P0C6X7 (R1AB_CVHSA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Replicase polyprotein 1ab
Short name=pp1ab

Alternative name(s):
ORF1ab polyprotein

Cleaved into the following 15 chains:

1. Non-structural protein 1
   Short name=nsp1
   Alternative name(s):
   Leader protein
2. Non-structural protein 2
   Short name=nsp2
   Alternative name(s):
   p65 homolog
3. Non-structural protein 3
   Short name=nsp3
   EC=3.4.19.12
   EC=3.4.22.69
   Alternative name(s):
   PL2-PRO
   Papain-like proteinase
   Short name=PL-PRO
   SARS coronavirus main proteinase
4. Non-structural protein 4
   Short name=nsp4
5. 3C-like proteinase
   Short name=3CL-PRO
   Short name=3CLp
   EC=3.4.22.-
   Alternative name(s):
   nsp5
6. Non-structural protein 6
   Short name=nsp6
7. Non-structural protein 7
   Short name=nsp7
8. Non-structural protein 8
   Short name=nsp8
9. Non-structural protein 9
   Short name=nsp9
10. Non-structural protein 10
    Short name=nsp10
    Alternative name(s):
    Growth factor-like peptide
    Short name=GFL
11. RNA-directed RNA polymerase
    Short name=Pol
    Short name=RdRp
    EC=2.7.7.48
    Alternative name(s):
    nsp12
12. Helicase
    Short name=Hel
    EC=3.6.4.12
    EC=3.6.4.13
    Alternative name(s):
    nsp13
13. Exoribonuclease
    Short name=ExoN
    EC=3.1.13.-
    Alternative name(s):
    nsp14
14. Uridylate-specific endoribonuclease
    EC=3.1.-.-
    Alternative name(s):
    NendoU
    nsp15
15. Putative 2'-O-methyl transferase
    EC=2.1.1.-
    Alternative name(s):
    nsp16

Gene names

Name:	rep
ORF Names:	1a-1b

Organism

Human SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome coronavirus) [Reference proteome]

Taxonomic identifier

227859 [NCBI]

Taxonomic lineage

Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Nidovirales › Coronaviridae › Coronavirinae › Betacoronavirus › Severe acute respiratory syndrome-related coronavirus

Virus host

Homo sapiens (Human) [TaxID: 9606]
Paguma larvata (Masked palm civet) [TaxID: 9675]

Protein attributes

Sequence length	7073 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.30 Ref.31 Ref.32 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. Ref.30 Ref.31 Ref.32 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. Ref.30 Ref.31 Ref.32 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. Ref.30 Ref.31 Ref.32 The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction. Ref.30 Ref.31 Ref.32 Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter. Ref.30 Ref.31 Ref.32 Nsp9 is a ssRNA-binding protein. Ref.30 Ref.31 Ref.32 NendoU is a Mn2+-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond. Ref.30 Ref.31 Ref.32
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). Ref.25 ATP + H2O = ADP + phosphate. Ref.25 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. Ref.25 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). Ref.25
Subunit structure	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. Ref.25 Ref.33 Ref.38
Subcellular location	Non-structural protein 3: Host membrane; Multi-pass membrane protein Potential. Non-structural protein 4: Host membrane; Multi-pass membrane protein Potential. Non-structural protein 6: Host membrane; Multi-pass membrane protein Potential. Non-structural protein 7: Host cytoplasm › host 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. Non-structural protein 8: Host cytoplasm › host 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. Non-structural protein 9: Host cytoplasm › host 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. Non-structural protein 10: Host cytoplasm › host 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. Helicase: Host endoplasmic reticulum-Golgi intermediate compartment Potential. Note: The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA By similarity. Uridylate-specific endoribonuclease: Host cytoplasm › host perinuclear region By similarity.
Domain	The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane. Ref.25
Post-translational modification	Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed By similarity.
Sequence similarities	Belongs to the coronaviruses polyprotein 1ab family. Contains 1 (+)RNA virus helicase ATP-binding domain. Contains 1 (+)RNA virus helicase C-terminal domain. Contains 1 CV MBD (coronavirus metal-binding) domain. Contains 1 Macro domain. Contains 1 peptidase C16 domain. Contains 1 peptidase C30 domain. Contains 1 RdRp catalytic domain.
Caution	Isolates SZ3 and SZ16 have been isolated from Paguma larvata and are described as SARS-like in litterature.
Biophysicochemical properties	Kinetic parameters: The kinetic parameters are studied for the 3C-like proteinase domain. The cleavage takes place at the /. KM=1.15 mM for peptide TSAVLQ/SGFRK-NH2 Ref.25 KM=0.58 mM for peptide SGVTFQ/GKFKK KM=1.44 mM for peptide ATVRLQ/AGNAT pH dependence: Optimum pH is 7.0 for 3C-like proteinase activity.
Sequence caution	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.

Ontologies

Keywords
Biological process	Activation of host autophagy by virus Host-virus interaction Inhibition of host ISG15 by virus Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Modulation of host ubiquitin pathway by viral deubiquitinase Modulation of host ubiquitin pathway by virus Ubl conjugation pathway Viral RNA replication Viral immunoevasion
Cellular component	Host cytoplasm Host membrane Membrane
Coding sequence diversity	Ribosomal frameshifting
Domain	Repeat Transmembrane Transmembrane helix Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc
Molecular function	Endonuclease Exonuclease Helicase Hydrolase Nuclease Nucleotidyltransferase Protease RNA-directed RNA polymerase Thiol protease Transferase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	induction by virus of host autophagy Inferred from electronic annotation. Source: UniProtKB-KW methylation Inferred from electronic annotation. Source: GOC modulation by virus of host protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC proteolysis Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host ISG15 activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro viral genome replication Inferred from electronic annotation. Source: InterPro viral protein processing Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell endoplasmic reticulum-Golgi intermediate compartment Inferred from electronic annotation. Source: UniProtKB-SubCell host cell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host cell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW viral replication complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW exoribonuclease activity, producing 5'-phosphomonoesters Inferred from electronic annotation. Source: InterPro helicase activity Inferred from electronic annotation. Source: UniProtKB-KW methyltransferase activity Inferred from electronic annotation. Source: InterPro omega peptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]

Isoform Replicase polyprotein 1ab (identifier: P0C6X7-1)

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.

