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P0C6X7

- R1AB_CVHSA

UniProt

P0C6X7 - R1AB_CVHSA

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Protein

Replicase polyprotein 1ab

Gene

rep

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

Replicase polyprotein 1ab: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.
Host translation inhibitor nsp1: Inhibits host translation by interacting with the 40S ribosomal subunit. 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.1 Publication
Non-structural protein 2: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.1 Publication
Papain-like proteinase: Responsible for the cleavages located at the N-terminus of the 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. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.2 Publications
Non-structural protein 4: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.1 Publication
Proteinase 3CL-PRO: Ccleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP).1 PublicationPROSITE-ProRule annotation
Non-structural protein 6: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.1 Publication
Non-structural protein 7: Forms an hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.1 Publication
Non-structural protein 8: Forms an hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.1 Publication
Non-structural protein 9: May participate in viral replication by acting as a ssRNA-binding protein.1 Publication
Non-structural protein 10: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.1 Publication
RNA-directed RNA polymerase: Responsible for replication and transcription of the viral RNA genome.1 Publication
Helicase: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium.2 Publications
Guanine-N7 methyltransferase: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity.3 Publications
Uridylate-specific endoribonuclease: Mn2+-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.
2'-O-methyltransferase: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.2 PublicationsCurated

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).1 PublicationPROSITE-ProRule annotation
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/GKFKK1 Publication
  3. KM=1.44 mM for peptide ATVRLQ/AGNAT1 Publication

pH dependencei

Optimum pH is 7.0 for 3C-like proteinase activity.1 Publication

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
Sitei5301 – 53022Cleavage; by 3CL-PROBy similarity
Sitei5902 – 59032Cleavage; by 3CL-PROBy similarity
Sitei6429 – 64302Cleavage; by 3CL-PROBy similarity
Sitei6775 – 67762Cleavage; 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
Nucleotide bindingi5583 – 55908ATPBy similarity

GO - Molecular functioni

  1. 3'-5'-exoribonuclease activity Source: CACAO
  2. ATP binding Source: UniProtKB-KW
  3. cysteine-type endopeptidase activity Source: InterPro
  4. endonuclease activity Source: UniProtKB-KW
  5. helicase activity Source: UniProtKB
  6. Lys48-specific deubiquitinase activity Source: UniProtKB
  7. methyltransferase activity Source: InterPro
  8. mRNA (guanine-N7-)-methyltransferase activity Source: UniProtKB
  9. mRNA (nucleoside-2'-O-)-methyltransferase activity Source: UniProtKB
  10. omega peptidase activity Source: InterPro
  11. RNA binding Source: UniProtKB-KW
  12. RNA-directed RNA polymerase activity Source: UniProtKB
  13. single-stranded RNA binding Source: UniProtKB
  14. zinc ion binding Source: InterPro

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: UniProtKB
  2. induction by virus of catabolism of host mRNA Source: UniProtKB-KW
  3. induction by virus of host autophagy Source: UniProtKB-KW
  4. metabolic process Source: GOC
  5. modulation by virus of host autophagy Source: UniProtKB
  6. modulation by virus of host protein ubiquitination Source: UniProtKB
  7. mRNA methylation Source: UniProtKB
  8. positive regulation of ubiquitin-specific protease activity Source: UniProtKB
  9. protein K48-linked deubiquitination Source: GOC
  10. RNA (guanine-N7)-methylation Source: GOC
  11. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
  12. suppression by virus of host gene expression Source: UniProtKB-KW
  13. suppression by virus of host IRF3 activity by inhibition of IRF3 phosphorylation Source: UniProtKB
  14. suppression by virus of host ISG15 activity Source: UniProtKB
  15. suppression by virus of host NF-kappaB transcription factor activity Source: UniProtKB
  16. suppression by virus of host translation Source: UniProtKB
  17. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB
  18. transcription, DNA-templated Source: InterPro
  19. transcription, RNA-templated Source: UniProtKB
  20. viral protein processing Source: InterPro
  21. viral RNA genome replication Source: InterPro
  22. 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, Inhibition of host NF-kappa-B 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:
Alternative name(s):
Leader protein
Non-structural protein 2
Short name:
nsp2
Alternative name(s):
p65 homolog
Papain-like proteinase (EC:3.4.19.12, EC:3.4.22.69)
Short name:
PL-PRO
Alternative name(s):
Non-structural protein 3
Short name:
nsp3
PL2-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
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 Papain-like proteinase : Host membrane; Multi-pass membrane protein. Host cytoplasm 1 Publication
Chain Non-structural protein 4 : Host membrane; Multi-pass membrane protein. Host cytoplasm
Note: Localizes in virally-induced cytoplasmic double-membrane vesicles.3 Publications
Chain Non-structural protein 7 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity
Chain Non-structural protein 8 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity
Chain Non-structural protein 9 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity
Chain Non-structural protein 10 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity
Chain Helicase : Host endoplasmic reticulum-Golgi intermediate compartment Curated
Note: The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA.By similarity

