1
    Alternative name(s):
    Leader protein
    Non-structural protein 2
    Short name:
    nsp2
    Alternative name(s):
    p65 homolog
    Alternative name(s):
    PL2-PRO
    Papain-like proteinase
    Short name:
    PL-PRO
    SARS coronavirus main proteinase
    Non-structural protein 4
    Short name:
    nsp4
    3C-like proteinase (EC:3.4.22.-)
    Short name:
    3CL-PRO
    Short name:
    3CLp
    Alternative name(s):
    nsp5
    Non-structural protein 6
    Short name:
    nsp6
    Non-structural protein 7
    Short name:
    nsp7
    Non-structural protein 8
    Short name:
    nsp8
    Non-structural protein 9
    Short name:
    nsp9
    Non-structural protein 10
    Short name:
    nsp10
    Alternative name(s):
    Growth factor-like peptide
    Short name:
    GFL
    Non-structural protein 11
    Short name:
    nsp11
    Gene namesi
    ORF Names:1a
    OrganismiHuman SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome coronavirus)
    Taxonomic identifieri227859 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    Paguma larvata (Masked palm civet) [TaxID: 9675]
    ProteomesiUP000000354: 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

    GO - Cellular componenti

    1. host cell membrane Source: UniProtKB-SubCell
    2. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Host cytoplasm, Host membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 43824382Replicase polyprotein 1aPRO_0000338254Add
    BLAST
    Chaini1 – 180180Non-structural protein 1By similarityPRO_0000338255Add
    BLAST
    Chaini181 – 818638Non-structural protein 2By similarityPRO_0000338256Add
    BLAST
    Chaini819 – 27401922Non-structural protein 3By similarityPRO_0000338257Add
    BLAST
    Chaini2741 – 3240500Non-structural protein 4Sequence AnalysisPRO_0000338258Add
    BLAST
    Chaini3241 – 35463063C-like proteinaseBy similarityPRO_0000338259Add
    BLAST
    Chaini3547 – 3836290Non-structural protein 6By similarityPRO_0000338260Add
    BLAST
    Chaini3837 – 391983Non-structural protein 7By similarityPRO_0000338261Add
    BLAST
    Chaini3920 – 4117198Non-structural protein 8By similarityPRO_0000338262Add
    BLAST
    Chaini4118 – 4230113Non-structural protein 9By similarityPRO_0000338263Add
    BLAST
    Chaini4231 – 4369139Non-structural protein 10By similarityPRO_0000338264Add
    BLAST
    Chaini4370 – 438213Non-structural protein 11Sequence AnalysisPRO_0000338265Add
    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

    Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer.

    Protein-protein interaction databases

    DIPiDIP-48580N.

    Structurei

    Secondary structure

    1
    4382
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1208 – 12114
    Beta strandi1214 – 12163
    Helixi1219 – 12224
    Turni1223 – 12253
    Beta strandi1229 – 12335
    Beta strandi1235 – 12373
    Helixi1241 – 12444
    Helixi1253 – 12553
    Turni1256 – 12583
    Beta strandi1266 – 12694
    Beta strandi1272 – 12765
    Helixi1280 – 12823
    Helixi1286 – 12938
    Beta strandi1298 – 13036
    Beta strandi1309 – 13124
    Helixi1315 – 132410
    Beta strandi1325 – 13317
    Helixi1343 – 13453
    Helixi1351 – 136111
    Beta strandi1364 – 13685
    Helixi1372 – 138110
    Turni1382 – 13843
    Beta strandi1389 – 140113
    Beta strandi1403 – 14053
    Helixi1407 – 141711
    Beta strandi1421 – 14233
    Turni1429 – 14313
    Helixi1435 – 14428
    Beta strandi1449 – 14524
    Helixi1456 – 146712
    Helixi1473 – 148412
    Beta strandi1485 – 14873
    Beta strandi1500 – 15067
    Beta strandi1509 – 15135
    Beta strandi1515 – 15184
    Beta strandi1521 – 15233
    Beta strandi1526 – 15283
    Helixi1530 – 15378
    Beta strandi1544 – 155512
    Beta strandi1557 – 15626
    Beta strandi1563 – 15653
    Helixi1567 – 15704
    Beta strandi1571 – 15766
    Helixi1581 – 15833
    Helixi1588 – 15903
    Beta strandi1594 – 15974
    Helixi1602 – 161211
    Helixi1619 – 163012
    Turni1648 – 16503
    Helixi1651 – 166010
    Beta strandi1667 – 16693
    Helixi1670 – 168011
    Helixi1685 – 169511
    Helixi1705 – 17139
    Beta strandi1722 – 17298
    Turni1730 – 17323
    Beta strandi1733 – 17408
    Helixi1741 – 17444
    Beta strandi1746 – 17494
    Helixi1753 – 17586
    Beta strandi1760 – 17634
    Beta strandi1767 – 179428
    Beta strandi1799 – 18068
    Helixi1808 – 18103
    Beta strandi1811 – 182616
    Beta strandi1829 – 184618
    Beta strandi1848 – 18514
    Helixi3251 – 32544
    Beta strandi3257 – 32626
    Beta strandi3265 – 32728
    Beta strandi3275 – 32795
    Helixi3280 – 32834
    Helixi3286 – 32883
    Beta strandi3289 – 32913
    Helixi3294 – 32996
    Helixi3303 – 33053
    Beta strandi3306 – 33105
    Beta strandi3313 – 33153
    Beta strandi3317 – 33237
    Beta strandi3326 – 33338
    Beta strandi3340 – 33434
    Beta strandi3351 – 33588
    Beta strandi3361 – 33699
    Turni3380 – 33834
    Beta strandi3388 – 33936
    Beta strandi3396 – 340611
    Turni3408 – 34103
    Beta strandi3412 – 34154
    Beta strandi3417 – 34193
    Beta strandi3421 – 34244
    Beta strandi3427 – 34304
    Helixi3441 – 345313
    Turni3458 – 34603
    Helixi3467 – 347610
    Helixi3484 – 34896
    Helixi3491 – 34977
    Helixi3501 – 351414
    Beta strandi3521 – 35233
    Beta strandi3524 – 35263
    Helixi3533 – 35397
    Beta strandi3541 – 35433
    Helixi3847 – 38548
    Turni3855 – 38573
    Helixi3864 – 387613
    Beta strandi3878 – 38814
    Helixi3882 – 38887
    Turni3889 – 38913
    Helixi3892 – 38987
    Helixi3904 – 39118
    Helixi3913 – 39164
    Beta strandi4127 – 413610
    Turni4137 – 41393
    Beta strandi4142 – 41509
    Turni4152 – 41543
    Beta strandi4157 – 41648
    Beta strandi4170 – 41734
    Beta strandi4176 – 41794
    Beta strandi4180 – 41867
    Beta strandi4190 – 41945
    Beta strandi4201 – 42088
    Helixi4213 – 422412
    Helixi4240 – 42489
    Beta strandi4250 – 42523
    Helixi4253 – 426210
    Beta strandi4273 – 42753
    Beta strandi4284 – 42885
    Beta strandi4295 – 42995
    Helixi4301 – 43033
    Helixi4305 – 43095
    Turni4321 – 43244
    Beta strandi4325 – 43306
    Helixi4331 – 43333
    Helixi4337 – 43437
    Turni4348 – 43503
    Turni4354 – 43563