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

Isoform Replicase polyprotein 1a (identifier: P0C6U8-1)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 180

180

Non-structural protein 1 By similarity

PRO_0000037309

Chain

181 – 818

638

Non-structural protein 2 By similarity

PRO_0000037310

Chain

819 – 2740

1922

Non-structural protein 3 By similarity

PRO_0000037311

Chain

2741 – 3240

500

Non-structural protein 4 Potential

PRO_0000283841

Chain

3241 – 3546

306

3C-like proteinase By similarity

PRO_0000037312

Chain

3547 – 3836

290

Non-structural protein 6 By similarity

PRO_0000037313

Chain

3837 – 3919

83

Non-structural protein 7 By similarity

PRO_0000037314

Chain

3920 – 4117

198

Non-structural protein 8 By similarity

PRO_0000037315

Chain

4118 – 4230

113

Non-structural protein 9 By similarity

PRO_0000037316

Chain

4231 – 4369

139

Non-structural protein 10 By similarity

PRO_0000037317

Chain

4370 – 5301

932

RNA-directed RNA polymerase By similarity

PRO_0000037318

Chain

5302 – 5902

601

Helicase By similarity

PRO_0000037319

Chain

5903 – 6429

527

Exoribonuclease By similarity

PRO_0000037320

Chain

6430 – 6775

346

Uridylate-specific endoribonuclease By similarity

PRO_0000037321

Chain

6776 – 7073

298

Putative 2'-O-methyl transferase By similarity

PRO_0000037322

Regions

Transmembrane

2092 – 2112

21

Helical; Potential

Transmembrane

2203 – 2223

21

Helical; Potential

Transmembrane

2304 – 2324

21

Helical; Potential

Transmembrane

2326 – 2346

21

Helical; Potential

Transmembrane

2351 – 2371

21

Helical; Potential

Transmembrane

2755 – 2775

21

Helical; Potential

Transmembrane

2830 – 2850

21

Helical; Potential

Transmembrane

2879 – 2899

21

Helical; Potential

Transmembrane

2992 – 3012

21

Helical; Potential

Transmembrane

3022 – 3042

21

Helical; Potential

Transmembrane

3054 – 3074

21

Helical; Potential

Transmembrane

3077 – 3097

21

Helical; Potential

Transmembrane

3105 – 3125

21

Helical; Potential

Transmembrane

3142 – 3162

21

Helical; Potential

Transmembrane

3564 – 3584

21

Helical; Potential

Transmembrane

3586 – 3606

21

Helical; Potential

Transmembrane

3612 – 3632

21

Helical; Potential

Transmembrane

3658 – 3678

21

Helical; Potential

Transmembrane

3707 – 3727

21

Helical; Potential

Transmembrane

3728 – 3748

21

Helical; Potential

Transmembrane

3756 – 3776

21

Helical; Potential

Domain

1003 – 1169

167

Macro

Domain

1611 – 1875

265

Peptidase C16

Domain

3241 – 3546

306

Peptidase C30

Domain

4981 – 5143

163

RdRp catalytic

Domain

5302 – 5385

84

CV MBD

Domain

5558 – 5739

182

(+)RNA virus helicase ATP-binding

Domain

5740 – 5909

170

(+)RNA virus helicase C-terminal

Zinc finger

1729 – 1766

38

C4-type

Zinc finger

4304 – 4320

17

Zinc finger

4347 – 4360

14

Nucleotide binding

5583 – 5590

8

ATP By similarity

Region

2092 – 2371

280

HD1

Region

2755 – 3162

408

HD2

Region

3564 – 3776

213

HD3

Compositional bias

930 – 1001

72

Glu-rich

Compositional bias

2210 – 2213

4

Poly-Leu

Compositional bias

3766 – 3769

4

Poly-Cys

Sites

Active site

1651

1

For PL-PRO activity By similarity

Active site

1812

1

For PL-PRO activity By similarity

Active site

3281

1

For 3CL-PRO activity By similarity

Active site

3385

1

For 3CL-PRO activity By similarity

Metal binding

4304

1

Zinc

Metal binding

4307

1

Zinc

Metal binding

4313

1

Zinc

Metal binding

4320

1

Zinc

Metal binding

4347

1

Zinc

Metal binding

4350

1

Zinc

Metal binding

4358

1

Zinc

Site

180 – 181

2

Cleavage By similarity

Site

818 – 819

2

Cleavage; by PL-PRO By similarity

Site

2740 – 2741

2

Cleavage; by PL-PRO By similarity

Site

3240 – 3241

2

Cleavage; by 3CL-PRO By similarity

Site

3546 – 3547

2

Cleavage; by 3CL-PRO By similarity

Site

3836 – 3837

2

Cleavage; by 3CL-PRO By similarity

Site

3919 – 3920

2

Cleavage; by 3CL-PRO By similarity

Site

4117 – 4118

2

Cleavage; by 3CL-PRO By similarity

Site

4230 – 4231

2

Cleavage; by 3CL-PRO By similarity

Site

4369 – 4370

2

Cleavage; by 3CL-PRO By similarity

Site

5301 – 5302

2

Cleavage; by 3CL-PRO By similarity

Site

5902 – 5903

2

Cleavage; by 3CL-PRO By similarity

Site

6429 – 6430

2

Cleavage; by 3CL-PRO By similarity

Site

6775 – 6776

2

Cleavage; by 3CL-PRO By similarity

Amino acid modifications

Disulfide bond

4304 ↔ 4307

Disulfide bond

4307 ↔ 4320

Natural variations

Natural variant

82

1

G → C in strain: Isolate GD01.

Natural variant

130

1

G → R in strain: Isolate GD01.

Natural variant

138

1

I → T in strain: Isolate SZ16.