GO - Cellular componenti

  1. host cell 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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4217 – 42171G → E: Complete loss of nsp9 dimerization. 1 Publication
Mutagenesisi4221 – 42211G → E: Complete loss of nsp9 dimerization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 180180Host translation inhibitor nsp1By similarityPRO_0000037309Add
BLAST
Chaini181 – 818638Non-structural protein 2By similarityPRO_0000037310Add
BLAST
Chaini819 – 27401922Papain-like proteinaseBy similarityPRO_0000037311Add
BLAST
Chaini2741 – 3240500Non-structural protein 4Sequence AnalysisPRO_0000283841Add
BLAST
Chaini3241 – 35463063C-like proteinaseBy similarityPRO_0000037312Add
BLAST
Chaini3547 – 3836290Non-structural protein 6By similarityPRO_0000037313Add
BLAST
Chaini3837 – 391983Non-structural protein 7By similarityPRO_0000037314Add
BLAST
Chaini3920 – 4117198Non-structural protein 8By similarityPRO_0000037315Add
BLAST
Chaini4118 – 4230113Non-structural protein 9By similarityPRO_0000037316Add
BLAST
Chaini4231 – 4369139Non-structural protein 10By similarityPRO_0000037317Add
BLAST
Chaini4370 – 5301932RNA-directed RNA polymeraseBy similarityPRO_0000037318Add
BLAST
Chaini5302 – 5902601HelicaseBy similarityPRO_0000037319Add
BLAST
Chaini5903 – 6429527Guanine-N7 methyltransferaseBy similarityPRO_0000037320Add
BLAST
Chaini6430 – 6775346Uridylate-specific endoribonucleaseBy similarityPRO_0000037321Add
BLAST
Chaini6776 – 70732982'-O-methyltransferaseBy similarityPRO_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).By similarity

Proteomic databases

PRIDEiP0C6X7.

Interactioni

Subunit structurei

Nsp2 interacts with host PHB and PHB2. 3CL-PRO exists as monomer and homodimer. Nsp4 interacts with PL-PRO and nsp6. Only the homodimer shows catalytic activity. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure. Nsp9 is a dimer. Nsp10 forms a dodecamer and interacts with nsp14 and nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities. Nsp14 interacts (via N-terminus) with DDX1.8 Publications

Protein-protein interaction databases

MINTiMINT-1487760.

Structurei

Secondary structure

1
7073
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C6X7.

Transmembrane

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1003 – 1169167MacroPROSITE-ProRule annotationAdd
BLAST
Domaini1611 – 1875265Peptidase C16PROSITE-ProRule annotationAdd
BLAST
Domaini3241 – 3546306Peptidase C30PROSITE-ProRule annotationAdd
BLAST
Domaini4981 – 5143163RdRp catalyticPROSITE-ProRule annotationAdd
BLAST
Domaini5302 – 538584CV MBDAdd
BLAST
Domaini5558 – 5739182(+)RNA virus helicase ATP-bindingAdd
BLAST
Domaini5740 – 5909170(+)RNA virus helicase C-terminalAdd
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
Contains 1 RdRp catalytic 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