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P76model-A3241-3541[»]
    B4225-4231[»]
    1P9Tmodel-A3241-3544[»]
    1PA5model-A3241-3546[»]
    1PUKmodel-A3241-3550[»]
    1Q1Xmodel-A3241-3542[»]
    1Q2WX-ray1.86A/B3241-3544[»]
    1QZ8X-ray2.70A/B4118-4230[»]
    1UJ1X-ray1.90A/B3241-3546[»]
    1UK2X-ray2.20A/B3241-3546[»]
    1UK3X-ray2.40A/B3241-3546[»]
    1UK4X-ray2.50A/B3241-3546[»]
    1UW7X-ray2.80A4118-4230[»]
    1WOFX-ray2.00A/B3241-3546[»]
    1YSYNMR-A3837-3919[»]
    1Z1IX-ray2.80A3241-3546[»]
    1Z1JX-ray2.80A/B3241-3546[»]
    2A5AX-ray2.08A3241-3546[»]
    2A5IX-ray1.88A3241-3546[»]
    2A5KX-ray2.30A/B3241-3546[»]
    2ACFX-ray1.40A/B/C/D1002-1176[»]
    2AHMX-ray2.40A/B/C/D3837-3919[»]
    E/F/G/H3920-4117[»]
    2AJ5model-A3241-3546[»]
    2ALVX-ray1.90A3241-3543[»]
    2AMDX-ray1.85A/B3241-3546[»]
    2AMQX-ray2.30A/B3241-3546[»]
    2BX3X-ray2.00A3241-3546[»]
    2BX4X-ray2.79A3241-3546[»]
    2C3SX-ray1.90A3241-3546[»]
    2D2DX-ray2.70A/B3241-3546[»]
    2DUCX-ray1.70A/B3241-3546[»]
    2FAVX-ray1.80A/B/C1000-1173[»]
    2FE8X-ray1.85A/B/C1541-1854[»]
    2FYGX-ray1.80A4240-4362[»]
    2G9TX-ray2.10A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X4231-4382[»]
    2GA6X-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X4231-4382[»]
    2GDTNMR-A13-127[»]
    2GRINMR-A819-930[»]
    2GT7X-ray1.82A/B3241-3546[»]
    2GT8X-ray2.00A3241-3546[»]
    2GTBX-ray2.00A3241-3546[»]
    2GX4X-ray1.93A3241-3546[»]
    2GZ7X-ray1.86A3241-3546[»]
    2GZ8X-ray1.97A3241-3546[»]
    2GZ9X-ray2.17A3241-3546[»]
    2H2ZX-ray1.60A3241-3546[»]
    2HOBX-ray1.95A3241-3546[»]
    2HSXNMR-A13-127[»]
    2IDYNMR-A819-930[»]
    2KAFNMR-A1473-1538[»]
    2KQVNMR-A1345-1538[»]
    2KQWNMR-A1345-1538[»]
    2KYSNMR-A3837-3919[»]
    2LIZNMR-A3427-3546[»]
    2OP9X-ray1.80A/B3241-3541[»]
    2PWXX-ray2.50A3241-3546[»]
    2W2GX-ray2.22A/B1207-1470[»]
    2WCTX-ray2.79A/B/C/D1207-1470[»]
    2Z3CX-ray1.79A3241-3546[»]
    2Z3DX-ray2.10A3241-3546[»]
    2Z3EX-ray2.32A3241-3546[»]
    2ZU4X-ray1.93A3241-3546[»]
    2ZU5X-ray1.65A3241-3546[»]
    3ATWX-ray2.36A/B3241-3546[»]
    3AVZX-ray2.46A3241-3546[»]
    3AW0X-ray2.30A3241-3546[»]
    3AW1X-ray2.00A/B3241-3546[»]
    3E91X-ray2.55A/B3241-3546[»]
    3EA7X-ray2.65A/B3241-3546[»]
    3EA8X-ray2.25A3241-3546[»]
    3EA9X-ray2.40A3241-3546[»]
    3EAJX-ray2.70A/B3241-3546[»]
    3EE7X-ray2.60A/B/C/D4118-4230[»]
    3F9EX-ray2.50A3241-3546[»]
    3F9FX-ray2.30A/B3241-3546[»]
    3F9GX-ray2.60A/B3241-3541[»]
    3F9HX-ray2.90A/B3241-3546[»]
    3FZDX-ray2.35A3241-3541[»]
    3IWMX-ray3.20A/B/C/D3241-3546[»]
    3M3SX-ray2.30A/B3241-3546[»]
    3M3TX-ray2.90A3241-3546[»]
    3M3VX-ray2.70A/B3241-3546[»]
    3MJ5X-ray2.63A/B1541-1855[»]
    3R24X-ray2.00B4240-4382[»]
    3SN8X-ray1.99A3241-3546[»]
    3SNAX-ray3.05A3241-3541[»]
    3SNBX-ray2.40A3241-3546[»]
    3SNCX-ray2.58A3241-3546[»]
    3SNDX-ray1.89A/B3241-3546[»]
    3SNEX-ray2.60A3241-3546[»]
    3SZNX-ray1.69A3241-3546[»]
    3TITX-ray1.99A3241-3546[»]
    3TIUX-ray2.08A3241-3546[»]
    3TNSX-ray1.99A3241-3546[»]
    3TNTX-ray1.59A3241-3546[»]
    3V3MX-ray1.96A3241-3546[»]
    3VB3X-ray2.20A/B3241-3546[»]
    3VB4X-ray2.20A/B3241-3546[»]
    3VB5X-ray1.95A/B3241-3546[»]
    3VB6X-ray2.50A/B3241-3546[»]
    3VB7X-ray1.95A/B3241-3546[»]
    4HI3X-ray2.09A/B3241-3546[»]
    4M0WX-ray1.40A1541-1858[»]
    4MDSX-ray1.60A3241-3542[»]
    4OVZX-ray2.50A/B1541-1855[»]
    4OW0X-ray2.10A/B1541-1855[»]
    ProteinModelPortaliP0C6U8.
    SMRiP0C6U8. Positions 13-127, 819-930, 1002-1176, 1331-1469, 1541-1854, 3241-3546, 3837-3910, 3921-4111, 4118-4230, 4240-4362.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C6U8.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2092 – 211221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2203 – 222321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2304 – 232421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2326 – 234621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2351 – 237121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2755 – 277521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2830 – 285021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2879 – 289921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2992 – 301221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3022 – 304221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3054 – 307421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3077 – 309721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3105 – 312521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3142 – 316221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3564 – 358421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3586 – 360621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3612 – 363221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3658 – 367821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3707 – 372721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3728 – 374821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3756 – 377621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1003 – 1169167MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1611 – 1875265Peptidase C16PROSITE-ProRule annotationAdd
    BLAST
    Domaini3241 – 3546306Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2092 – 2371280HD1Add
    BLAST
    Regioni2755 – 3162408HD2Add
    BLAST
    Regioni3564 – 3776213HD3Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi930 – 100172Glu-richAdd
    BLAST
    Compositional biasi2210 – 22134Poly-Leu
    Compositional biasi3766 – 37694Poly-Cys