Natural variant

181

1

A → V in strain: Isolate Shanghai LY.

Natural variant

225

1

K → Q in strain: Isolate GD01.

Natural variant

249

1

Y → C in strain: Isolate Shanghai LY.

Natural variant

306

1

V → F in strain: Isolate BJ04.

Natural variant

549

1

A → S in strain: Isolate SZ3.

Natural variant

765

1

A → T in strain: Isolate FRA and Isolate Frankfurt-1.

Natural variant

852

1

K → R in strain: Isolate SZ16.

Natural variant

1004

1

N → H in strain: Isolate BJ03.

Natural variant

1021

1

V → A in strain: Isolate SZ3 and Isolate SZ16.

Natural variant

1023

1

I → T in strain: Isolate Shanghai QXC1.

Natural variant

1121

1

I → T in strain: Isolate GD01, Isolate SZ3 and Isolate SZ16.

Natural variant

1136

1

P → L in strain: Isolate SZ3 and Isolate SZ16.

Natural variant

1257

1

K → E in strain: Isolate Shanghai QXC1.

Natural variant

1319

1

K → R in strain: Isolate GD01.

Natural variant

1329

1

F → S in strain: Isolate GD01.

Natural variant

1361

1

T → A in strain: Isolate Shanghai QXC1.

Natural variant

1385

1

I → V in strain: Isolate Shanghai QXC1.

Natural variant

1538

1

S → T in strain: Isolate GD01.

Natural variant

1563

1

M → K in strain: Isolate BJ02.

Natural variant

1663

1

L → I in strain: Isolate SZ3 and Isolate SZ16.

Natural variant

1762

1

I → L in strain: Isolate BJ03.

Natural variant

1776 – 1777

2

QQ → PP in strain: Isolate BJ03.

Natural variant

1790

1

E → G in strain: Isolate Shanghai QXC1.

Natural variant

1806

1

G → V in strain: Isolate BJ02.

Natural variant

1962

1

L → I in strain: Isolate BJ04.

Natural variant

2116

1

L → F in strain: Isolate GD01, Isolate SZ3 and Isolate SZ16.

Natural variant

2222

1

C → Y in strain: Isolate GD01, Isolate SZ3 and Isolate SZ16.

Natural variant

2269

1

L → S in strain: Isolate SZ3 and Isolate SZ16.

Natural variant

2326

1

V → A in strain: Isolate Shanghai QXC1.

Natural variant

2392 – 2394

3

RNR → CNH in strain: Isolate Shanghai QXC1.

Natural variant

2480

1

L → P in strain: Isolate Shanghai QXC1.

Natural variant

2552

1

A → V in strain: Isolate Urbani and Isolate Taiwan TC2.

Natural variant

2556

1

D → N in strain: Isolate HKU-39849.

Natural variant

2564

1

S → P in strain: Isolate GD01.

Natural variant

2648

1

N → Y in strain: Isolate Shanghai QXC1.

Natural variant

2708

1

S → T in strain: Isolate HKU-39849.

Natural variant

2718

1

R → T in strain: Isolate HKU-39849.

Natural variant

2746

1

C → W in strain: Isolate SZ3 and Isolate SZ16.

Natural variant

2770

1

V → L in strain: Isolate BJ01 and Isolate BJ02.

Natural variant

2944

1

T → I in strain: Isolate SIN2500, Isolate GD01 and Isolate GZ50.

Natural variant

2971

1

V → A in strain: Isolate GD01 and Isolate SZ16.

Natural variant

3020

1

V → A in strain: Isolate Shanghai QXC1.

Natural variant

3047

1

V → A in strain: Isolate CUHK-W1, Isolate GD01, Isolate SZ3, Isolate SZ16, Isolate BJ01, Isolate BJ02, Isolate BJ03 and Isolate Shanghai QXC1.

Natural variant

3072

1

V → A in strain: Isolate CUHK-W1, Isolate SZ3, Isolate SZ16 and Isolate GD01.

Natural variant

3197

1

A → V in strain: Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04 and Isolate Shanghai QXC1.

Natural variant

3429

1

Q → P in strain: Isolate BJ02.

Natural variant

3488

1

D → E in strain: Isolate BJ04.

Natural variant

3717

1

V → A in strain: Isolate Shanghai QXC1.

Natural variant

3818

1

N → T in strain: Isolate BJ04.

Natural variant

3903

1

D → N in strain: Isolate BJ03.

Natural variant

3904

1

I → F in strain: Isolate BJ02.

Natural variant

3911

1

M → V in strain: Isolate Shanghai QXC1.

Natural variant

4001

1

K → Q in strain: Isolate Shanghai LY.

Natural variant

4003

1

T → A in strain: Isolate Shanghai LY.

Natural variant

4085

1

I → H in strain: Isolate ZJ01.

Natural variant

4114

1

V → A in strain: Isolate Shanghai QXC1.

Natural variant

4202

1

V → M in strain: Isolate Shanghai QXC1.

Natural variant

4240

1

N → H in strain: Isolate ZJ01.

Natural variant

4296

1

E → G in strain: Isolate Shanghai QXC1.

Natural variant

4377 – 4378

2

LN → FK in strain: Isolate Shanghai QXC1.

Natural variant

4411

1

V → S in strain: Isolate HKU-39849.

Natural variant

4459

1

V → I in strain: Isolate Shanghai QXC1.

Natural variant

4592

1

V → E in strain: Isolate ZJ01.

Natural variant

4910

1

Q → L in strain: Isolate ZJ01.

Natural variant

5112

1

D → G in strain: Isolate SZ3.

Natural variant

5131

1

A → G in strain: Isolate Taiwan.

Natural variant

5134 – 5135

2

CY → VL in strain: Isolate Taiwan.

Natural variant

5623

1

L → S in strain: Isolate GD01.

Natural variant

5720

1

P → S in strain: Isolate GZ50 and Isolate SIN2500.

Natural variant

5744

1

R → C in strain: Isolate ZJ01.

