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P0C6X7

- R1AB_CVHSA

UniProt

P0C6X7 - R1AB_CVHSA

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Protein
Replicase polyprotein 1ab
Gene
rep, 1a-1b
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 replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products By similarity.5 Publications
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-3.5 Publications
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.5 Publications
The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Its ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G). Activity of helicase is dependent on magnesium.5 Publications
The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction.5 Publications
Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter.5 Publications
Nsp9 is a ssRNA-binding protein.5 Publications
NendoU is a Mn2+-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.5 Publications
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.5 Publications

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).1 Publication
ATP + H2O = ADP + phosphate.1 Publication
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.1 Publication
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).1 Publication

Kineticsi

The kinetic parameters are studied for the 3C-like proteinase domain. The cleavage takes place at the /.

  1. KM=1.15 mM for peptide TSAVLQ/SGFRK-NH21 Publication
  2. KM=0.58 mM for peptide SGVTFQ/GKFKK
  3. KM=1.44 mM for peptide ATVRLQ/AGNAT

pH dependencei

Optimum pH is 7.0 for 3C-like proteinase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei180 – 1812Cleavage By similarity
Sitei818 – 8192Cleavage; by PL-PRO By similarity
Active sitei1651 – 16511For PL-PRO activity By similarity
Active sitei1812 – 18121For PL-PRO activity By similarity
Sitei2740 – 27412Cleavage; by PL-PRO By similarity
Sitei3240 – 32412Cleavage; by 3CL-PRO By similarity
Active sitei3281 – 32811For 3CL-PRO activity By similarity
Active sitei3385 – 33851For 3CL-PRO activity By similarity
Sitei3546 – 35472Cleavage; by 3CL-PRO By similarity
Sitei3836 – 38372Cleavage; by 3CL-PRO By similarity
Sitei3919 – 39202Cleavage; by 3CL-PRO By similarity
Sitei4117 – 41182Cleavage; by 3CL-PRO By similarity
Sitei4230 – 42312Cleavage; by 3CL-PRO By 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-PRO By similarity
Sitei5301 – 53022Cleavage; by 3CL-PRO By similarity
Sitei5902 – 59032Cleavage; by 3CL-PRO By similarity
Sitei6429 – 64302Cleavage; by 3CL-PRO By similarity
Sitei6775 – 67762Cleavage; by 3CL-PRO By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1729 – 176638C4-type
Add
BLAST
Zinc fingeri4304 – 432017
Add
BLAST
Zinc fingeri4347 – 436014
Add
BLAST
Nucleotide bindingi5583 – 55908ATP By similarity

GO - Molecular functioni

  1. 3'-5'-exoribonuclease activity Source: CACAO
  2. ATP binding Source: UniProtKB-KW
  3. RNA binding Source: UniProtKB-KW
  4. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  5. cysteine-type endopeptidase activity Source: InterPro
  6. endonuclease activity Source: UniProtKB-KW
  7. helicase activity Source: UniProtKB-KW
  8. methyltransferase activity Source: InterPro
  9. omega peptidase activity Source: InterPro
  10. zinc ion binding Source: InterPro

GO - Biological processi

  1. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
  2. induction by virus of catabolism of host mRNA Source: UniProtKB-KW
  3. induction by virus of host autophagy Source: UniProtKB-KW
  4. modulation by virus of host protein ubiquitination Source: UniProtKB-KW
  5. suppression by virus of host ISG15 activity Source: UniProtKB-KW
  6. suppression by virus of host translation Source: UniProtKB-KW
  7. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
  8. transcription, DNA-templated Source: InterPro
  9. viral RNA genome replication Source: InterPro
  10. viral protein processing Source: InterPro
  11. viral transcription Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Exonuclease, Helicase, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase

Keywords - Biological processi

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

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Replicase polyprotein 1ab
Short name:
pp1ab
Alternative name(s):
ORF1ab polyprotein
Cleaved into the following 15 chains:
Non-structural protein 1
Short name:
nsp1
Alternative name(s):
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
RNA-directed RNA polymerase (EC:2.7.7.48)
Short name:
Pol
Short name:
RdRp
Alternative name(s):
nsp12
Helicase (EC:3.6.4.12, EC:3.6.4.13)
Short name:
Hel
Alternative name(s):
nsp13
Exoribonuclease (EC:3.1.13.-)
Short name:
ExoN
Alternative name(s):
nsp14
Alternative name(s):
NendoU
nsp15
Alternative name(s):
nsp16
Gene namesi
Name:rep
ORF Names:1a-1b
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.
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.
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.
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.
Chain Helicase : Host endoplasmic reticulum-Golgi intermediate compartment Reviewed prediction
Note: The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA By similarity.