    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 1 peptidase C16 domain.PROSITE-ProRule annotation
    Contains 1 peptidase C30 domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1729 – 176638C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri4304 – 432017Add
    BLAST
    Zinc fingeri4347 – 436014Add
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    InterProiIPR002589. Macro_dom.
    IPR021590. NSP1.
    IPR024375. Nsp3_coronavir.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR024358. SARS-CoV_Nsp3_N.
    IPR022733. SARS_polyprot_cleavage.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view]
    PfamiPF12379. DUF3655. 1 hit.
    PF01661. Macro. 1 hit.
    PF11501. Nsp1. 1 hit.
    PF09401. NSP10. 1 hit.
    PF12124. Nsp3_PL2pro. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF11633. SUD-M. 1 hit.
    PF08715. Viral_protease. 1 hit.
    [Graphical view]
    SUPFAMiSSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 1 hit.
    SSF50494. SSF50494. 1 hit.
    PROSITEiPS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 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 1a (identifier: P0C6U8-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1a, ORF1a polyprotein

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MESLVLGVNE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKNGT     50
    CGLVELEKGV LPQLEQPYVF IKRSDALSTN HGHKVVELVA EMDGIQYGRS 100
    GITLGVLVPH VGETPIAYRN VLLRKNGNKG AGGHSYGIDL KSYDLGDELG 150
    TDPIEDYEQN WNTKHGSGAL RELTRELNGG AVTRYVDNNF CGPDGYPLDC 200
    IKDFLARAGK SMCTLSEQLD YIESKRGVYC CRDHEHEIAW FTERSDKSYE 250
    HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI 300
    RSVYPVASPQ ECNNMHLSTL MKCNHCDEVS WQTCDFLKAT CEHCGTENLV 350
    IEGPTTCGYL PTNAVVKMPC PACQDPEIGP EHSVADYHNH SNIETRLRKG 400
    GRTRCFGGCV FAYVGCYNKR AYWVPRASAD IGSGHTGITG DNVETLNEDL 450
    LEILSRERVN INIVGDFHLN EEVAIILASF SASTSAFIDT IKSLDYKSFK 500
    TIVESCGNYK VTKGKPVKGA WNIGQQRSVL TPLCGFPSQA AGVIRSIFAR 550
    TLDAANHSIP DLQRAAVTIL DGISEQSLRL VDAMVYTSDL LTNSVIIMAY 600
    VTGGLVQQTS QWLSNLLGTT VEKLRPIFEW IEAKLSAGVE FLKDAWEILK 650
    FLITGVFDIV KGQIQVASDN IKDCVKCFID VVNKALEMCI DQVTIAGAKL 700
    RSLNLGEVFI AQSKGLYRQC IRGKEQLQLL MPLKAPKEVT FLEGDSHDTV 750
    LTSEEVVLKN GELEALETPV DSFTNGAIVG TPVCVNGLML LEIKDKEQYC 800
    ALSPGLLATN NVFRLKGGAP IKGVTFGEDT VWEVQGYKNV RITFELDERV 850
    DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE 900
    WSVATFYLFD DAGEENFSSR MYCSFYPPDE EEEDDAECEE EEIDETCEHE 950
    YGTEDDYQGL PLEFGASAET VRVEEEEEED WLDDTTEQSE IEPEPEPTPE 1000
    EPVNQFTGYL KLTDNVAIKC VDIVKEAQSA NPMVIVNAAN IHLKHGGGVA 1050
    GALNKATNGA MQKESDDYIK LNGPLTVGGS CLLSGHNLAK KCLHVVGPNL 1100
    NAGEDIQLLK AAYENFNSQD ILLAPLLSAG IFGAKPLQSL QVCVQTVRTQ 1150
    VYIAVNDKAL YEQVVMDYLD NLKPRVEAPK QEEPPNTEDS KTEEKSVVQK 1200
    PVDVKPKIKA CIDEVTTTLE ETKFLTNKLL LFADINGKLY HDSQNMLRGE 1250
    DMSFLEKDAP YMVGDVITSG DITCVVIPSK KAGGTTEMLS RALKKVPVDE 1300
    YITTYPGQGC AGYTLEEAKT ALKKCKSAFY VLPSEAPNAK EEILGTVSWN 1350
    LREMLAHAEE TRKLMPICMD VRAIMATIQR KYKGIKIQEG IVDYGVRFFF 1400
    YTSKEPVASI ITKLNSLNEP LVTMPIGYVT HGFNLEEAAR CMRSLKAPAV 1450
    VSVSSPDAVT TYNGYLTSSS KTSEEHFVET VSLAGSYRDW SYSGQRTELG 1500
    VEFLKRGDKI VYHTLESPVE FHLDGEVLSL DKLKSLLSLR EVKTIKVFTT 1550
    VDNTNLHTQL VDMSMTYGQQ FGPTYLDGAD VTKIKPHVNH EGKTFFVLPS 1600
    DDTLRSEAFE YYHTLDESFL GRYMSALNHT KKWKFPQVGG LTSIKWADNN 1650
    CYLSSVLLAL QQLEVKFNAP ALQEAYYRAR AGDAANFCAL ILAYSNKTVG 1700
    ELGDVRETMT HLLQHANLES AKRVLNVVCK HCGQKTTTLT GVEAVMYMGT 1750
    LSYDNLKTGV SIPCVCGRDA TQYLVQQESS FVMMSAPPAE YKLQQGTFLC 1800