Natural variant

5767

1

D → 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 variant

6274

1

T → I in strain: Isolate FRA, Isolate Frankfurt-1 Isolate SIN2677, Isolate SIN2679 and Isolate SIN2748.

Natural variant

6474

1

N → S in strain: Isolate Shanghai QXC1.

Natural variant

6700

1

M → I in strain: Isolate BJ03.

Natural variant

6721

1

C → R in strain: Isolate Shanghai QXC1.

Natural variant

6729

1

D → N in strain: Isolate GD01.

Natural variant

6840

1

M → L in strain: Isolate BJ02.

Natural variant

6862

1

Q → P in strain: Isolate BJ04.

Natural variant

6877

1

D → E in strain: Isolate GD01.

Natural variant

6910

1

R → K in strain: Isolate SZ3 and Isolate SZ16.

Natural variant

6937

1

A → P in strain: Isolate BJ03.

Natural variant

6992

1

E → D in strain: Isolate BJ04.

Natural variant

7008

1

N → K in strain: Isolate GD01.

Natural variant

7024

1

K → Q in strain: Isolate BJ04.

Secondary structure

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7073

Helix Strand Turn

Details...

Beta strand

14 – 20

7

Turn

23 – 25

3

Helix

35 – 48

14

Beta strand

51 – 54

4

Helix

61 – 63

3

Beta strand

68 – 72

5

Beta strand

87 – 93

7

Turn

95 – 98

4

Beta strand

99 – 102

4

Beta strand

105 – 109

5

Beta strand

116 – 123

8

Beta strand

827 – 829

3

Turn

831 – 833

3

Beta strand

839 – 841

3

Beta strand

848 – 851

4

Turn

852 – 856

5

Beta strand

860 – 862

3

Turn

869 – 871

3

Helix

872 – 882

11

Helix

888 – 894

7

Helix

898 – 901

4

Beta strand

907 – 909

3

Beta strand

911 – 915

5

Beta strand

918 – 920

3

Beta strand

922 – 926

5

Beta strand

1013 – 1021

9

Helix

1023 – 1030

8

Beta strand

1033 – 1038

6

Helix

1048 – 1056

9

Turn

1057 – 1059

3

Helix

1060 – 1072

13

Beta strand

1080 – 1084

5

Turn

1086 – 1088

3

Beta strand

1090 – 1095

6

Helix

1100 – 1102

3

Helix

1108 – 1114

7

Helix

1115 – 1118

4

Beta strand

1119 – 1124

6

Helix

1130 – 1132

3

Helix

1136 – 1146

11

Beta strand

1149 – 1156

8

Helix

1158 – 1168

11

Beta strand

1345 – 1347

3

Helix

1351 – 1361

11

Beta strand

1364 – 1368

5

Helix

1372 – 1381

10

Beta strand

1389 – 1401

13

Helix

1407 – 1417

11

Beta strand

1421 – 1424

4

Beta strand

1426 – 1428

3

Helix

1429 – 1431

3

Helix

1435 – 1442

8

Beta strand

1449 – 1452

4

Helix

1457 – 1467

11

Helix

1473 – 1484

12

Beta strand

1500 – 1506

7

Beta strand

1509 – 1513

5

Beta strand

1515 – 1518

4

Beta strand

1521 – 1523

3

Helix

1530 – 1537

8

Beta strand

1544 – 1555

12

Beta strand

1557 – 1562

6

Helix

1567 – 1571

5

Beta strand

1572 – 1576

5

Helix

1588 – 1590

3

Beta strand

1594 – 1597

4

Helix

1602 – 1612

11

Helix

1619 – 1630

12

Helix

1651 – 1661

11

Beta strand

1667 – 1669

3

Helix

1670 – 1680

11

Helix

1685 – 1694

10

Helix

1705 – 1713

9

Beta strand

1722 – 1728

7

Beta strand

1730 – 1732

3

Beta strand

1734 – 1740

7

Helix

1742 – 1745

4

Beta strand

1746 – 1749

4

Helix

1753 – 1758

6

Beta strand

1760 – 1763

4

Beta strand

1765 – 1785

21

Beta strand

1790 – 1793

4

Beta strand

1799 – 1807

9

Beta strand

1810 – 1826

17

Beta strand

1829 – 1834

6

Beta strand

1836 – 1846

11

Beta strand

1904 – 1911

8

Helix

1912 – 1921

10

Beta strand

1929 – 1936

8

Beta strand

1942 – 1948

7

Helix

1949 – 1951

3

Helix

1954 – 1956

3

Beta strand

