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P0C6U8

- R1A_CVHSA

UniProt

P0C6U8 - R1A_CVHSA

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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

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
Complete GO annotation...

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

Protein family/group databases

MEROPSiC16.009.

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

Topology

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

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
  2. host cell membrane Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4MM3X-ray2.75B1541-1855[»]
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.

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

        10         20         30         40         50
MESLVLGVNE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKNGT
60 70 80 90 100
CGLVELEKGV LPQLEQPYVF IKRSDALSTN HGHKVVELVA EMDGIQYGRS
110 120 130 140 150
GITLGVLVPH VGETPIAYRN VLLRKNGNKG AGGHSYGIDL KSYDLGDELG
160 170 180 190 200
TDPIEDYEQN WNTKHGSGAL RELTRELNGG AVTRYVDNNF CGPDGYPLDC
210 220 230 240 250
IKDFLARAGK SMCTLSEQLD YIESKRGVYC CRDHEHEIAW FTERSDKSYE
260 270 280 290 300
HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI
310 320 330 340 350
RSVYPVASPQ ECNNMHLSTL MKCNHCDEVS WQTCDFLKAT CEHCGTENLV
360 370 380 390 400
IEGPTTCGYL PTNAVVKMPC PACQDPEIGP EHSVADYHNH SNIETRLRKG
410 420 430 440 450
GRTRCFGGCV FAYVGCYNKR AYWVPRASAD IGSGHTGITG DNVETLNEDL
460 470 480 490 500
LEILSRERVN INIVGDFHLN EEVAIILASF SASTSAFIDT IKSLDYKSFK
510 520 530 540 550
TIVESCGNYK VTKGKPVKGA WNIGQQRSVL TPLCGFPSQA AGVIRSIFAR
560 570 580 590 600
TLDAANHSIP DLQRAAVTIL DGISEQSLRL VDAMVYTSDL LTNSVIIMAY
610 620 630 640 650
VTGGLVQQTS QWLSNLLGTT VEKLRPIFEW IEAKLSAGVE FLKDAWEILK
660 670 680 690 700
FLITGVFDIV KGQIQVASDN IKDCVKCFID VVNKALEMCI DQVTIAGAKL
710 720 730 740 750
RSLNLGEVFI AQSKGLYRQC IRGKEQLQLL MPLKAPKEVT FLEGDSHDTV
760 770 780 790 800
LTSEEVVLKN GELEALETPV DSFTNGAIVG TPVCVNGLML LEIKDKEQYC
810 820 830 840 850
ALSPGLLATN NVFRLKGGAP IKGVTFGEDT VWEVQGYKNV RITFELDERV
860 870 880 890 900
DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE
910 920 930 940 950
WSVATFYLFD DAGEENFSSR MYCSFYPPDE EEEDDAECEE EEIDETCEHE
960 970 980 990 1000
YGTEDDYQGL PLEFGASAET VRVEEEEEED WLDDTTEQSE IEPEPEPTPE
1010 1020 1030 1040 1050
EPVNQFTGYL KLTDNVAIKC VDIVKEAQSA NPMVIVNAAN IHLKHGGGVA
1060 1070 1080 1090 1100
GALNKATNGA MQKESDDYIK LNGPLTVGGS CLLSGHNLAK KCLHVVGPNL
1110 1120 1130 1140 1150
NAGEDIQLLK AAYENFNSQD ILLAPLLSAG IFGAKPLQSL QVCVQTVRTQ
1160 1170 1180 1190 1200
VYIAVNDKAL YEQVVMDYLD NLKPRVEAPK QEEPPNTEDS KTEEKSVVQK
1210 1220 1230 1240 1250