    ANEYTGNYQC GHYTHITAKE TLYRIDGAHL TKMSEYKGPV TDVFYKETSY 1850
    TTTIKPVSYK LDGVTYTEIE PKLDGYYKKD NAYYTEQPID LVPTQPLPNA 1900
    SFDNFKLTCS NTKFADDLNQ MTGFTKPASR ELSVTFFPDL NGDVVAIDYR 1950
    HYSASFKKGA KLLHKPIVWH INQATTKTTF KPNTWCLRCL WSTKPVDTSN 2000
    SFEVLAVEDT QGMDNLACES QQPTSEEVVE NPTIQKEVIE CDVKTTEVVG 2050
    NVILKPSDEG VKVTQELGHE DLMAAYVENT SITIKKPNEL SLALGLKTIA 2100
    THGIAAINSV PWSKILAYVK PFLGQAAITT SNCAKRLAQR VFNNYMPYVF 2150
    TLLFQLCTFT KSTNSRIRAS LPTTIAKNSV KSVAKLCLDA GINYVKSPKF 2200
    SKLFTIAMWL LLLSICLGSL ICVTAAFGVL LSNFGAPSYC NGVRELYLNS 2250
    SNVTTMDFCE GSFPCSICLS GLDSLDSYPA LETIQVTISS YKLDLTILGL 2300
    AAEWVLAYML FTKFFYLLGL SAIMQVFFGY FASHFISNSW LMWFIISIVQ 2350
    MAPVSAMVRM YIFFASFYYI WKSYVHIMDG CTSSTCMMCY KRNRATRVEC 2400
    TTIVNGMKRS FYVYANGGRG FCKTHNWNCL NCDTFCTGST FISDEVARDL 2450
    SLQFKRPINP TDQSSYIVDS VAVKNGALHL YFDKAGQKTY ERHPLSHFVN 2500
    LDNLRANNTK GSLPINVIVF DGKSKCDESA SKSASVYYSQ LMCQPILLLD 2550
    QALVSDVGDS TEVSVKMFDA YVDTFSATFS VPMEKLKALV ATAHSELAKG 2600
    VALDGVLSTF VSAARQGVVD TDVDTKDVIE CLKLSHHSDL EVTGDSCNNF 2650
    MLTYNKVENM TPRDLGACID CNARHINAQV AKSHNVSLIW NVKDYMSLSE 2700
    QLRKQIRSAA KKNNIPFRLT CATTRQVVNV ITTKISLKGG KIVSTCFKLM 2750
    LKATLLCVLA ALVCYIVMPV HTLSIHDGYT NEIIGYKAIQ DGVTRDIIST 2800
    DDCFANKHAG FDAWFSQRGG SYKNDKSCPV VAAIITREIG FIVPGLPGTV 2850
    LRAINGDFLH FLPRVFSAVG NICYTPSKLI EYSDFATSAC VLAAECTIFK 2900
    DAMGKPVPYC YDTNLLEGSI SYSELRPDTR YVLMDGSIIQ FPNTYLEGSV 2950
    RVVTTFDAEY CRHGTCERSE VGICLSTSGR WVLNNEHYRA LSGVFCGVDA 3000
    MNLIANIFTP LVQPVGALDV SASVVAGGII AILVTCAAYY FMKFRRVFGE 3050
    YNHVVAANAL LFLMSFTILC LVPAYSFLPG VYSVFYLYLT FYFTNDVSFL 3100
    AHLQWFAMFS PIVPFWITAI YVFCISLKHC HWFFNNYLRK RVMFNGVTFS 3150
    TFEEAALCTF LLNKEMYLKL RSETLLPLTQ YNRYLALYNK YKYFSGALDT 3200
    TSYREAACCH LAKALNDFSN SGADVLYQPP QTSITSAVLQ SGFRKMAFPS 3250
    GKVEGCMVQV TCGTTTLNGL WLDDTVYCPR HVICTAEDML NPNYEDLLIR 3300
    KSNHSFLVQA GNVQLRVIGH SMQNCLLRLK VDTSNPKTPK YKFVRIQPGQ 3350
    TFSVLACYNG SPSGVYQCAM RPNHTIKGSF LNGSCGSVGF NIDYDCVSFC 3400
    YMHHMELPTG VHAGTDLEGK FYGPFVDRQT AQAAGTDTTI TLNVLAWLYA 3450
    AVINGDRWFL NRFTTTLNDF NLVAMKYNYE PLTQDHVDIL GPLSAQTGIA 3500
    VLDMCAALKE LLQNGMNGRT ILGSTILEDE FTPFDVVRQC SGVTFQGKFK 3550
    KIVKGTHHWM LLTFLTSLLI LVQSTQWSLF FFVYENAFLP FTLGIMAIAA 3600
    CAMLLVKHKH AFLCLFLLPS LATVAYFNMV YMPASWVMRI MTWLELADTS 3650
    LSGYRLKDCV MYASALVLLI LMTARTVYDD AARRVWTLMN VITLVYKVYY 3700
    GNALDQAISM WALVISVTSN YSGVVTTIMF LARAIVFVCV EYYPLLFITG 3750
    NTLQCIMLVY CFLGYCCCCY FGLFCLLNRY FRLTLGVYDY LVSTQEFRYM 3800
    NSQGLLPPKS SIDAFKLNIK LLGIGGKPCI KVATVQSKMS DVKCTSVVLL 3850
    SVLQQLRVES SSKLWAQCVQ LHNDILLAKD TTEAFEKMVS LLSVLLSMQG 3900
    AVDINRLCEE MLDNRATLQA IASEFSSLPS YAAYATAQEA YEQAVANGDS 3950
    EVVLKKLKKS LNVAKSEFDR DAAMQRKLEK MADQAMTQMY KQARSEDKRA 4000
    KVTSAMQTML FTMLRKLDND ALNNIINNAR DGCVPLNIIP LTTAAKLMVV 4050
    VPDYGTYKNT CDGNTFTYAS ALWEIQQVVD ADSKIVQLSE INMDNSPNLA 4100
    WPLIVTALRA NSAVKLQNNE LSPVALRQMS CAAGTTQTAC TDDNALAYYN 4150
    NSKGGRFVLA LLSDHQDLKW ARFPKSDGTG TIYTELEPPC RFVTDTPKGP 4200
    KVKYLYFIKG LNNLNRGMVL GSLAATVRLQ AGNATEVPAN STVLSFCAFA 4250
    VDPAKAYKDY LASGGQPITN CVKMLCTHTG TGQAITVTPE ANMDQESFGG 4300
    ASCCLYCRCH IDHPNPKGFC DLKGKYVQIP TTCANDPVGF TLRNTVCTVC 4350
    GMWKGYGCSC DQLREPLMQS ADASTFLNGF AV 4382

    Note: Produced by conventional translation.

    Length:4,382
    Mass (Da):486,373
    Last modified:June 10, 2008 - v1
    Checksum:iE1F65D5FD5DFF828
    GO
    Isoform Replicase polyprotein 1ab (identifier: P0C6X7-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry P0C6X7.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