1963 – 1966

4

Beta strand

1969 – 1971

3

Helix

1977 – 1990

14

Helix

3253 – 3256

4

Beta strand

3257 – 3262

6

Beta strand

3265 – 3272

8

Beta strand

3275 – 3279

5

Helix

3280 – 3283

4

Helix

3288 – 3290

3

Helix

3294 – 3298

5

Helix

3303 – 3305

3

Beta strand

3307 – 3310

4

Beta strand

3313 – 3315

3

Beta strand

3317 – 3323

7

Beta strand

3326 – 3333

8

Beta strand

3340 – 3343

4

Beta strand

3351 – 3358

8

Beta strand

3361 – 3369

9

Helix

3379 – 3381

3

Beta strand

3388 – 3393

6

Beta strand

3396 – 3406

11

Turn

3408 – 3410

3

Beta strand

3412 – 3415

4

Beta strand

3421 – 3424

4

Beta strand

3427 – 3430

4

Helix

3441 – 3454

14

Turn

3458 – 3460

3

Helix

3467 – 3476

10

Helix

3484 – 3489

6

Helix

3491 – 3497

7

Helix

3501 – 3514

14

Beta strand

3521 – 3523

3

Beta strand

3524 – 3526

3

Helix

3533 – 3540

8

Beta strand

4120 – 4125

6

Beta strand

4127 – 4131

5

Beta strand

4134 – 4137

4

Beta strand

4145 – 4150

6

Beta strand

4153 – 4155

3

Beta strand

4157 – 4164

8

Beta strand

4170 – 4174

5

Beta strand

4181 – 4186

6

Beta strand

4191 – 4194

4

Beta strand

4201 – 4208

8

Helix

4213 – 4222

10

Helix

4224 – 4227

4

Helix

6431 – 6441

11

Beta strand

6453 – 6456

4

Beta strand

6459 – 6464

6

Beta strand

6467 – 6473

7

Beta strand

6476 – 6478

3

Helix

6480 – 6488

9

Beta strand

6493 – 6495

3

Helix

6498 – 6503

6

Beta strand

6508 – 6513

6

Turn

6517 – 6520

4

Beta strand

6521 – 6530

10

Turn

6532 – 6534

3

Beta strand

6535 – 6539

5

Helix

6543 – 6545

3

Beta strand

6550 – 6553

4

Helix

6559 – 6565

7

Beta strand

6567 – 6575

9

Beta strand

6589 – 6591

3

Beta strand

6594 – 6596

3

Beta strand

6599 – 6601

3

Beta strand

6606 – 6611

6

Beta strand

6614 – 6616

3

Helix

6629 – 6631

3

Helix

6637 – 6644

8

Helix

6647 – 6653

7

Helix

6661 – 6664

4

Beta strand

6670 – 6673

4

Beta strand

6677 – 6679

3

Helix

6680 – 6689

10

Beta strand

6692 – 6698

7

Beta strand

6703 – 6711

9

Turn

6712 – 6714

3

Beta strand

6717 – 6724

8

Helix

6728 – 6736

9

Beta strand

6741 – 6751

11

Beta strand

6754 – 6763

10

Beta strand

6766 – 6772

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform Replicase polyprotein 1ab (pp1ab) [UniParc]. Last modified June 10, 2008. Version 1. Checksum: E6504CAFDC36BC09	FASTA	7,073	790,248
	10 20 30 40 50 60 MESLVLGVNE KTHVQLSLPV LQVRDVLVRG FGDSVEEALS EAREHLKNGT CGLVELEKGV 70 80 90 100 110 120 LPQLEQPYVF IKRSDALSTN HGHKVVELVA EMDGIQYGRS GITLGVLVPH VGETPIAYRN 130 140 150 160 170 180 VLLRKNGNKG AGGHSYGIDL KSYDLGDELG TDPIEDYEQN WNTKHGSGAL RELTRELNGG 190 200 210 220 230 240 AVTRYVDNNF CGPDGYPLDC IKDFLARAGK SMCTLSEQLD YIESKRGVYC CRDHEHEIAW 250 260 270 280 290 300 FTERSDKSYE HQTPFEIKSA KKFDTFKGEC PKFVFPLNSK VKVIQPRVEK KKTEGFMGRI 310 320 330 340 350 360 RSVYPVASPQ ECNNMHLSTL MKCNHCDEVS WQTCDFLKAT CEHCGTENLV IEGPTTCGYL 370 380 390 400 410 420 PTNAVVKMPC PACQDPEIGP EHSVADYHNH SNIETRLRKG GRTRCFGGCV FAYVGCYNKR 430 440 450 460 470 480 AYWVPRASAD IGSGHTGITG DNVETLNEDL LEILSRERVN INIVGDFHLN EEVAIILASF 490 500 510 520 530 540 SASTSAFIDT IKSLDYKSFK TIVESCGNYK VTKGKPVKGA WNIGQQRSVL TPLCGFPSQA 550 560 570 580 590 600 AGVIRSIFAR TLDAANHSIP DLQRAAVTIL DGISEQSLRL VDAMVYTSDL LTNSVIIMAY 610 620 630 640 650 660 VTGGLVQQTS QWLSNLLGTT VEKLRPIFEW IEAKLSAGVE FLKDAWEILK FLITGVFDIV 670 680 690 700 710 720 KGQIQVASDN