PVDVKPKIKA CIDEVTTTLE ETKFLTNKLL LFADINGKLY HDSQNMLRGE
1260 1270 1280 1290 1300
DMSFLEKDAP YMVGDVITSG DITCVVIPSK KAGGTTEMLS RALKKVPVDE
1310 1320 1330 1340 1350
YITTYPGQGC AGYTLEEAKT ALKKCKSAFY VLPSEAPNAK EEILGTVSWN
1360 1370 1380 1390 1400
LREMLAHAEE TRKLMPICMD VRAIMATIQR KYKGIKIQEG IVDYGVRFFF
1410 1420 1430 1440 1450
YTSKEPVASI ITKLNSLNEP LVTMPIGYVT HGFNLEEAAR CMRSLKAPAV
1460 1470 1480 1490 1500
VSVSSPDAVT TYNGYLTSSS KTSEEHFVET VSLAGSYRDW SYSGQRTELG
1510 1520 1530 1540 1550
VEFLKRGDKI VYHTLESPVE FHLDGEVLSL DKLKSLLSLR EVKTIKVFTT
1560 1570 1580 1590 1600
VDNTNLHTQL VDMSMTYGQQ FGPTYLDGAD VTKIKPHVNH EGKTFFVLPS
1610 1620 1630 1640 1650
DDTLRSEAFE YYHTLDESFL GRYMSALNHT KKWKFPQVGG LTSIKWADNN
1660 1670 1680 1690 1700
CYLSSVLLAL QQLEVKFNAP ALQEAYYRAR AGDAANFCAL ILAYSNKTVG
1710 1720 1730 1740 1750
ELGDVRETMT HLLQHANLES AKRVLNVVCK HCGQKTTTLT GVEAVMYMGT
1760 1770 1780 1790 1800
LSYDNLKTGV SIPCVCGRDA TQYLVQQESS FVMMSAPPAE YKLQQGTFLC
1810 1820 1830 1840 1850
ANEYTGNYQC GHYTHITAKE TLYRIDGAHL TKMSEYKGPV TDVFYKETSY
1860 1870 1880 1890 1900
TTTIKPVSYK LDGVTYTEIE PKLDGYYKKD NAYYTEQPID LVPTQPLPNA
1910 1920 1930 1940 1950
SFDNFKLTCS NTKFADDLNQ MTGFTKPASR ELSVTFFPDL NGDVVAIDYR
1960 1970 1980 1990 2000
HYSASFKKGA KLLHKPIVWH INQATTKTTF KPNTWCLRCL WSTKPVDTSN
2010 2020 2030 2040 2050
SFEVLAVEDT QGMDNLACES QQPTSEEVVE NPTIQKEVIE CDVKTTEVVG
2060 2070 2080 2090 2100
NVILKPSDEG VKVTQELGHE DLMAAYVENT SITIKKPNEL SLALGLKTIA
2110 2120 2130 2140 2150
THGIAAINSV PWSKILAYVK PFLGQAAITT SNCAKRLAQR VFNNYMPYVF
2160 2170 2180 2190 2200
TLLFQLCTFT KSTNSRIRAS LPTTIAKNSV KSVAKLCLDA GINYVKSPKF
2210 2220 2230 2240 2250
SKLFTIAMWL LLLSICLGSL ICVTAAFGVL LSNFGAPSYC NGVRELYLNS
2260 2270 2280 2290 2300
SNVTTMDFCE GSFPCSICLS GLDSLDSYPA LETIQVTISS YKLDLTILGL
2310 2320 2330 2340 2350
AAEWVLAYML FTKFFYLLGL SAIMQVFFGY FASHFISNSW LMWFIISIVQ
2360 2370 2380 2390 2400
MAPVSAMVRM YIFFASFYYI WKSYVHIMDG CTSSTCMMCY KRNRATRVEC
2410 2420 2430 2440 2450
TTIVNGMKRS FYVYANGGRG FCKTHNWNCL NCDTFCTGST FISDEVARDL
2460 2470 2480 2490 2500
SLQFKRPINP TDQSSYIVDS VAVKNGALHL YFDKAGQKTY ERHPLSHFVN
2510 2520 2530 2540 2550
LDNLRANNTK GSLPINVIVF DGKSKCDESA SKSASVYYSQ LMCQPILLLD
2560 2570 2580 2590 2600
QALVSDVGDS TEVSVKMFDA YVDTFSATFS VPMEKLKALV ATAHSELAKG
2610 2620 2630 2640 2650
VALDGVLSTF VSAARQGVVD TDVDTKDVIE CLKLSHHSDL EVTGDSCNNF
2660 2670 2680 2690 2700
MLTYNKVENM TPRDLGACID CNARHINAQV AKSHNVSLIW NVKDYMSLSE
2710 2720 2730 2740 2750
QLRKQIRSAA KKNNIPFRLT CATTRQVVNV ITTKISLKGG KIVSTCFKLM
2760 2770 2780 2790 2800
LKATLLCVLA ALVCYIVMPV HTLSIHDGYT NEIIGYKAIQ DGVTRDIIST
2810 2820 2830 2840 2850
DDCFANKHAG FDAWFSQRGG SYKNDKSCPV VAAIITREIG FIVPGLPGTV
2860 2870 2880 2890 2900
LRAINGDFLH FLPRVFSAVG NICYTPSKLI EYSDFATSAC VLAAECTIFK
2910 2920 2930 2940 2950