Topology

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

GO - Cellular componenti

  1. host cell endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
  2. host cell membrane Source: UniProtKB-SubCell
  3. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 180180Non-structural protein 1 By similarity
PRO_0000037309Add
BLAST
Chaini181 – 818638Non-structural protein 2 By similarity
PRO_0000037310Add
BLAST
Chaini819 – 27401922Non-structural protein 3 By similarity
PRO_0000037311Add
BLAST
Chaini2741 – 3240500Non-structural protein 4 Reviewed prediction
PRO_0000283841Add
BLAST
Chaini3241 – 35463063C-like proteinase By similarity
PRO_0000037312Add
BLAST
Chaini3547 – 3836290Non-structural protein 6 By similarity
PRO_0000037313Add
BLAST
Chaini3837 – 391983Non-structural protein 7 By similarity
PRO_0000037314Add
BLAST
Chaini3920 – 4117198Non-structural protein 8 By similarity
PRO_0000037315Add
BLAST
Chaini4118 – 4230113Non-structural protein 9 By similarity
PRO_0000037316Add
BLAST
Chaini4231 – 4369139Non-structural protein 10 By similarity
PRO_0000037317Add
BLAST
Chaini4370 – 5301932RNA-directed RNA polymerase By similarity
PRO_0000037318Add
BLAST
Chaini5302 – 5902601Helicase By similarity
PRO_0000037319Add
BLAST
Chaini5903 – 6429527Exoribonuclease By similarity
PRO_0000037320Add
BLAST
Chaini6430 – 6775346Uridylate-specific endoribonuclease By similarity
PRO_0000037321Add
BLAST
Chaini6776 – 7073298Putative 2'-O-methyl transferase By similarity
PRO_0000037322Add
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.

Proteomic databases

PRIDEiP0C6X7.

Interactioni

Subunit structurei

3CL-PRO exists as monomer and homodimer. Only the homodimer shows catalytic activity. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer By similarity. Interacts (via N-terminus) with DDX1.3 Publications