IKDCVKCFID VVNKALEMCI DQVTIAGAKL RSLNLGEVFI AQSKGLYRQC 730 740 750 760 770 780 IRGKEQLQLL MPLKAPKEVT FLEGDSHDTV LTSEEVVLKN GELEALETPV DSFTNGAIVG 790 800 810 820 830 840 TPVCVNGLML LEIKDKEQYC ALSPGLLATN NVFRLKGGAP IKGVTFGEDT VWEVQGYKNV 850 860 870 880 890 900 RITFELDERV DKVLNEKCSV YTVESGTEVT EFACVVAEAV VKTLQPVSDL LTNMGIDLDE 910 920 930 940 950 960 WSVATFYLFD DAGEENFSSR MYCSFYPPDE EEEDDAECEE EEIDETCEHE YGTEDDYQGL 970 980 990 1000 1010 1020 PLEFGASAET VRVEEEEEED WLDDTTEQSE IEPEPEPTPE EPVNQFTGYL KLTDNVAIKC 1030 1040 1050 1060 1070 1080 VDIVKEAQSA NPMVIVNAAN IHLKHGGGVA GALNKATNGA MQKESDDYIK LNGPLTVGGS 1090 1100 1110 1120 1130 1140 CLLSGHNLAK KCLHVVGPNL NAGEDIQLLK AAYENFNSQD ILLAPLLSAG IFGAKPLQSL 1150 1160 1170 1180 1190 1200 QVCVQTVRTQ VYIAVNDKAL YEQVVMDYLD NLKPRVEAPK QEEPPNTEDS KTEEKSVVQK 1210 1220 1230 1240 1250 1260 PVDVKPKIKA CIDEVTTTLE ETKFLTNKLL LFADINGKLY HDSQNMLRGE DMSFLEKDAP 1270 1280 1290 1300 1310 1320 YMVGDVITSG DITCVVIPSK KAGGTTEMLS RALKKVPVDE YITTYPGQGC AGYTLEEAKT 1330 1340 1350 1360 1370 1380 ALKKCKSAFY VLPSEAPNAK EEILGTVSWN LREMLAHAEE TRKLMPICMD VRAIMATIQR 1390 1400 1410 1420 1430 1440 KYKGIKIQEG IVDYGVRFFF YTSKEPVASI ITKLNSLNEP LVTMPIGYVT HGFNLEEAAR 1450 1460 1470 1480 1490 1500 CMRSLKAPAV VSVSSPDAVT TYNGYLTSSS KTSEEHFVET VSLAGSYRDW SYSGQRTELG 1510 1520 1530 1540 1550 1560 VEFLKRGDKI VYHTLESPVE FHLDGEVLSL DKLKSLLSLR EVKTIKVFTT VDNTNLHTQL 1570 1580 1590 1600 1610 1620 VDMSMTYGQQ FGPTYLDGAD VTKIKPHVNH EGKTFFVLPS DDTLRSEAFE YYHTLDESFL 1630 1640 1650 1660 1670 1680 GRYMSALNHT KKWKFPQVGG LTSIKWADNN CYLSSVLLAL QQLEVKFNAP ALQEAYYRAR 1690 1700 1710 1720 1730 1740 AGDAANFCAL ILAYSNKTVG ELGDVRETMT HLLQHANLES AKRVLNVVCK HCGQKTTTLT 1750 1760 1770 1780 1790 1800 GVEAVMYMGT LSYDNLKTGV SIPCVCGRDA TQYLVQQESS FVMMSAPPAE YKLQQGTFLC 1810 1820 1830 1840 1850 1860 ANEYTGNYQC GHYTHITAKE TLYRIDGAHL TKMSEYKGPV TDVFYKETSY TTTIKPVSYK 1870 1880 1890 1900 1910 1920 LDGVTYTEIE PKLDGYYKKD NAYYTEQPID LVPTQPLPNA SFDNFKLTCS NTKFADDLNQ 1930 1940 1950 1960 1970 1980 MTGFTKPASR ELSVTFFPDL NGDVVAIDYR HYSASFKKGA KLLHKPIVWH INQATTKTTF 1990 2000 2010 2020 2030 2040 KPNTWCLRCL WSTKPVDTSN SFEVLAVEDT QGMDNLACES QQPTSEEVVE NPTIQKEVIE 2050 2060 2070 2080 2090 2100 CDVKTTEVVG NVILKPSDEG VKVTQELGHE DLMAAYVENT SITIKKPNEL SLALGLKTIA 2110 2120 2130 2140 2150 2160 THGIAAINSV PWSKILAYVK PFLGQAAITT SNCAKRLAQR VFNNYMPYVF TLLFQLCTFT 2170 2180 2190 2200 2210 2220 KSTNSRIRAS LPTTIAKNSV KSVAKLCLDA GINYVKSPKF SKLFTIAMWL LLLSICLGSL 2230 2240 2250 2260 2270 2280 ICVTAAFGVL LSNFGAPSYC NGVRELYLNS SNVTTMDFCE GSFPCSICLS GLDSLDSYPA 2290 2300 2310 2320 2330 2340 LETIQVTISS YKLDLTILGL AAEWVLAYML FTKFFYLLGL SAIMQVFFGY FASHFISNSW 2350 2360 2370 2380 2390 2400 LMWFIISIVQ MAPVSAMVRM YIFFASFYYI WKSYVHIMDG CTSSTCMMCY KRNRATRVEC 2410 2420 2430 2440 2450 2460 TTIVNGMKRS FYVYANGGRG FCKTHNWNCL NCDTFCTGST FISDEVARDL SLQFKRPINP 2470 2480 2490 2500 2510 2520 TDQSSYIVDS VAVKNGALHL YFDKAGQKTY ERHPLSHFVN LDNLRANNTK GSLPINVIVF 2530 2540 2550 2560 2570 2580 DGKSKCDESA SKSASVYYSQ LMCQPILLLD QALVSDVGDS TEVSVKMFDA YVDTFSATFS 2590 2600 2610 2620 2630 2640 VPMEKLKALV ATAHSELAKG VALDGVLSTF VSAARQGVVD TDVDTKDVIE CLKLSHHSDL 2650 2660 2670 2680 2690 2700 EVTGDSCNNF MLTYNKVENM TPRDLGACID CNARHINAQV AKSHNVSLIW NVKDYMSLSE 2710 2720 2730 2740 2750 2760 QLRKQIRSAA KKNNIPFRLT CATTRQVVNV ITTKISLKGG KIVSTCFKLM LKATLLCVLA 2770 2780 2790 2800 2810 2820 ALVCYIVMPV HTLSIHDGYT NEIIGYKAIQ DGVTRDIIST DDCFANKHAG FDAWFSQRGG 2830 2840 2850 2860 2870 2880 SYKNDKSCPV