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

        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 4390 4400
GMWKGYGCSC DQLREPLMQS ADASTFLNRV CGVSAARLTP CGTGTSTDVV
4410 4420 4430 4440 4450
YRAFDIYNEK VAGFAKFLKT NCCRFQEKDE EGNLLDSYFV VKRHTMSNYQ
4460 4470 4480 4490 4500
HEETIYNLVK DCPAVAVHDF FKFRVDGDMV PHISRQRLTK YTMADLVYAL
4510 4520 4530 4540 4550
RHFDEGNCDT LKEILVTYNC CDDDYFNKKD WYDFVENPDI LRVYANLGER
4560 4570 4580 4590 4600
VRQSLLKTVQ FCDAMRDAGI VGVLTLDNQD LNGNWYDFGD FVQVAPGCGV
4610 4620 4630 4640 4650
PIVDSYYSLL MPILTLTRAL AAESHMDADL AKPLIKWDLL KYDFTEERLC
4660 4670 4680 4690 4700
LFDRYFKYWD QTYHPNCINC LDDRCILHCA NFNVLFSTVF PPTSFGPLVR
4710 4720 4730 4740 4750
KIFVDGVPFV VSTGYHFREL GVVHNQDVNL HSSRLSFKEL LVYAADPAMH
4760 4770 4780 4790 4800
AASGNLLLDK RTTCFSVAAL TNNVAFQTVK PGNFNKDFYD FAVSKGFFKE
4810 4820 4830 4840 4850
GSSVELKHFF FAQDGNAAIS DYDYYRYNLP TMCDIRQLLF VVEVVDKYFD
4860 4870 4880 4890 4900
CYDGGCINAN QVIVNNLDKS AGFPFNKWGK ARLYYDSMSY EDQDALFAYT
4910 4920 4930 4940 4950
KRNVIPTITQ MNLKYAISAK NRARTVAGVS ICSTMTNRQF HQKLLKSIAA
4960 4970 4980 4990 5000
TRGATVVIGT SKFYGGWHNM LKTVYSDVET PHLMGWDYPK CDRAMPNMLR
5010 5020 5030 5040 5050
IMASLVLARK HNTCCNLSHR FYRLANECAQ VLSEMVMCGG SLYVKPGGTS
5060 5070 5080 5090 5100
SGDATTAYAN SVFNICQAVT ANVNALLSTD GNKIADKYVR NLQHRLYECL
5110 5120 5130 5140 5150
YRNRDVDHEF VDEFYAYLRK HFSMMILSDD AVVCYNSNYA AQGLVASIKN
5160 5170 5180 5190 5200
FKAVLYYQNN VFMSEAKCWT ETDLTKGPHE FCSQHTMLVK QGDDYVYLPY
5210 5220 5230 5240 5250
PDPSRILGAG CFVDDIVKTD GTLMIERFVS LAIDAYPLTK HPNQEYADVF
5260 5270 5280 5290 5300
HLYLQYIRKL HDELTGHMLD MYSVMLTNDN TSRYWEPEFY EAMYTPHTVL
5310 5320 5330 5340 5350
QAVGACVLCN SQTSLRCGAC IRRPFLCCKC CYDHVISTSH KLVLSVNPYV
5360 5370 5380 5390 5400
CNAPGCDVTD VTQLYLGGMS YYCKSHKPPI SFPLCANGQV FGLYKNTCVG
5410 5420 5430 5440 5450
SDNVTDFNAI ATCDWTNAGD YILANTCTER LKLFAAETLK ATEETFKLSY
5460 5470 5480 5490 5500
GIATVREVLS DRELHLSWEV GKPRPPLNRN YVFTGYRVTK NSKVQIGEYT
5510 5520 5530 5540 5550
FEKGDYGDAV VYRGTTTYKL NVGDYFVLTS HTVMPLSAPT LVPQEHYVRI
5560 5570 5580 5590 5600
TGLYPTLNIS DEFSSNVANY QKVGMQKYST LQGPPGTGKS HFAIGLALYY
5610 5620 5630 5640 5650
PSARIVYTAC SHAAVDALCE KALKYLPIDK CSRIIPARAR VECFDKFKVN
5660 5670 5680 5690 5700