Protein-protein interaction databases

MINTiMINT-1487760.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 207
Turni23 – 253
Helixi35 – 4814
Beta strandi51 – 544
Helixi61 – 633
Beta strandi68 – 725
Beta strandi87 – 937
Turni95 – 984
Beta strandi99 – 1024
Beta strandi105 – 1095
Beta strandi116 – 1238
Beta strandi827 – 8293
Turni831 – 8333
Beta strandi839 – 8413
Beta strandi848 – 8514
Turni852 – 8565
Beta strandi860 – 8623
Turni869 – 8713
Helixi872 – 88211
Helixi888 – 8947
Helixi898 – 9014
Beta strandi907 – 9093
Beta strandi911 – 9155
Beta strandi918 – 9203
Beta strandi922 – 9265
Beta strandi1013 – 10219
Helixi1023 – 10308
Beta strandi1033 – 10386
Helixi1048 – 10569
Turni1057 – 10593
Helixi1060 – 107213
Beta strandi1080 – 10845
Turni1086 – 10883
Beta strandi1090 – 10956
Helixi1100 – 11023
Helixi1108 – 11147
Helixi1115 – 11184
Beta strandi1119 – 11246
Helixi1130 – 11323
Helixi1136 – 114611
Beta strandi1149 – 11568
Helixi1158 – 116811
Beta strandi1345 – 13473
Helixi1351 – 136111
Beta strandi1364 – 13685
Helixi1372 – 138110
Beta strandi1389 – 140113
Helixi1407 – 141711
Beta strandi1421 – 14244
Beta strandi1426 – 14283
Helixi1429 – 14313
Helixi1435 – 14428
Beta strandi1449 – 14524
Helixi1457 – 146711
Beta strandi1544 – 155512
Beta strandi1557 – 15626
Helixi1567 – 15715
Beta strandi1572 – 15765
Helixi1588 – 15903
Beta strandi1594 – 15974
Helixi1602 – 161211
Helixi1619 – 163012
Helixi1651 – 166111
Beta strandi1667 – 16693
Helixi1670 – 168011
Helixi1685 – 169410
Helixi1705 – 17139
Beta strandi1722 – 17287
Beta strandi1730 – 17323
Beta strandi1734 – 17407
Helixi1742 – 17454
Beta strandi1746 – 17494
Helixi1753 – 17586
Beta strandi1760 – 17634
Beta strandi1765 – 178521
Beta strandi1790 – 17934
Beta strandi1799 – 18079
Beta strandi1810 – 182617
Beta strandi1829 – 18346
Beta strandi1836 – 184611
Beta strandi1904 – 19118
Helixi1912 – 192110
Beta strandi1929 – 19368
Beta strandi1942 – 19487
Helixi1949 – 19513
Helixi1954 – 19563
Beta strandi1963 – 19664
Beta strandi1969 – 19713
Helixi1977 – 199014
Helixi3251 – 32544
Beta strandi3257 – 32626
Beta strandi3265 – 32728
Beta strandi3275 – 32795
Helixi3280 – 32834
Helixi3288 – 32903
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
Helixi3379 – 33813
Beta strandi3388 – 33936
Beta strandi3396 – 340611
Turni3408 – 34103
Beta strandi3412 – 34154
Beta strandi3421 – 34244
Beta strandi3427 – 34304
Helixi3441 – 345313
Turni3458 – 34603
Helixi3467 – 347610
Beta strandi3477 – 34793
Helixi3484 – 34896
Helixi3491 – 34977
Helixi3501 – 351414
Beta strandi3516 – 35183
Beta strandi3521 – 35233
Beta strandi3524 – 35263
Helixi3533 – 35397
Turni3540 – 35423
Helixi3837 – 385519
Helixi3862 – 387615
Beta strandi3878 – 38803
Helixi3881 – 390525
Helixi3906 – 39094
Turni3910 – 39123
Helixi3913 – 39164
Turni3959 – 39635
Turni3970 – 39723
Helixi3973 – 398715
Helixi3996 – 401722
Helixi4020 – 403011
Beta strandi4034 – 40374
Beta strandi4046 – 40516
Helixi4054 – 40607
Beta strandi4065 – 40684
Beta strandi4071 – 40799
Helixi4088 – 40903
Turni4093 – 40953
Helixi4096 – 40983
Beta strandi4103 – 41097
Beta strandi4120 – 41256
Beta strandi4127 – 41315
Beta strandi4134 – 41374
Beta strandi4145 – 41506
Beta strandi4153 – 41553
Beta strandi4157 – 41648
Beta strandi4170 – 41745
Beta strandi4181 – 41866
Beta strandi4191 – 41944
Beta strandi4201 – 42088
Helixi4213 – 422210
Helixi4224 – 42274
Helixi4243 – 42486
Beta strandi4250 – 42523
Helixi4253 – 426210
Beta strandi4284 – 42885
Beta strandi4295 – 43006
Helixi4301 – 43033
Helixi4305 – 43084
Beta strandi4314 – 43185
Beta strandi4325 – 43306
Helixi4331 – 43333
Helixi4337 – 43437
Turni4348 – 43503
Turni4354 – 43574
Helixi6431 – 644111
Beta strandi6453 – 64564
Beta strandi6459 – 64646
Beta strandi6467 – 64737
Beta strandi6476 – 64783
Helixi6480 – 64889
Beta strandi6493 – 64953
Helixi6498 – 65036
Beta strandi6508 – 65136
Turni6517 – 65204
Beta strandi6521 – 653010
Turni6532 – 65343
Beta strandi6535 – 65395
Helixi6543 – 65453
Beta strandi6550 – 65534
Helixi6559 – 65657
Beta strandi6567 – 65759
Beta strandi6589 – 65913
Beta strandi6594 – 65963
Beta strandi6599 – 66013
Beta strandi6606 – 66116
Beta strandi6614 – 66163
Helixi6629 – 66313
Helixi6637 – 66448
Helixi6647 – 66537
Helixi6661 – 66644
Beta strandi6670 – 66734
Beta strandi6677 – 66793
Helixi6680 – 668910
Beta strandi6692 – 66987
Beta strandi6703 – 67119
Turni6712 – 67143
Beta strandi6717 – 67248
Helixi6728 – 67369
Beta strandi6741 – 675111
Beta strandi6754 – 676310
Beta strandi6766 – 67727
Helixi6777 – 67804
Beta strandi6781 – 67855
Helixi6788 – 67914
Helixi6817 – 682913
Beta strandi6841 – 68466
Helixi6855 – 68639
Beta strandi6869 – 68768
Beta strandi6881 – 68888
Helixi6890 – 68923
Beta strandi6893 – 68975
Beta strandi6899 – 69046
Helixi6924 – 693512
Beta strandi6936 – 694611
Beta strandi6948 – 69503
Helixi6953 – 69597
Beta strandi6962 – 69709
Helixi6971 – 69733
Beta strandi6979 – 69868
Helixi6996 – 700914
Helixi7017 – 70204
Beta strandi7033 – 70353
Helixi7039 – 70413
Helixi7044 – 70518
Beta strandi7055 – 70573
Beta strandi7065 – 70673

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O5Smodel-A4745-5301[»]
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[»]
1SXFmodel-A4765-5244[»]
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[»]
2G1Fmodel-A/B5302-5877[»]
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/X4231-4378[»]
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/X4231-4378[»]
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[»]
2H85X-ray2.60A6429-6774[»]
2HOBX-ray1.95A3241-3546[»]
2HSXNMR-A13-127[»]
2IDYNMR-A819-930[»]
2JZDNMR-A1345-1469[»]
2JZENMR-A1345-1469[»]
2JZFNMR-A1331-1469[»]
2K87NMR-A1884-1998[»]
2OP9X-ray1.80A/B3241-3541[»]
2OZKX-ray2.90A/B/C/D6430-6775[»]
2PWXX-ray2.50A3241-3546[»]
2Q6GX-ray2.50A/B3241-3546[»]
2QC2X-ray2.70A/B3241-3546[»]
2QCYX-ray1.75A3241-3546[»]
2QIQX-ray1.90A3242-3541[»]
2RHBX-ray2.80A/B/C/D/E/F6430-6775[»]
2RNKNMR-A1331-1469[»]
2V6NX-ray1.98A3241-3546[»]
2VJ1X-ray2.25A/B3242-3544[»]
2XYQX-ray2.00A6776-7065[»]
B4240-4361[»]
2XYRX-ray2.50A6776-7067[»]
B4240-4361[»]
2XYVX-ray2.06A6776-7067[»]
B4240-4361[»]
2YY4X-ray2.20A/B3241-3556[»]
2Z3CX-ray1.79A3241-3546[»]
2Z3DX-ray2.10A3241-3546[»]
2Z3EX-ray2.32A3241-3546[»]
2Z94X-ray1.78A3241-3546[»]
2Z9GX-ray1.86A3241-3546[»]
2Z9JX-ray1.95A/B3241-3546[»]
2Z9KX-ray1.85A/B3241-3546[»]
2Z9LX-ray2.10A/B3241-3546[»]
3D62X-ray2.70A3243-3541[»]
3E9SX-ray2.50A1541-1855[»]
3EBNX-ray2.40A/B/C/D3429-3546[»]
3R24X-ray2.00A6776-7073[»]
B4240-4382[»]
ProteinModelPortaliP0C6X7.
SMRiP0C6X7. Positions 13-127, 819-930, 1002-1176, 1331-1469, 1541-1854, 3241-3546, 3837-3910, 3921-4111, 4118-4230, 4240-4362, 6430-6773.