DAMGKPVPYC YDTNLLEGSI SYSELRPDTR YVLMDGSIIQ FPNTYLEGSV
2960 2970 2980 2990 3000
RVVTTFDAEY CRHGTCERSE VGICLSTSGR WVLNNEHYRA LSGVFCGVDA
3010 3020 3030 3040 3050
MNLIANIFTP LVQPVGALDV SASVVAGGII AILVTCAAYY FMKFRRVFGE
3060 3070 3080 3090 3100
YNHVVAANAL LFLMSFTILC LVPAYSFLPG VYSVFYLYLT FYFTNDVSFL
3110 3120 3130 3140 3150
AHLQWFAMFS PIVPFWITAI YVFCISLKHC HWFFNNYLRK RVMFNGVTFS
3160 3170 3180 3190 3200
TFEEAALCTF LLNKEMYLKL RSETLLPLTQ YNRYLALYNK YKYFSGALDT
3210 3220 3230 3240 3250
TSYREAACCH LAKALNDFSN SGADVLYQPP QTSITSAVLQ SGFRKMAFPS
3260 3270 3280 3290 3300
GKVEGCMVQV TCGTTTLNGL WLDDTVYCPR HVICTAEDML NPNYEDLLIR
3310 3320 3330 3340 3350
KSNHSFLVQA GNVQLRVIGH SMQNCLLRLK VDTSNPKTPK YKFVRIQPGQ
3360 3370 3380 3390 3400
TFSVLACYNG SPSGVYQCAM RPNHTIKGSF LNGSCGSVGF NIDYDCVSFC
3410 3420 3430 3440 3450
YMHHMELPTG VHAGTDLEGK FYGPFVDRQT AQAAGTDTTI TLNVLAWLYA
3460 3470 3480 3490 3500
AVINGDRWFL NRFTTTLNDF NLVAMKYNYE PLTQDHVDIL GPLSAQTGIA
3510 3520 3530 3540 3550
VLDMCAALKE LLQNGMNGRT ILGSTILEDE FTPFDVVRQC SGVTFQGKFK
3560 3570 3580 3590 3600
KIVKGTHHWM LLTFLTSLLI LVQSTQWSLF FFVYENAFLP FTLGIMAIAA
3610 3620 3630 3640 3650
CAMLLVKHKH AFLCLFLLPS LATVAYFNMV YMPASWVMRI MTWLELADTS
3660 3670 3680 3690 3700
LSGYRLKDCV MYASALVLLI LMTARTVYDD AARRVWTLMN VITLVYKVYY
3710 3720 3730 3740 3750
GNALDQAISM WALVISVTSN YSGVVTTIMF LARAIVFVCV EYYPLLFITG
3760 3770 3780 3790 3800
NTLQCIMLVY CFLGYCCCCY FGLFCLLNRY FRLTLGVYDY LVSTQEFRYM
3810 3820 3830 3840 3850
NSQGLLPPKS SIDAFKLNIK LLGIGGKPCI KVATVQSKMS DVKCTSVVLL
3860 3870 3880 3890 3900
SVLQQLRVES SSKLWAQCVQ LHNDILLAKD TTEAFEKMVS LLSVLLSMQG
3910 3920 3930 3940 3950
AVDINRLCEE MLDNRATLQA IASEFSSLPS YAAYATAQEA YEQAVANGDS
3960 3970 3980 3990 4000
EVVLKKLKKS LNVAKSEFDR DAAMQRKLEK MADQAMTQMY KQARSEDKRA
4010 4020 4030 4040 4050
KVTSAMQTML FTMLRKLDND ALNNIINNAR DGCVPLNIIP LTTAAKLMVV
4060 4070 4080 4090 4100
VPDYGTYKNT CDGNTFTYAS ALWEIQQVVD ADSKIVQLSE INMDNSPNLA
4110 4120 4130 4140 4150
WPLIVTALRA NSAVKLQNNE LSPVALRQMS CAAGTTQTAC TDDNALAYYN
4160 4170 4180 4190 4200
NSKGGRFVLA LLSDHQDLKW ARFPKSDGTG TIYTELEPPC RFVTDTPKGP
4210 4220 4230 4240 4250
KVKYLYFIKG LNNLNRGMVL GSLAATVRLQ AGNATEVPAN STVLSFCAFA
4260 4270 4280 4290 4300
VDPAKAYKDY LASGGQPITN CVKMLCTHTG TGQAITVTPE ANMDQESFGG
4310 4320 4330 4340 4350
ASCCLYCRCH IDHPNPKGFC DLKGKYVQIP TTCANDPVGF TLRNTVCTVC
4360 4370 4380
GMWKGYGCSC DQLREPLMQS ADASTFLNGF AV

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
4MM3 X-ray 2.75 B 1541-1855 [» ]
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.

Protein family/group databases

MEROPSi C16.009.

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: November 26, 2014
This is version 67 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