STLEQYVFCT VNALPETTAD IVVFDEISMA TNYDLSVVNA RLRAKHYVYI
5710 5720 5730 5740 5750
GDPAQLPAPR TLLTKGTLEP EYFNSVCRLM KTIGPDMFLG TCRRCPAEIV
5760 5770 5780 5790 5800
DTVSALVYDN KLKAHKDKSA QCFKMFYKGV ITHDVSSAIN RPQIGVVREF
5810 5820 5830 5840 5850
LTRNPAWRKA VFISPYNSQN AVASKILGLP TQTVDSSQGS EYDYVIFTQT
5860 5870 5880 5890 5900
TETAHSCNVN RFNVAITRAK IGILCIMSDR DLYDKLQFTS LEIPRRNVAT
5910 5920 5930 5940 5950
LQAENVTGLF KDCSKIITGL HPTQAPTHLS VDIKFKTEGL CVDIPGIPKD
5960 5970 5980 5990 6000
MTYRRLISMM GFKMNYQVNG YPNMFITREE AIRHVRAWIG FDVEGCHATR
6010 6020 6030 6040 6050
DAVGTNLPLQ LGFSTGVNLV AVPTGYVDTE NNTEFTRVNA KPPPGDQFKH
6060 6070 6080 6090 6100
LIPLMYKGLP WNVVRIKIVQ MLSDTLKGLS DRVVFVLWAH GFELTSMKYF
6110 6120 6130 6140 6150
VKIGPERTCC LCDKRATCFS TSSDTYACWN HSVGFDYVYN PFMIDVQQWG
6160 6170 6180 6190 6200
FTGNLQSNHD QHCQVHGNAH VASCDAIMTR CLAVHECFVK RVDWSVEYPI
6210 6220 6230 6240 6250
IGDELRVNSA CRKVQHMVVK SALLADKFPV LHDIGNPKAI KCVPQAEVEW
6260 6270 6280 6290 6300
KFYDAQPCSD KAYKIEELFY SYATHHDKFT DGVCLFWNCN VDRYPANAIV
6310 6320 6330 6340 6350
CRFDTRVLSN LNLPGCDGGS LYVNKHAFHT PAFDKSAFTN LKQLPFFYYS
6360 6370 6380 6390 6400
DSPCESHGKQ VVSDIDYVPL KSATCITRCN LGGAVCRHHA NEYRQYLDAY
6410 6420 6430 6440 6450
NMMISAGFSL WIYKQFDTYN LWNTFTRLQS LENVAYNVVN KGHFDGHAGE
6460 6470 6480 6490 6500
APVSIINNAV YTKVDGIDVE IFENKTTLPV NVAFELWAKR NIKPVPEIKI
6510 6520 6530 6540 6550
LNNLGVDIAA NTVIWDYKRE APAHVSTIGV CTMTDIAKKP TESACSSLTV
6560 6570 6580 6590 6600
LFDGRVEGQV DLFRNARNGV LITEGSVKGL TPSKGPAQAS VNGVTLIGES
6610 6620 6630 6640 6650
VKTQFNYFKK VDGIIQQLPE TYFTQSRDLE DFKPRSQMET DFLELAMDEF
6660 6670 6680 6690 6700
IQRYKLEGYA FEHIVYGDFS HGQLGGLHLM IGLAKRSQDS PLKLEDFIPM
6710 6720 6730 6740 6750
DSTVKNYFIT DAQTGSSKCV CSVIDLLLDD FVEIIKSQDL SVISKVVKVT
6760 6770 6780 6790 6800
IDYAEISFML WCKDGHVETF YPKLQASQAW QPGVAMPNLY KMQRMLLEKC
6810 6820 6830 6840 6850
DLQNYGENAV IPKGIMMNVA KYTQLCQYLN TLTLAVPYNM RVIHFGAGSD
6860 6870 6880 6890 6900
KGVAPGTAVL RQWLPTGTLL VDSDLNDFVS DADSTLIGDC ATVHTANKWD
6910 6920 6930 6940 6950
LIISDMYDPR TKHVTKENDS KEGFFTYLCG FIKQKLALGG SIAVKITEHS
6960 6970 6980 6990 7000
WNADLYKLMG HFSWWTAFVT NVNASSSEAF LIGANYLGKP KEQIDGYTMH
7010 7020 7030 7040 7050
ANYIFWRNTN PIQLSSYSLF DMSKFPLKLR GTAVMSLKEN QINDMIYSLL
7060 7070
EKGRLIIREN NRVVVSSDIL VNN