Miscellaneous databases

EvolutionaryTraceiP0C6X7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1003 – 1169167Macro
Add
BLAST
Domaini1611 – 1875265Peptidase C16
Add
BLAST
Domaini3241 – 3546306Peptidase C30
Add
BLAST
Domaini4981 – 5143163RdRp catalytic
Add
BLAST
Domaini5302 – 538584CV MBD
Add
BLAST
Domaini5558 – 5739182(+)RNA virus helicase ATP-binding
Add
BLAST
Domaini5740 – 5909170(+)RNA virus helicase C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2092 – 2371280HD1
Add
BLAST
Regioni2755 – 3162408HD2
Add
BLAST
Regioni3564 – 3776213HD3
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi930 – 100172Glu-rich
Add
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.1 Publication

Sequence similaritiesi

Contains 1 Macro domain.

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_dom.
IPR021590. NSP1.
IPR009466. NSP11.
IPR024375. Nsp3_coronavir.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR027417. P-loop_NTPase.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009469. RNA_pol_N_coronovir.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR029063. SAM-dependent_MTases-like.
IPR024358. SARS-CoV_Nsp3_N.
IPR022733. SARS_polyprot_cleavage.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view]
PfamiPF06478. Corona_RPol_N. 1 hit.
PF12379. DUF3655. 1 hit.
PF01661. Macro. 1 hit.
PF11501. Nsp1. 1 hit.
PF09401. NSP10. 1 hit.
PF06471. NSP11. 1 hit.
PF06460. NSP13. 1 hit.
PF12124. Nsp3_PL2pro. 1 hit.
PF08716. nsp7. 1 hit.
PF08717. nsp8. 1 hit.
PF08710. nsp9. 1 hit.
PF05409. Peptidase_C30. 1 hit.
PF00680. RdRP_1. 1 hit.
PF11633. SUD-M. 1 hit.
PF01443. Viral_helicase1. 1 hit.
PF08715. Viral_protease. 1 hit.
[Graphical view]
SUPFAMiSSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51653. CV_MBD. 1 hit.
PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 1 hit.
PS51657. PSRV_HELICASE. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

Isoform Replicase polyprotein 1ab (identifier: P0C6X7-1) [UniParc]FASTAAdd to Basket