VAAIITREIG FIVPGLPGTV LRAINGDFLH FLPRVFSAVG NICYTPSKLI 2890 2900 2910 2920 2930 2940 EYSDFATSAC VLAAECTIFK DAMGKPVPYC YDTNLLEGSI SYSELRPDTR YVLMDGSIIQ 2950 2960 2970 2980 2990 3000 FPNTYLEGSV RVVTTFDAEY CRHGTCERSE VGICLSTSGR WVLNNEHYRA LSGVFCGVDA 3010 3020 3030 3040 3050 3060 MNLIANIFTP LVQPVGALDV SASVVAGGII AILVTCAAYY FMKFRRVFGE YNHVVAANAL 3070 3080 3090 3100 3110 3120 LFLMSFTILC LVPAYSFLPG VYSVFYLYLT FYFTNDVSFL AHLQWFAMFS PIVPFWITAI 3130 3140 3150 3160 3170 3180 YVFCISLKHC HWFFNNYLRK RVMFNGVTFS TFEEAALCTF LLNKEMYLKL RSETLLPLTQ 3190 3200 3210 3220 3230 3240 YNRYLALYNK YKYFSGALDT TSYREAACCH LAKALNDFSN SGADVLYQPP QTSITSAVLQ 3250 3260 3270 3280 3290 3300 SGFRKMAFPS GKVEGCMVQV TCGTTTLNGL WLDDTVYCPR HVICTAEDML NPNYEDLLIR 3310 3320 3330 3340 3350 3360 KSNHSFLVQA GNVQLRVIGH SMQNCLLRLK VDTSNPKTPK YKFVRIQPGQ TFSVLACYNG 3370 3380 3390 3400 3410 3420 SPSGVYQCAM RPNHTIKGSF LNGSCGSVGF NIDYDCVSFC YMHHMELPTG VHAGTDLEGK 3430 3440 3450 3460 3470 3480 FYGPFVDRQT AQAAGTDTTI TLNVLAWLYA AVINGDRWFL NRFTTTLNDF NLVAMKYNYE 3490 3500 3510 3520 3530 3540 PLTQDHVDIL GPLSAQTGIA VLDMCAALKE LLQNGMNGRT ILGSTILEDE FTPFDVVRQC 3550 3560 3570 3580 3590 3600 SGVTFQGKFK KIVKGTHHWM LLTFLTSLLI LVQSTQWSLF FFVYENAFLP FTLGIMAIAA 3610 3620 3630 3640 3650 3660 CAMLLVKHKH AFLCLFLLPS LATVAYFNMV YMPASWVMRI MTWLELADTS LSGYRLKDCV 3670 3680 3690 3700 3710 3720 MYASALVLLI LMTARTVYDD AARRVWTLMN VITLVYKVYY GNALDQAISM WALVISVTSN 3730 3740 3750 3760 3770 3780 YSGVVTTIMF LARAIVFVCV EYYPLLFITG NTLQCIMLVY CFLGYCCCCY FGLFCLLNRY 3790 3800 3810 3820 3830 3840 FRLTLGVYDY LVSTQEFRYM NSQGLLPPKS SIDAFKLNIK LLGIGGKPCI KVATVQSKMS 3850 3860 3870 3880 3890 3900 DVKCTSVVLL SVLQQLRVES SSKLWAQCVQ LHNDILLAKD TTEAFEKMVS LLSVLLSMQG 3910 3920 3930 3940 3950 3960 AVDINRLCEE MLDNRATLQA IASEFSSLPS YAAYATAQEA YEQAVANGDS EVVLKKLKKS 3970 3980 3990 4000 4010 4020 LNVAKSEFDR DAAMQRKLEK MADQAMTQMY KQARSEDKRA KVTSAMQTML FTMLRKLDND 4030 4040 4050 4060 4070 4080 ALNNIINNAR DGCVPLNIIP LTTAAKLMVV VPDYGTYKNT CDGNTFTYAS ALWEIQQVVD 4090 4100 4110 4120 4130 4140 ADSKIVQLSE INMDNSPNLA WPLIVTALRA NSAVKLQNNE LSPVALRQMS CAAGTTQTAC 4150 4160 4170 4180 4190 4200 TDDNALAYYN NSKGGRFVLA LLSDHQDLKW ARFPKSDGTG TIYTELEPPC RFVTDTPKGP 4210 4220 4230 4240 4250 4260 KVKYLYFIKG LNNLNRGMVL GSLAATVRLQ AGNATEVPAN STVLSFCAFA VDPAKAYKDY 4270 4280 4290 4300 4310 4320 LASGGQPITN CVKMLCTHTG TGQAITVTPE ANMDQESFGG ASCCLYCRCH IDHPNPKGFC 4330 4340 4350 4360 4370 4380 DLKGKYVQIP TTCANDPVGF TLRNTVCTVC GMWKGYGCSC DQLREPLMQS ADASTFLNRV 4390 4400 4410 4420 4430 4440 CGVSAARLTP CGTGTSTDVV YRAFDIYNEK VAGFAKFLKT NCCRFQEKDE EGNLLDSYFV 4450 4460 4470 4480 4490 4500 VKRHTMSNYQ HEETIYNLVK DCPAVAVHDF FKFRVDGDMV PHISRQRLTK YTMADLVYAL 4510 4520 4530 4540 4550 4560 RHFDEGNCDT LKEILVTYNC CDDDYFNKKD WYDFVENPDI LRVYANLGER VRQSLLKTVQ 4570 4580 4590 4600 4610 4620 FCDAMRDAGI VGVLTLDNQD LNGNWYDFGD FVQVAPGCGV PIVDSYYSLL MPILTLTRAL 4630 4640 4650 4660 4670 4680 AAESHMDADL AKPLIKWDLL KYDFTEERLC LFDRYFKYWD QTYHPNCINC LDDRCILHCA 4690 4700 4710 4720 4730 4740 NFNVLFSTVF PPTSFGPLVR KIFVDGVPFV VSTGYHFREL GVVHNQDVNL HSSRLSFKEL 4750 4760 4770 4780 4790 4800 LVYAADPAMH AASGNLLLDK RTTCFSVAAL TNNVAFQTVK PGNFNKDFYD FAVSKGFFKE 4810 4820 4830 4840 4850 4860 GSSVELKHFF FAQDGNAAIS DYDYYRYNLP TMCDIRQLLF VVEVVDKYFD CYDGGCINAN 4870 4880 4890 4900 4910 4920 QVIVNNLDKS AGFPFNKWGK ARLYYDSMSY EDQDALFAYT KRNVIPTITQ MNLKYAISAK 4930 4940 4950 4960 4970 4980 NRARTVAGVS ICSTMTNRQF HQKLLKSIAA TRGATVVIGT SKFYGGWHNM LKTVYSDVET 4990 