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: FUNCTION (HELICASE).
  23. Cited for: PROTEOLYTIC PROCESSING (REPLICASE POLYPROTEIN 1AB).
  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 (3C-LIKE PROTEINASE), SUBUNIT (3C-LIKE PROTEINASE), BIOPHYSICOCHEMICAL PROPERTIES (3C-LIKE PROTEINASE).
  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 (REPLICASE POLYPROTEIN 1AB).
  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 (REPLICASE POLYPROTEIN 1AB).
    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: FUNCTION (GUANINE-N7 METHYLTRANSFERASE).
    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 (URIDYLATE-SPECIFIC ENDORIBONUCLEASE).
  29. Cited for: FUNCTION (NON-STRUCTURAL PROTEIN 8).
  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 (PAPAIN-LIKE PROTEINASE).
  31. "Localization and membrane topology of coronavirus nonstructural protein 4: involvement of the early secretory pathway in replication."
    Oostra M., te Lintelo E.G., Deijs M., Verheije M.H., Rottier P.J., de Haan C.A.
    J. Virol. 81:12323-12336(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4).
  32. "Coronavirus nonstructural protein 16 is a cap-0 binding enzyme possessing (nucleoside-2'O)-methyltransferase activity."
    Decroly E., Imbert I., Coutard B., Bouvet M., Selisko B., Alvarez K., Gorbalenya A.E., Snijder E.J., Canard B.
    J. Virol. 82:8071-8084(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (2'-O-METHYLTRANSFERASE).
  33. "Genome-wide analysis of protein-protein interactions and involvement of viral proteins in SARS-CoV replication."
    Pan J., Peng X., Gao Y., Li Z., Lu X., Chen Y., Ishaq M., Liu D., Dediego M.L., Enjuanes L., Guo D.
    PLoS ONE 3:E3299-E3299(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF NSP10 WITH NSP14 AND NSP16.
  34. "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 (PAPAIN-LIKE PROTEINASE).
  35. "Severe acute respiratory syndrome coronavirus nonstructural protein 2 interacts with a host protein complex involved in mitochondrial biogenesis and intracellular signaling."
    Cornillez-Ty C.T., Liao L., Yates J.R., Kuhn P., Buchmeier M.J.
    J. Virol. 83:10314-10318(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (NON-STRUCTURAL PROTEIN 2), INTERACTION WITH HOST PHB AND PHB2.
  36. "Severe acute respiratory syndrome coronavirus nsp9 dimerization is essential for efficient viral growth."
    Miknis Z.J., Donaldson E.F., Umland T.C., Rimmer R.A., Baric R.S., Schultz L.W.
    J. Virol. 83:3007-3018(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (NON-STRUCTURAL PROTEIN 9), MUTAGENESIS OF GLY-4217 AND GLY-4221.
  37. "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 OF NSP14 WITH DDX1.
  38. "In vitro reconstitution of SARS-coronavirus mRNA cap methylation."
    Bouvet M., Debarnot C., Imbert I., Selisko B., Snijder E.J., Canard B., Decroly E.
    PLoS Pathog. 6:E1000863-E1000863(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (GUANINE-N7 METHYLTRANSFERASE), FUNCTION (2'-O-METHYLTRANSFERASE).
  39. "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 (HOST TRANSLATION INHIBITOR NSP1).
  40. "Mobility and interactions of coronavirus nonstructural protein 4."
    Hagemeijer M.C., Ulasli M., Vonk A.M., Reggiori F., Rottier P.J., de Haan C.A.
    J. Virol. 85:4572-4577(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF NSP4 WITH PL-PRO AND NSP6, SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4).
  41. "The SARS-coronavirus nsp7+nsp8 complex is a unique multimeric RNA polymerase capable of both de novo initiation and primer extension."
    te Velthuis A.J., van den Worm S.H., Snijder E.J.
    Nucleic Acids Res. 40:1737-1747(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (NON-STRUCTURAL PROTEIN 7), FUNCTION (NON-STRUCTURAL PROTEIN 8).
  42. "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 (HOST TRANSLATION INHIBITOR NSP1).
  43. Cited for: FUNCTION (HELICASE).
  44. "Biochemical characterization of a recombinant SARS coronavirus nsp12 RNA-dependent RNA polymerase capable of copying viral RNA templates."
    Ahn D.G., Choi J.K., Taylor D.R., Oh J.W.
    Arch. Virol. 157:2095-2104(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (RNA-DIRECTED RNA POLYMERASE).
  45. "RNA 3'-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex."
    Bouvet M., Imbert I., Subissi L., Gluais L., Canard B., Decroly E.
    Proc. Natl. Acad. Sci. U.S.A. 109:9372-9377(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (NON-STRUCTURAL PROTEIN 10), FUNCTION (GUANINE-N7 METHYLTRANSFERASE), INTERACTION OF NSP10 AND NSP14.
  46. "Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4, and 6 induce double-membrane vesicles."
    Angelini M.M., Akhlaghpour M., Neuman B.W., Buchmeier M.J.
    MBio 4:0-0(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (NON-STRUCTURAL PROTEIN 4), SUBCELLULAR LOCATION (NON-STRUCTURAL PROTEIN 4).
  47. "Coronavirus NSP6 restricts autophagosome expansion."
    Cottam E.M., Whelband M.C., Wileman T.
    Autophagy 10:1426-1441(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (NON-STRUCTURAL PROTEIN 6).
  48. "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.
  49. "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.
  50. "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.
  51. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4107-4230, INTERACTION OF NSP8 WITH NSP9.
  52. "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.
  53. "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, FUNCTION (3C-LIKE PROTEINASE).
  54. "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.
  55. "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.
  56. "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, SUBUNIT (NON-STRUCTURAL PROTEIN 10).
  57. "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.
  58. "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: October 29, 2014
This is version 68 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