Also known as: pp1ab

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

« Hide

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 ADASTFLNRV CGVSAARLTP CGTGTSTDVV 4400
YRAFDIYNEK VAGFAKFLKT NCCRFQEKDE EGNLLDSYFV VKRHTMSNYQ 4450
HEETIYNLVK DCPAVAVHDF FKFRVDGDMV PHISRQRLTK YTMADLVYAL 4500
RHFDEGNCDT LKEILVTYNC CDDDYFNKKD WYDFVENPDI LRVYANLGER 4550
VRQSLLKTVQ FCDAMRDAGI VGVLTLDNQD LNGNWYDFGD FVQVAPGCGV 4600
PIVDSYYSLL MPILTLTRAL AAESHMDADL AKPLIKWDLL KYDFTEERLC 4650
LFDRYFKYWD QTYHPNCINC LDDRCILHCA NFNVLFSTVF PPTSFGPLVR 4700
KIFVDGVPFV VSTGYHFREL GVVHNQDVNL HSSRLSFKEL LVYAADPAMH 4750
AASGNLLLDK RTTCFSVAAL TNNVAFQTVK PGNFNKDFYD FAVSKGFFKE 4800
GSSVELKHFF FAQDGNAAIS DYDYYRYNLP TMCDIRQLLF VVEVVDKYFD 4850
CYDGGCINAN QVIVNNLDKS AGFPFNKWGK ARLYYDSMSY EDQDALFAYT 4900
KRNVIPTITQ MNLKYAISAK NRARTVAGVS ICSTMTNRQF HQKLLKSIAA 4950
TRGATVVIGT SKFYGGWHNM LKTVYSDVET PHLMGWDYPK CDRAMPNMLR 5000
IMASLVLARK HNTCCNLSHR FYRLANECAQ VLSEMVMCGG SLYVKPGGTS 5050
SGDATTAYAN SVFNICQAVT ANVNALLSTD GNKIADKYVR NLQHRLYECL 5100
YRNRDVDHEF VDEFYAYLRK HFSMMILSDD AVVCYNSNYA AQGLVASIKN 5150
FKAVLYYQNN VFMSEAKCWT ETDLTKGPHE FCSQHTMLVK QGDDYVYLPY 5200
PDPSRILGAG CFVDDIVKTD GTLMIERFVS LAIDAYPLTK HPNQEYADVF 5250
HLYLQYIRKL HDELTGHMLD MYSVMLTNDN TSRYWEPEFY EAMYTPHTVL 5300
QAVGACVLCN SQTSLRCGAC IRRPFLCCKC CYDHVISTSH KLVLSVNPYV 5350
CNAPGCDVTD VTQLYLGGMS YYCKSHKPPI SFPLCANGQV FGLYKNTCVG 5400
SDNVTDFNAI ATCDWTNAGD YILANTCTER LKLFAAETLK ATEETFKLSY 5450
GIATVREVLS DRELHLSWEV GKPRPPLNRN YVFTGYRVTK NSKVQIGEYT 5500
FEKGDYGDAV VYRGTTTYKL NVGDYFVLTS HTVMPLSAPT LVPQEHYVRI 5550
TGLYPTLNIS DEFSSNVANY QKVGMQKYST LQGPPGTGKS HFAIGLALYY 5600
PSARIVYTAC SHAAVDALCE KALKYLPIDK CSRIIPARAR VECFDKFKVN 5650
STLEQYVFCT VNALPETTAD IVVFDEISMA TNYDLSVVNA RLRAKHYVYI 5700
GDPAQLPAPR TLLTKGTLEP EYFNSVCRLM KTIGPDMFLG TCRRCPAEIV 5750
DTVSALVYDN KLKAHKDKSA QCFKMFYKGV ITHDVSSAIN RPQIGVVREF 5800
LTRNPAWRKA VFISPYNSQN AVASKILGLP TQTVDSSQGS EYDYVIFTQT 5850
TETAHSCNVN RFNVAITRAK IGILCIMSDR DLYDKLQFTS LEIPRRNVAT 5900
LQAENVTGLF KDCSKIITGL HPTQAPTHLS VDIKFKTEGL CVDIPGIPKD 5950
MTYRRLISMM GFKMNYQVNG YPNMFITREE AIRHVRAWIG FDVEGCHATR 6000
DAVGTNLPLQ LGFSTGVNLV AVPTGYVDTE NNTEFTRVNA KPPPGDQFKH 6050
LIPLMYKGLP WNVVRIKIVQ MLSDTLKGLS DRVVFVLWAH GFELTSMKYF 6100
VKIGPERTCC LCDKRATCFS TSSDTYACWN HSVGFDYVYN PFMIDVQQWG 6150
FTGNLQSNHD QHCQVHGNAH VASCDAIMTR CLAVHECFVK RVDWSVEYPI 6200
IGDELRVNSA CRKVQHMVVK SALLADKFPV LHDIGNPKAI KCVPQAEVEW 6250
KFYDAQPCSD KAYKIEELFY SYATHHDKFT DGVCLFWNCN VDRYPANAIV 6300
CRFDTRVLSN LNLPGCDGGS LYVNKHAFHT PAFDKSAFTN LKQLPFFYYS 6350
DSPCESHGKQ VVSDIDYVPL KSATCITRCN LGGAVCRHHA NEYRQYLDAY 6400
NMMISAGFSL WIYKQFDTYN LWNTFTRLQS LENVAYNVVN KGHFDGHAGE 6450
APVSIINNAV YTKVDGIDVE IFENKTTLPV NVAFELWAKR NIKPVPEIKI 6500
LNNLGVDIAA NTVIWDYKRE APAHVSTIGV CTMTDIAKKP TESACSSLTV 6550
LFDGRVEGQV DLFRNARNGV LITEGSVKGL TPSKGPAQAS VNGVTLIGES 6600
VKTQFNYFKK VDGIIQQLPE TYFTQSRDLE DFKPRSQMET DFLELAMDEF 6650
IQRYKLEGYA FEHIVYGDFS HGQLGGLHLM IGLAKRSQDS PLKLEDFIPM 6700
DSTVKNYFIT DAQTGSSKCV CSVIDLLLDD FVEIIKSQDL SVISKVVKVT 6750
IDYAEISFML WCKDGHVETF YPKLQASQAW QPGVAMPNLY KMQRMLLEKC 6800
DLQNYGENAV IPKGIMMNVA KYTQLCQYLN TLTLAVPYNM RVIHFGAGSD 6850
KGVAPGTAVL RQWLPTGTLL VDSDLNDFVS DADSTLIGDC ATVHTANKWD 6900
LIISDMYDPR TKHVTKENDS KEGFFTYLCG FIKQKLALGG SIAVKITEHS 6950
WNADLYKLMG HFSWWTAFVT NVNASSSEAF LIGANYLGKP KEQIDGYTMH 7000
ANYIFWRNTN PIQLSSYSLF DMSKFPLKLR GTAVMSLKEN QINDMIYSLL 7050
EKGRLIIREN NRVVVSSDIL VNN 7073

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

Length:7,073
Mass (Da):790,248
Last modified:June 10, 2008 - v1
Checksum:iE6504CAFDC36BC09
GO
Isoform Replicase polyprotein 1a (identifier: P0C6U8-1) [UniParc]FASTAAdd to Basket

Also known as: pp1a, ORF1a polyprotein

The sequence of this isoform can be found in the external entry P0C6U8.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by conventional translation.