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

    Length:7,073
    Mass (Da):790,248
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti82 – 821G → C in strain: Isolate GD01.
    Natural varianti130 – 1301G → R in strain: Isolate GD01.
    Natural varianti138 – 1381I → T in strain: Isolate SZ16.
    Natural varianti181 – 1811A → V in strain: Isolate Shanghai LY.
    Natural varianti225 – 2251K → Q in strain: Isolate GD01.
    Natural varianti249 – 2491Y → C in strain: Isolate Shanghai LY.
    Natural varianti306 – 3061V → F in strain: Isolate BJ04.
    Natural varianti549 – 5491A → S in strain: Isolate SZ3.
    Natural varianti765 – 7651A → T in strain: Isolate FRA and Isolate Frankfurt-1.
    Natural varianti852 – 8521K → R in strain: Isolate SZ16.
    Natural varianti1004 – 10041N → H in strain: Isolate BJ03.
    Natural varianti1021 – 10211V → A in strain: Isolate SZ3 and Isolate SZ16.
    Natural varianti1023 – 10231I → T in strain: Isolate Shanghai QXC1.
    Natural varianti1121 – 11211I → T in strain: Isolate GD01, Isolate SZ3 and Isolate SZ16.
    Natural varianti1136 – 11361P → L in strain: Isolate SZ3 and Isolate SZ16.
    Natural varianti1257 – 12571K → E in strain: Isolate Shanghai QXC1.
    Natural varianti1319 – 13191K → R in strain: Isolate GD01.
    Natural varianti1329 – 13291F → S in strain: Isolate GD01.
    Natural varianti1361 – 13611T → A in strain: Isolate Shanghai QXC1.
    Natural varianti1385 – 13851I → V in strain: Isolate Shanghai QXC1.
    Natural varianti1538 – 15381S → T in strain: Isolate GD01.
    Natural varianti1563 – 15631M → K in strain: Isolate BJ02.
    Natural varianti1663 – 16631L → I in strain: Isolate SZ3 and Isolate SZ16.
    Natural varianti1762 – 17621I → L in strain: Isolate BJ03.
    Natural varianti1776 – 17772QQ → PP in strain: Isolate BJ03.
    Natural varianti1790 – 17901E → G in strain: Isolate Shanghai QXC1.
    Natural varianti1806 – 18061G → V in strain: Isolate BJ02.
    Natural varianti1962 – 19621L → I in strain: Isolate BJ04.
    Natural varianti2116 – 21161L → F in strain: Isolate GD01, Isolate SZ3 and Isolate SZ16.
    Natural varianti2222 – 22221C → Y in strain: Isolate GD01, Isolate SZ3 and Isolate SZ16.
    Natural varianti2269 – 22691L → S in strain: Isolate SZ3 and Isolate SZ16.
    Natural varianti2326 – 23261V → A in strain: Isolate Shanghai QXC1.
    Natural varianti2392 – 23943RNR → CNH in strain: Isolate Shanghai QXC1.
    Natural varianti2480 – 24801L → P in strain: Isolate Shanghai QXC1.
    Natural varianti2552 – 25521A → V in strain: Isolate Urbani and Isolate Taiwan TC2.
    Natural varianti2556 – 25561D → N in strain: Isolate HKU-39849.
    Natural varianti2564 – 25641S → P in strain: Isolate GD01.
    Natural varianti2648 – 26481N → Y in strain: Isolate Shanghai QXC1.
    Natural varianti2708 – 27081S → T in strain: Isolate HKU-39849.
    Natural varianti2718 – 27181R → T in strain: Isolate HKU-39849.
    Natural varianti2746 – 27461C → W in strain: Isolate SZ3 and Isolate SZ16.
    Natural varianti2770 – 27701V → L in strain: Isolate BJ01 and Isolate BJ02.
    Natural varianti2944 – 29441T → I in strain: Isolate SIN2500, Isolate GD01 and Isolate GZ50.
    Natural varianti2971 – 29711V → A in strain: Isolate GD01 and Isolate SZ16.
    Natural varianti3020 – 30201V → A in strain: Isolate Shanghai QXC1.
    Natural varianti3047 – 30471V → A in strain: Isolate CUHK-W1, Isolate GD01, Isolate SZ3, Isolate SZ16, Isolate BJ01, Isolate BJ02, Isolate BJ03 and Isolate Shanghai QXC1.
    Natural varianti3072 – 30721V → A in strain: Isolate CUHK-W1, Isolate SZ3, Isolate SZ16 and Isolate GD01.
    Natural varianti3197 – 31971A → V in strain: Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04 and Isolate Shanghai QXC1.
    Natural varianti3429 – 34291Q → P in strain: Isolate BJ02.
    Natural varianti3488 – 34881D → E in strain: Isolate BJ04.
    Natural varianti3717 – 37171V → A in strain: Isolate Shanghai QXC1.
    Natural varianti3818 – 38181N → T in strain: Isolate BJ04.
    Natural varianti3903 – 39031D → N in strain: Isolate BJ03.
    Natural varianti3904 – 39041I → F in strain: Isolate BJ02.
    Natural varianti3911 – 39111M → V in strain: Isolate Shanghai QXC1.
    Natural varianti4001 – 40011K → Q in strain: Isolate Shanghai LY.
    Natural varianti4003 – 40031T → A in strain: Isolate Shanghai LY.
    Natural varianti4085 – 40851I → H in strain: Isolate ZJ01.
    Natural varianti4114 – 41141V → A in strain: Isolate Shanghai QXC1.
    Natural varianti4202 – 42021V → M in strain: Isolate Shanghai QXC1.
    Natural varianti4240 – 42401N → H in strain: Isolate ZJ01.
    Natural varianti4296 – 42961E → G in strain: Isolate Shanghai QXC1.
    Natural varianti4377 – 43782LN → FK in strain: Isolate Shanghai QXC1.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY278741 Genomic RNA. Translation: AAP13439.1.
    AY274119 Genomic RNA. No translation available.
    AY278554 Genomic RNA. Translation: AAP13575.1.
    AY282752 Genomic RNA. Translation: AAP30712.1.
    AY304495 Genomic RNA. No translation available.
    AY304486 Genomic RNA. No translation available.
    AY304488 Genomic RNA. No translation available.
    AY278491 Genomic RNA. No translation available.
    AY283794 Genomic RNA. No translation available.
    AY283795 Genomic RNA. No translation available.
    AY283796 Genomic RNA. No translation available.
    AY283797 Genomic RNA. No translation available.
    AY283798 Genomic RNA. No translation available.
    AY286320 Genomic RNA. Translation: AAR16181.1.
    AY278488 Genomic RNA. Translation: AAP30029.1.
    AY278490 Genomic RNA. No translation available.
    AY279354 Genomic RNA. No translation available.
    AY278489 Genomic RNA. Translation: AAP51226.1.
    AY291451 Genomic RNA. Translation: AAP37016.1.
    AY310120 Genomic RNA. Translation: AAP50484.1.
    AY291315 Genomic RNA. Translation: AAP33695.1.
    AY323977 Genomic RNA. Translation: AAP72974.2.
    AY321118 Genomic RNA. No translation available.
    AY338174 Genomic RNA. Translation: AAQ01595.1.
    AY338175 Genomic RNA. Translation: AAQ01607.1.
    AY348314 Genomic RNA. Translation: AAP97880.1.
    AP006557 Genomic RNA. Translation: BAC81347.1.
    AP006558 Genomic RNA. Translation: BAC81361.1.
    AP006559 Genomic RNA. Translation: BAC81375.1.
    AP006560 Genomic RNA. Translation: BAC81389.1.
    AP006561 Genomic RNA. Translation: BAC81403.1.
    AY427439 Genomic RNA. Translation: AAQ94059.1.
    AY322205 Genomic RNA. Translation: AAP82966.1.
    AY322206 Genomic RNA. Translation: AAP82976.1.
    AY463059 Genomic RNA. No translation available.
    RefSeqiNP_828850.1. NC_004718.3. [P0C6U8-1]