Length:4,382
Mass (Da):486,373
GO

Sequence cautioni

The sequence AAP13440.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence AAP41036.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence AAP82975.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence AAP97881.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence AAQ01596.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence AAQ01608.1 differs from that shown. Reason: Erroneous gene model prediction.

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.
Natural varianti4411 – 44111V → S in strain: Isolate HKU-39849.
Natural varianti4459 – 44591V → I in strain: Isolate Shanghai QXC1.
Natural varianti4592 – 45921V → E in strain: Isolate ZJ01.
Natural varianti4910 – 49101Q → L in strain: Isolate ZJ01.
Natural varianti5112 – 51121D → G in strain: Isolate SZ3.
Natural varianti5131 – 51311A → G in strain: Isolate Taiwan.
Natural varianti5134 – 51352CY → VL in strain: Isolate Taiwan.
Natural varianti5623 – 56231L → S in strain: Isolate GD01.
Natural varianti5720 – 57201P → S in strain: Isolate GZ50 and Isolate SIN2500.
Natural varianti5744 – 57441R → C in strain: Isolate ZJ01.
Natural varianti5767 – 57671D → E in strain: Isolate CUHK-W1, Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04, Isolate SIN2500, Isolate GD01, Isolate GZ50, Isolate SZ3, Isolate SZ16 and Isolate Shanghai QXC1.
Natural varianti6274 – 62741T → I in strain: Isolate FRA, Isolate Frankfurt-1 Isolate SIN2677, Isolate SIN2679 and Isolate SIN2748.
Natural varianti6474 – 64741N → S in strain: Isolate Shanghai QXC1.
Natural varianti6700 – 67001M → I in strain: Isolate BJ03.
Natural varianti6721 – 67211C → R in strain: Isolate Shanghai QXC1.
Natural varianti6729 – 67291D → N in strain: Isolate GD01.
Natural varianti6840 – 68401M → L in strain: Isolate BJ02.
Natural varianti6862 – 68621Q → P in strain: Isolate BJ04.
Natural varianti6877 – 68771D → E in strain: Isolate GD01.
Natural varianti6910 – 69101R → K in strain: Isolate SZ3 and Isolate SZ16.
Natural varianti6937 – 69371A → P in strain: Isolate BJ03.
Natural varianti6992 – 69921E → D in strain: Isolate BJ04.
Natural varianti7008 – 70081N → K in strain: Isolate GD01.
Natural varianti7024 – 70241K → Q in strain: Isolate BJ04.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY278741 Genomic RNA. Translation: AAP13442.1.
AY278741 Genomic RNA. Translation: AAP13440.1. Sequence problems.
AY274119 Genomic RNA. Translation: AAP41036.1. Sequence problems.
AY278554 Genomic RNA. Translation: AAP13566.1.
AY282752 Genomic RNA. Translation: AAP30711.1.
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: AAP49011.4.
AY278488 Genomic RNA. Translation: AAP30028.1.
AY278489 Genomic RNA. Translation: AAP51225.1.
AY278490 Genomic RNA. No translation available.
AY279354 Genomic RNA. No translation available.
AY291451 Genomic RNA. Translation: AAP37015.1.
AY310120 Genomic RNA. Translation: AAP50483.1.
AY291315 Genomic RNA. Translation: AAP33696.1.
AY323977 Genomic RNA. Translation: AAP72973.2.
AY321118 Genomic RNA. No translation available.
AY338174 Genomic RNA. Translation: AAQ01594.1.
AY338174 Genomic RNA. Translation: AAQ01596.1. Sequence problems.
AY338175 Genomic RNA. Translation: AAQ01606.1.
AY338175 Genomic RNA. Translation: AAQ01608.1. Sequence problems.
AY348314 Genomic RNA. Translation: AAP97879.1.
AY348314 Genomic RNA. Translation: AAP97881.1. Sequence problems.
AP006557 Genomic RNA. Translation: BAC81346.1.
AP006558 Genomic RNA. Translation: BAC81360.1.
AP006559 Genomic RNA. Translation: BAC81374.1.
AP006560 Genomic RNA. Translation: BAC81388.1.
AP006561 Genomic RNA. Translation: BAC81402.1.
AY427439 Genomic RNA. Translation: AAQ94058.1.
AY322205 Genomic RNA. Translation: AAP82966.1.
AY322206 Genomic RNA. Translation: AAP82975.1. Sequence problems.
AY322207 Genomic RNA. Translation: AAP82967.1.
AY463059 Genomic RNA. Translation: AAP82978.2.
AY269391 Genomic RNA. Translation: AAP04003.1.
AY268049 Genomic RNA. Translation: AAP04587.1.
RefSeqiNP_828849.2. NC_004718.3. [P0C6X7-1]

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: AAP13442.1 .
AY278741 Genomic RNA. Translation: AAP13440.1 . Sequence problems.
AY274119 Genomic RNA. Translation: AAP41036.1 . Sequence problems.
AY278554 Genomic RNA. Translation: AAP13566.1 .
AY282752 Genomic RNA. Translation: AAP30711.1 .
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: AAP49011.4 .
AY278488 Genomic RNA. Translation: AAP30028.1 .
AY278489 Genomic RNA. Translation: AAP51225.1 .
AY278490 Genomic RNA. No translation available.
AY279354 Genomic RNA. No translation available.
AY291451 Genomic RNA. Translation: AAP37015.1 .
AY310120 Genomic RNA. Translation: AAP50483.1 .
AY291315 Genomic RNA. Translation: AAP33696.1 .
AY323977 Genomic RNA. Translation: AAP72973.2 .
AY321118 Genomic RNA. No translation available.
AY338174 Genomic RNA. Translation: AAQ01594.1 .
AY338174 Genomic RNA. Translation: AAQ01596.1 . Sequence problems.
AY338175 Genomic RNA. Translation: AAQ01606.1 .
AY338175 Genomic RNA. Translation: AAQ01608.1 . Sequence problems.
AY348314 Genomic RNA. Translation: AAP97879.1 .
AY348314 Genomic RNA. Translation: AAP97881.1 . Sequence problems.
AP006557 Genomic RNA. Translation: BAC81346.1 .
AP006558 Genomic RNA. Translation: BAC81360.1 .
AP006559 Genomic RNA. Translation: BAC81374.1 .
AP006560 Genomic RNA. Translation: BAC81388.1 .
AP006561 Genomic RNA. Translation: BAC81402.1 .
AY427439 Genomic RNA. Translation: AAQ94058.1 .
AY322205 Genomic RNA. Translation: AAP82966.1 .
AY322206 Genomic RNA. Translation: AAP82975.1 . Sequence problems.
AY322207 Genomic RNA. Translation: AAP82967.1 .
AY463059 Genomic RNA. Translation: AAP82978.2 .
AY269391 Genomic RNA. Translation: AAP04003.1 .
AY268049 Genomic RNA. Translation: AAP04587.1 .
RefSeqi NP_828849.2. NC_004718.3. [P0C6X7-1 ]

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1O5S model - A 4745-5301 [» ]
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 [» ]
1SXF model - A 4765-5244 [» ]
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 [» ]
2G1F model - A/B 5302-5877 [» ]
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 4231-4378 [» ]
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 4231-4378 [» ]
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 [» ]
2H85 X-ray 2.60 A 6429-6774 [» ]
2HOB X-ray 1.95 A 3241-3546 [» ]
2HSX NMR - A 13-127 [» ]
2IDY NMR - A 819-930 [» ]
2JZD NMR - A 1345-1469 [» ]
2JZE NMR - A 1345-1469 [» ]
2JZF NMR - A 1331-1469 [» ]
2K87 NMR - A 1884-1998 [» ]
2OP9 X-ray 1.80 A/B 3241-3541 [» ]
2OZK X-ray 2.90 A/B/C/D 6430-6775 [» ]
2PWX X-ray 2.50 A 3241-3546 [» ]
2Q6G X-ray 2.50 A/B 3241-3546 [» ]
2QC2 X-ray 2.70 A/B 3241-3546 [» ]
2QCY X-ray 1.75 A 3241-3546 [» ]
2QIQ X-ray 1.90 A 3242-3541 [» ]
2RHB X-ray 2.80 A/B/C/D/E/F 6430-6775 [» ]
2RNK NMR - A 1331-1469 [» ]
2V6N X-ray 1.98 A 3241-3546 [» ]
2VJ1 X-ray 2.25 A/B 3242-3544 [» ]
2XYQ X-ray 2.00 A 6776-7065 [» ]
B 4240-4361 [» ]
2XYR X-ray 2.50 A 6776-7067 [» ]
B 4240-4361 [» ]
2XYV X-ray 2.06 A 6776-7067 [» ]
B 4240-4361 [» ]
2YY4 X-ray 2.20 A/B 3241-3556 [» ]
2Z3C X-ray 1.79 A 3241-3546 [» ]
2Z3D X-ray 2.10 A 3241-3546 [» ]
2Z3E X-ray 2.32 A 3241-3546 [» ]
2Z94 X-ray 1.78 A 3241-3546 [» ]
2Z9G X-ray 1.86 A 3241-3546 [» ]
2Z9J X-ray 1.95 A/B 3241-3546 [» ]
2Z9K X-ray 1.85 A/B 3241-3546 [» ]
2Z9L X-ray 2.10 A/B 3241-3546 [» ]
3D62 X-ray 2.70 A 3243-3541 [» ]
3E9S X-ray 2.50 A 1541-1855 [» ]
3EBN X-ray 2.40 A/B/C/D 3429-3546 [» ]
3R24 X-ray 2.00 A 6776-7073 [» ]
B 4240-4382 [» ]
ProteinModelPortali P0C6X7.
SMRi P0C6X7. Positions 13-127, 819-930, 1002-1176, 1331-1469, 1541-1854, 3241-3546, 3837-3910, 3921-4111, 4118-4230, 4240-4362, 6430-6773.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1487760.