    Genome annotation databases

    GeneIDi1489680.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY278741 Genomic RNA. Translation: AAP13439.1 .
    AY274119 Genomic RNA. No translation available.
    AY278554 Genomic RNA. Translation: AAP13575.1 .
    AY282752 Genomic RNA. Translation: AAP30712.1 .
    AY304495 Genomic RNA. No translation available.
    AY304486 Genomic RNA. No translation available.
    AY304488 Genomic RNA. No translation available.
    AY278491 Genomic RNA. No translation available.
    AY283794 Genomic RNA. No translation available.
    AY283795 Genomic RNA. No translation available.
    AY283796 Genomic RNA. No translation available.
    AY283797 Genomic RNA. No translation available.
    AY283798 Genomic RNA. No translation available.
    AY286320 Genomic RNA. Translation: AAR16181.1 .
    AY278488 Genomic RNA. Translation: AAP30029.1 .
    AY278490 Genomic RNA. No translation available.
    AY279354 Genomic RNA. No translation available.
    AY278489 Genomic RNA. Translation: AAP51226.1 .
    AY291451 Genomic RNA. Translation: AAP37016.1 .
    AY310120 Genomic RNA. Translation: AAP50484.1 .
    AY291315 Genomic RNA. Translation: AAP33695.1 .
    AY323977 Genomic RNA. Translation: AAP72974.2 .
    AY321118 Genomic RNA. No translation available.
    AY338174 Genomic RNA. Translation: AAQ01595.1 .
    AY338175 Genomic RNA. Translation: AAQ01607.1 .
    AY348314 Genomic RNA. Translation: AAP97880.1 .
    AP006557 Genomic RNA. Translation: BAC81347.1 .
    AP006558 Genomic RNA. Translation: BAC81361.1 .
    AP006559 Genomic RNA. Translation: BAC81375.1 .
    AP006560 Genomic RNA. Translation: BAC81389.1 .
    AP006561 Genomic RNA. Translation: BAC81403.1 .
    AY427439 Genomic RNA. Translation: AAQ94059.1 .
    AY322205 Genomic RNA. Translation: AAP82966.1 .
    AY322206 Genomic RNA. Translation: AAP82976.1 .
    AY463059 Genomic RNA. No translation available.
    RefSeqi NP_828850.1. NC_004718.3. [P0C6U8-1 ]

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P76 model - A 3241-3541 [» ]
    B 4225-4231 [» ]
    1P9T model - A 3241-3544 [» ]
    1PA5 model - A 3241-3546 [» ]
    1PUK model - A 3241-3550 [» ]
    1Q1X model - A 3241-3542 [» ]
    1Q2W X-ray 1.86 A/B 3241-3544 [» ]
    1QZ8 X-ray 2.70 A/B 4118-4230 [» ]
    1UJ1 X-ray 1.90 A/B 3241-3546 [» ]
    1UK2 X-ray 2.20 A/B 3241-3546 [» ]
    1UK3 X-ray 2.40 A/B 3241-3546 [» ]
    1UK4 X-ray 2.50 A/B 3241-3546 [» ]
    1UW7 X-ray 2.80 A 4118-4230 [» ]
    1WOF X-ray 2.00 A/B 3241-3546 [» ]
    1YSY NMR - A 3837-3919 [» ]
    1Z1I X-ray 2.80 A 3241-3546 [» ]
    1Z1J X-ray 2.80 A/B 3241-3546 [» ]
    2A5A X-ray 2.08 A 3241-3546 [» ]
    2A5I X-ray 1.88 A 3241-3546 [» ]
    2A5K X-ray 2.30 A/B 3241-3546 [» ]
    2ACF X-ray 1.40 A/B/C/D 1002-1176 [» ]
    2AHM X-ray 2.40 A/B/C/D 3837-3919 [» ]
    E/F/G/H 3920-4117 [» ]
    2AJ5 model - A 3241-3546 [» ]
    2ALV X-ray 1.90 A 3241-3543 [» ]
    2AMD X-ray 1.85 A/B 3241-3546 [» ]
    2AMQ X-ray 2.30 A/B 3241-3546 [» ]
    2BX3 X-ray 2.00 A 3241-3546 [» ]
    2BX4 X-ray 2.79 A 3241-3546 [» ]
    2C3S X-ray 1.90 A 3241-3546 [» ]
    2D2D X-ray 2.70 A/B 3241-3546 [» ]
    2DUC X-ray 1.70 A/B 3241-3546 [» ]
    2FAV X-ray 1.80 A/B/C 1000-1173 [» ]
    2FE8 X-ray 1.85 A/B/C 1541-1854 [» ]
    2FYG X-ray 1.80 A 4240-4362 [» ]
    2G9T X-ray 2.10 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 4231-4382 [» ]
    2GA6 X-ray 2.70 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 4231-4382 [» ]
    2GDT NMR - A 13-127 [» ]
    2GRI NMR - A 819-930 [» ]
    2GT7 X-ray 1.82 A/B 3241-3546 [» ]
    2GT8 X-ray 2.00 A 3241-3546 [» ]
    2GTB X-ray 2.00 A 3241-3546 [» ]
    2GX4 X-ray 1.93 A 3241-3546 [» ]
    2GZ7 X-ray 1.86 A 3241-3546 [» ]
    2GZ8 X-ray 1.97 A 3241-3546 [» ]
    2GZ9 X-ray 2.17 A 3241-3546 [» ]
    2H2Z X-ray 1.60 A 3241-3546 [» ]
    2HOB X-ray 1.95 A 3241-3546 [» ]
    2HSX NMR - A 13-127 [» ]
    2IDY NMR - A 819-930 [» ]
    2KAF NMR - A 1473-1538 [» ]
    2KQV NMR - A 1345-1538 [» ]
    2KQW NMR - A 1345-1538 [» ]
    2KYS NMR - A 3837-3919 [» ]
    2LIZ NMR - A 3427-3546 [» ]
    2OP9 X-ray 1.80 A/B 3241-3541 [» ]
    2PWX X-ray 2.50 A 3241-3546 [» ]
    2W2G X-ray 2.22 A/B 1207-1470 [» ]
    2WCT X-ray 2.79 A/B/C/D 1207-1470 [» ]
    2Z3C X-ray 1.79 A 3241-3546 [» ]
    2Z3D X-ray 2.10 A 3241-3546 [» ]
    2Z3E X-ray 2.32 A 3241-3546 [» ]
    2ZU4 X-ray 1.93 A 3241-3546 [» ]
    2ZU5 X-ray 1.65 A 3241-3546 [» ]
    3ATW X-ray 2.36 A/B 3241-3546 [» ]
    3AVZ X-ray 2.46 A 3241-3546 [» ]
    3AW0 X-ray 2.30 A 3241-3546 [» ]
    3AW1 X-ray 2.00 A/B 3241-3546 [» ]
    3E91 X-ray 2.55 A/B 3241-3546 [» ]
    3EA7 X-ray 2.65 A/B 3241-3546 [» ]
    3EA8 X-ray 2.25 A 3241-3546 [» ]
    3EA9 X-ray 2.40 A 3241-3546 [» ]
    3EAJ X-ray 2.70 A/B 3241-3546 [» ]
    3EE7 X-ray 2.60 A/B/C/D 4118-4230 [» ]
    3F9E X-ray 2.50 A 3241-3546 [» ]
    3F9F X-ray 2.30 A/B 3241-3546 [» ]
    3F9G X-ray 2.60 A/B 3241-3541 [» ]
    3F9H X-ray 2.90 A/B 3241-3546 [» ]
    3FZD X-ray 2.35 A 3241-3541 [» ]
    3IWM X-ray 3.20 A/B/C/D 3241-3546 [» ]
    3M3S X-ray 2.30 A/B 3241-3546 [» ]
    3M3T X-ray 2.90 A 3241-3546 [» ]
    3M3V X-ray 2.70 A/B 3241-3546 [» ]
    3MJ5 X-ray 2.63 A/B 1541-1855 [» ]
    3R24 X-ray 2.00 B 4240-4382 [» ]
    3SN8 X-ray 1.99 A 3241-3546 [» ]
    3SNA X-ray 3.05 A 3241-3541 [» ]
    3SNB X-ray 2.40 A 3241-3546 [» ]
    3SNC X-ray 2.58 A 3241-3546 [» ]
    3SND X-ray 1.89 A/B 3241-3546 [» ]
    3SNE X-ray 2.60 A 3241-3546 [» ]
    3SZN X-ray 1.69 A 3241-3546 [» ]
    3TIT X-ray 1.99 A 3241-3546 [» ]
    3TIU X-ray 2.08 A 3241-3546 [» ]
    3TNS X-ray 1.99 A 3241-3546 [» ]
    3TNT X-ray 1.59 A 3241-3546 [» ]
    3V3M X-ray 1.96 A 3241-3546 [» ]
    3VB3 X-ray 2.20 A/B 3241-3546 [» ]
    3VB4 X-ray 2.20 A/B 3241-3546 [» ]
    3VB5 X-ray 1.95 A/B 3241-3546 [» ]
    3VB6 X-ray 2.50 A/B 3241-3546 [» ]
    3VB7 X-ray 1.95 A/B 3241-3546 [» ]
    4HI3 X-ray 2.09 A/B 3241-3546 [» ]
    4M0W X-ray 1.40 A 1541-1858 [» ]
    4MDS X-ray 1.60 A 3241-3542 [» ]
    4OVZ X-ray 2.50 A/B 1541-1855 [» ]
    4OW0 X-ray 2.10 A/B 1541-1855 [» ]
    ProteinModelPortali P0C6U8.
    SMRi P0C6U8. Positions 13-127, 819-930, 1002-1176, 1331-1469, 1541-1854, 3241-3546, 3837-3910, 3921-4111, 4118-4230, 4240-4362.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48580N.