Chemistry

BindingDBi P0C6X7.
ChEMBLi CHEMBL5118.

Proteomic databases

PRIDEi P0C6X7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1489680.

Miscellaneous databases

EvolutionaryTracei P0C6X7.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027351. (+)RNA_virus_helicase_core_dom.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_dom.
IPR021590. NSP1.
IPR009466. NSP11.
IPR024375. Nsp3_coronavir.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR027417. P-loop_NTPase.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009469. RNA_pol_N_coronovir.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR029063. SAM-dependent_MTases-like.
IPR024358. SARS-CoV_Nsp3_N.
IPR022733. SARS_polyprot_cleavage.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view ]
Pfami PF06478. Corona_RPol_N. 1 hit.
PF12379. DUF3655. 1 hit.
PF01661. Macro. 1 hit.
PF11501. Nsp1. 1 hit.
PF09401. NSP10. 1 hit.
PF06471. NSP11. 1 hit.
PF06460. NSP13. 1 hit.
PF12124. Nsp3_PL2pro. 1 hit.
PF08716. nsp7. 1 hit.
PF08717. nsp8. 1 hit.
PF08710. nsp9. 1 hit.
PF05409. Peptidase_C30. 1 hit.
PF00680. RdRP_1. 1 hit.
PF11633. SUD-M. 1 hit.
PF01443. Viral_helicase1. 1 hit.
PF08715. Viral_protease. 1 hit.
[Graphical view ]
SUPFAMi SSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEi PS51653. CV_MBD. 1 hit.
PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 1 hit.
PS51657. PSRV_HELICASE. 1 hit.
PS50507. RDRP_SSRNA_POS. 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; 1655-5170 AND 6903-7073.
    Strain: Isolate Shanghai LY.
  20. Emery S., Erdman D.D., Peret T.C.T., Ksiazek T.G.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 4993-5127.
    Strain: Isolate Vietnam.
  21. "Detection of a novel human coronavirus in a severe acute respiratory syndrome patient in Taiwan."
    Lin J.-H., Chiu S.-C., Yang J.-Y., Wang S.-F., Chen H.-Y.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 4993-5136.
    Strain: Isolate Taiwan.
  22. "The severe acute respiratory syndrome (SARS) coronavirus NTPase/helicase belongs to a distinct class of 5' to 3' viral helicases."
    Tanner J.A., Watt R.M., Chai Y.-B., Lu L.-Y., Lin M.C., Peiris J.S., Poon L.L.M., Kung H.-F., Huang J.-D.
    J. Biol. Chem. 278:39578-39582(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF HELICASE.
  23. Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
  24. "Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase."
    Fan K., Wei P., Feng Q., Chen S., Huang C., Ma L., Lai B., Pei J., Liu Y., Chen J., Lai L.
    J. Biol. Chem. 279:1637-1642(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY OF 3C-LIKE PROTEINASE DOMAIN, SUBUNIT OF 3C-LIKE PROTEINASE DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES OF 3C-LIKE PROTEINASE DOMAIN.
  25. "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.
  26. "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.
  27. "Discovery of an RNA virus 3'->5' exoribonuclease that is critically involved in coronavirus RNA synthesis."
    Minskaia E., Hertzig T., Gorbalenya A.E., Campanacci V., Cambillau C., Canard B., Ziebuhr J.
    Proc. Natl. Acad. Sci. U.S.A. 103:5108-5113(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF EXORIBONUCLEASE.
    Strain: Isolate Frankfurt-1.
  28. "Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family."
    Ricagno S., Egloff M.-P., Ulferts R., Coutard B., Nurizzo D., Campanacci V., Cambillau C., Ziebuhr J., Canard B.
    Proc. Natl. Acad. Sci. U.S.A. 103:11892-11897(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF ENDONUCLEASE.
  29. Cited for: FUNCTION OF NSP8.
  30. "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.
  31. "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.
  32. "The cellular RNA helicase DDX1 interacts with coronavirus nonstructural protein 14 and enhances viral replication."
    Xu L., Khadijah S., Fang S., Wang L., Tay F.P., Liu D.X.
    J. Virol. 84:8571-8583(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX1.
  33. "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.
  34. "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.
  35. "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.
  36. "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.
  37. "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.
  38. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4107-4230.
  39. "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.
  40. "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.
  41. "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.
  42. "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.
  43. "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.
  44. "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.
  45. "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 nameiR1AB_CVHSA
AccessioniPrimary (citable) accession number: P0C6X7
Secondary accession number(s): P59641
, Q6WGN0, Q7T697, Q808C0, Q80BV7, Q80BV8, Q80E51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: July 9, 2014
This is version 66 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

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