    Chemistry

    BindingDBi P0C6U8.
    ChEMBLi CHEMBL3927.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1489680.

    Miscellaneous databases

    EvolutionaryTracei P0C6U8.

    Family and domain databases

    InterProi IPR002589. Macro_dom.
    IPR021590. NSP1.
    IPR024375. Nsp3_coronavir.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR024358. SARS-CoV_Nsp3_N.
    IPR022733. SARS_polyprot_cleavage.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view ]
    Pfami PF12379. DUF3655. 1 hit.
    PF01661. Macro. 1 hit.
    PF11501. Nsp1. 1 hit.
    PF09401. NSP10. 1 hit.
    PF12124. Nsp3_PL2pro. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF11633. SUD-M. 1 hit.
    PF08715. Viral_protease. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 1 hit.
    SSF50494. SSF50494. 1 hit.
    PROSITEi PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Urbani.
    2. "The genome sequence of the SARS-associated coronavirus."
      Marra M.A., Jones S.J.M., Astell C.R., Holt R.A., Brooks-Wilson A., Butterfield Y.S.N., Khattra J., Asano J.K., Barber S.A., Chan S.Y., Cloutier A., Coughlin S.M., Freeman D., Girn N., Griffith O.L., Leach S.R., Mayo M., McDonald H.
      , Montgomery S.B., Pandoh P.K., Petrescu A.S., Robertson A.G., Schein J.E., Siddiqui A., Smailus D.E., Stott J.M., Yang G.S., Plummer F., Andonov A., Artsob H., Bastien N., Bernard K., Booth T.F., Bowness D., Czub M., Drebot M., Fernando L., Flick R., Garbutt M., Gray M., Grolla A., Jones S., Feldmann H., Meyers A., Kabani A., Li Y., Normand S., Stroher U., Tipples G.A., Tyler S., Vogrig R., Ward D., Watson B., Brunham R.C., Krajden M., Petric M., Skowronski D.M., Upton C., Roper R.L.
      Science 300:1399-1404(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Tor2.
    3. "Coronavirus genomic-sequence variations and the epidemiology of the severe acute respiratory syndrome."
      Tsui S.K.W., Chim S.S.C., Lo Y.M.D.
      N. Engl. J. Med. 349:187-188(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate CUHK-Su10 and Isolate CUHK-W1.
    4. "Isolation and characterization of viruses related to the SARS coronavirus from animals in southern China."
      Guan Y., Zheng B.J., He Y.Q., Liu X.L., Zhuang Z.X., Cheung C.L., Luo S.W., Li P.H., Zhang L.J., Guan Y.J., Butt K.M., Wong K.L., Chan K.W., Lim W., Shortridge K.F., Yuen K.Y., Peiris J.S.M., Poon L.L.M.
      Science 302:276-278(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate GZ50, Isolate SZ16 and Isolate SZ3.
    5. "The complete genome sequence of severe acute respiratory syndrome coronavirus strain HKU-39849 (HK-39)."
      Zeng F.Y., Chan C.W., Chan M.N., Chen J.D., Chow K.Y.C., Hon C.C.C., Hui R.K.H., Li J., Li V.Y.Y., Wang C.Y., Wang P.Y., Guan Y., Zheng B., Poon L.L.M., Chan K.H., Yuen K.Y., Peiris J.S.M., Leung F.C.
      Exp. Biol. Med. 228:866-873(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate HKU-39849.
    6. "Comparative full-length genome sequence analysis of 14 SARS coronavirus isolates and common mutations associated with putative origins of infection."
      Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y., Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L., Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M., Liu E.T.
      Lancet 361:1779-1785(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Sin2500, Isolate Sin2677, Isolate Sin2679, Isolate Sin2748 and Isolate sin2774.
    7. "Severe acute respiratory syndrome-associated coronavirus genotype and its characterization."
      Li L., Wang Z., Lu Y., Bao Q., Chen S., Wu N., Cheng S., Weng J., Zhang Y., Yan J., Mei L., Wang X., Zhu H., Yu Y., Zhang M., Li M., Yao J., Lu Q.
      , Yao P., Bo X., Wo J., Wang S., Hu S.
      Chin. Med. J. 116:1288-1292(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate ZJ01.
    8. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04 and Isolate GD01.
    9. "The complete genome of SARS coronavirus clone TW1."
      Yeh S.-H., Kao C.-L., Tsai C.-Y., Liu C.-J., Chen D.-S., Chen P.-J.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate TW1.
    10. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate FRA.
    11. Thiel V., Hertzig T., Putics A., Ivanov K.A., Schelle B., Bayer S., Scheiner B., Weinand H., Weissbrich B., Ziebuhr J.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Frankfurt-1.
    12. "Genomic sequence of SARS isolate from the first fatal case in Taiwan."
      Yang J.-Y., Lin J.-H., Chiu S.-C., Wang S.-F., Lee S.C., Lin Y.-C., Hsu C.-K., Chen H.-Y., Chang J.G., Chen P.-J., Su I.-J.
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate TWC.
    13. "Analysis of SARS coronavirus genome in Shanghai isolates."
      Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Shanghai QXC1.
    14. Canducci F., Clementi M., Poli G., Vicenzi E.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate HSR 1.
    15. Chang J.-G.C., Lin T.-H., Chen C.-M., Lin C.-S., Chan W.-L., Shih M.-C.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Taiwan TC1, Isolate Taiwan TC2 and Isolate Taiwan TC3.
    16. Shu H.Y., Wu K.M., Tsai S.F.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate TWH, Isolate TWJ, Isolate TWK, Isolate TWS and Isolate TWY.
    17. Balotta C., Corvasce S., Violin M., Galli M., Moroni M., Vigevani G.M., Ruan Y.J., Salemi M.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate AS.
    18. Wang Z., Cheng S., Zhang Y.
      Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate ZJ01.
    19. Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-507 AND 1655-4382.
      Strain: Isolate Shanghai LY.
    20. Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    21. "Identification and characterization of severe acute respiratory syndrome coronavirus replicase proteins."
      Prentice E., McAuliffe J., Lu X., Subbarao K., Denison M.R.
      J. Virol. 78:9977-9986(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
    22. "Identification of severe acute respiratory syndrome coronavirus replicase products and characterization of papain-like protease activity."
      Harcourt B.H., Jukneliene D., Kanjanahaluethai A., Bechill J., Severson K.M., Smith C.M., Rota P.A., Baker S.C.
      J. Virol. 78:13600-13612(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
      Strain: Isolate Urbani.
    23. Cited for: FUNCTION OF NSP8.
    24. "Selectivity in ISG15 and ubiquitin recognition by the SARS coronavirus papain-like protease."
      Lindner H.A., Lytvyn V., Qi H., Lachance P., Ziomek E., Menard R.
      Arch. Biochem. Biophys. 466:8-14(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF NSP3.
    25. "Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-kappaB signaling."
      Frieman M., Ratia K., Johnston R.E., Mesecar A.D., Baric R.S.
      J. Virol. 83:6689-6705(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF NSP3.
    26. "SARS coronavirus nsp1 protein induces template-dependent endonucleolytic cleavage of mRNAs: viral mRNAs are resistant to nsp1-induced RNA cleavage."
      Huang C., Lokugamage K.G., Rozovics J.M., Narayanan K., Semler B.L., Makino S.
      PLoS Pathog. 7:E1002433-E1002433(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF NSP1.
    27. "Severe acute respiratory syndrome coronavirus protein nsp1 is a novel eukaryotic translation inhibitor that represses multiple steps of translation initiation."
      Lokugamage K.G., Narayanan K., Huang C., Makino S.
      J. Virol. 86:13598-13608(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF NSP1.
    28. "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: 3D-STRUCTURE MODELING OF 3241-3540, CHARACTERIZATION.
    29. "Structural genomics of the SARS coronavirus: cloning, expression, crystallization and preliminary crystallographic study of the Nsp9 protein."
      Campanacci V., Egloff M.-P., Longhi S., Ferron F., Rancurel C., Salomoni A., Durousseau C., Tocque F., Bremond N., Dobbe J.C., Snijder E.J., Canard B., Cambillau C.
      Acta Crystallogr. D 59:1628-1631(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4118-4230 (NSP9).
      Strain: Isolate Frankfurt-1.
    30. "The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world."
      Egloff M.-P., Ferron F., Campanacci V., Longhi S., Rancurel C., Dutartre H., Snijder E.J., Gorbalenya A.E., Cambillau C., Canard B.
      Proc. Natl. Acad. Sci. U.S.A. 101:3792-3796(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 4118-4230.
    31. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4107-4230.
    32. "Insights into SARS-CoV transcription and replication from the structure of the nsp7-nsp8 hexadecamer."
      Zhai Y., Sun F., Li X., Pang H., Xu X., Bartlam M., Rao Z.
      Nat. Struct. Mol. Biol. 12:980-986(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 3837-4117 AND 3920-4117, INTERACTION OF NSP7 WITH NSP8.
    33. "Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3."
      Saikatendu K.S., Joseph J.S., Subramanian V., Clayton T., Griffith M., Moy K., Velasquez J., Neuman B.W., Buchmeier M.J., Stevens R.C., Kuhn P.
      Structure 13:1665-1675(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1002-1176.
    34. "Severe acute respiratory syndrome coronavirus papain-like protease: structure of a viral deubiquitinating enzyme."
      Ratia K., Saikatendu K.S., Santarsiero B.D., Barretto N., Baker S.C., Stevens R.C., Mesecar A.D.
      Proc. Natl. Acad. Sci. U.S.A. 103:5717-5722(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1541-1854.
    35. "Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs."
      Joseph J.S., Saikatendu K.S., Subramanian V., Neuman B.W., Brooun A., Griffith M., Moy K., Yadav M.K., Velasquez J., Buchmeier M.J., Stevens R.C., Kuhn P.
      J. Virol. 80:7894-7901(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4240-4362.
      Strain: Isolate Tor2.
    36. "Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10."
      Su D., Lou Z., Sun F., Zhai Y., Yang H., Zhang R., Joachimiak A., Zhang X.C., Bartlam M., Rao Z.
      J. Virol. 80:7902-7908(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 4231-4378.
    37. "Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus."
      Almeida M.S., Johnson M.A., Herrmann T., Geralt M., Wuthrich K.
      J. Virol. 81:3151-3161(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 13-127.
    38. "Crystal structure of Sars coronavirus main proteinase(3CLPRO)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3241-3546.

    Entry informationi

    Entry nameiR1A_CVHSA
    AccessioniPrimary (citable) accession number: P0C6U8
    Secondary accession number(s): P59641
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 65 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3