5000 5010 5020 5030 5040 PHLMGWDYPK CDRAMPNMLR IMASLVLARK HNTCCNLSHR FYRLANECAQ VLSEMVMCGG 5050 5060 5070 5080 5090 5100 SLYVKPGGTS SGDATTAYAN SVFNICQAVT ANVNALLSTD GNKIADKYVR NLQHRLYECL 5110 5120 5130 5140 5150 5160 YRNRDVDHEF VDEFYAYLRK HFSMMILSDD AVVCYNSNYA AQGLVASIKN FKAVLYYQNN 5170 5180 5190 5200 5210 5220 VFMSEAKCWT ETDLTKGPHE FCSQHTMLVK QGDDYVYLPY PDPSRILGAG CFVDDIVKTD 5230 5240 5250 5260 5270 5280 GTLMIERFVS LAIDAYPLTK HPNQEYADVF HLYLQYIRKL HDELTGHMLD MYSVMLTNDN 5290 5300 5310 5320 5330 5340 TSRYWEPEFY EAMYTPHTVL QAVGACVLCN SQTSLRCGAC IRRPFLCCKC CYDHVISTSH 5350 5360 5370 5380 5390 5400 KLVLSVNPYV CNAPGCDVTD VTQLYLGGMS YYCKSHKPPI SFPLCANGQV FGLYKNTCVG 5410 5420 5430 5440 5450 5460 SDNVTDFNAI ATCDWTNAGD YILANTCTER LKLFAAETLK ATEETFKLSY GIATVREVLS 5470 5480 5490 5500 5510 5520 DRELHLSWEV GKPRPPLNRN YVFTGYRVTK NSKVQIGEYT FEKGDYGDAV VYRGTTTYKL 5530 5540 5550 5560 5570 5580 NVGDYFVLTS HTVMPLSAPT LVPQEHYVRI TGLYPTLNIS DEFSSNVANY QKVGMQKYST 5590 5600 5610 5620 5630 5640 LQGPPGTGKS HFAIGLALYY PSARIVYTAC SHAAVDALCE KALKYLPIDK CSRIIPARAR 5650 5660 5670 5680 5690 5700 VECFDKFKVN STLEQYVFCT VNALPETTAD IVVFDEISMA TNYDLSVVNA RLRAKHYVYI 5710 5720 5730 5740 5750 5760 GDPAQLPAPR TLLTKGTLEP EYFNSVCRLM KTIGPDMFLG TCRRCPAEIV DTVSALVYDN 5770 5780 5790 5800 5810 5820 KLKAHKDKSA QCFKMFYKGV ITHDVSSAIN RPQIGVVREF LTRNPAWRKA VFISPYNSQN 5830 5840 5850 5860 5870 5880 AVASKILGLP TQTVDSSQGS EYDYVIFTQT TETAHSCNVN RFNVAITRAK IGILCIMSDR 5890 5900 5910 5920 5930 5940 DLYDKLQFTS LEIPRRNVAT LQAENVTGLF KDCSKIITGL HPTQAPTHLS VDIKFKTEGL 5950 5960 5970 5980 5990 6000 CVDIPGIPKD MTYRRLISMM GFKMNYQVNG YPNMFITREE AIRHVRAWIG FDVEGCHATR 6010 6020 6030 6040 6050 6060 DAVGTNLPLQ LGFSTGVNLV AVPTGYVDTE NNTEFTRVNA KPPPGDQFKH LIPLMYKGLP 6070 6080 6090 6100 6110 6120 WNVVRIKIVQ MLSDTLKGLS DRVVFVLWAH GFELTSMKYF VKIGPERTCC LCDKRATCFS 6130 6140 6150 6160 6170 6180 TSSDTYACWN HSVGFDYVYN PFMIDVQQWG FTGNLQSNHD QHCQVHGNAH VASCDAIMTR 6190 6200 6210 6220 6230 6240 CLAVHECFVK RVDWSVEYPI IGDELRVNSA CRKVQHMVVK SALLADKFPV LHDIGNPKAI 6250 6260 6270 6280 6290 6300 KCVPQAEVEW KFYDAQPCSD KAYKIEELFY SYATHHDKFT DGVCLFWNCN VDRYPANAIV 6310 6320 6330 6340 6350 6360 CRFDTRVLSN LNLPGCDGGS LYVNKHAFHT PAFDKSAFTN LKQLPFFYYS DSPCESHGKQ 6370 6380 6390 6400 6410 6420 VVSDIDYVPL KSATCITRCN LGGAVCRHHA NEYRQYLDAY NMMISAGFSL WIYKQFDTYN 6430 6440 6450 6460 6470 6480 LWNTFTRLQS LENVAYNVVN KGHFDGHAGE APVSIINNAV YTKVDGIDVE IFENKTTLPV 6490 6500 6510 6520 6530 6540 NVAFELWAKR NIKPVPEIKI LNNLGVDIAA NTVIWDYKRE APAHVSTIGV CTMTDIAKKP 6550 6560 6570 6580 6590 6600 TESACSSLTV LFDGRVEGQV DLFRNARNGV LITEGSVKGL TPSKGPAQAS VNGVTLIGES 6610 6620 6630 6640 6650 6660 VKTQFNYFKK VDGIIQQLPE TYFTQSRDLE DFKPRSQMET DFLELAMDEF IQRYKLEGYA 6670 6680 6690 6700 6710 6720 FEHIVYGDFS HGQLGGLHLM IGLAKRSQDS PLKLEDFIPM DSTVKNYFIT DAQTGSSKCV 6730 6740 6750 6760 6770 6780 CSVIDLLLDD FVEIIKSQDL SVISKVVKVT IDYAEISFML WCKDGHVETF YPKLQASQAW 6790 6800 6810 6820 6830 6840 QPGVAMPNLY KMQRMLLEKC DLQNYGENAV IPKGIMMNVA KYTQLCQYLN TLTLAVPYNM 6850 6860 6870 6880 6890 6900 RVIHFGAGSD KGVAPGTAVL RQWLPTGTLL VDSDLNDFVS DADSTLIGDC ATVHTANKWD 6910 6920 6930 6940 6950 6960 LIISDMYDPR TKHVTKENDS KEGFFTYLCG FIKQKLALGG SIAVKITEHS WNADLYKLMG 6970 6980 6990 7000 7010 7020 HFSWWTAFVT NVNASSSEAF LIGANYLGKP KEQIDGYTMH ANYIFWRNTN PIQLSSYSLF 7030 7040 7050 7060 7070 DMSKFPLKLR GTAVMSLKEN QINDMIYSLL EKGRLIIREN NRVVVSSDIL VNN
	Isoform Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [UniParc]. See P0C6U8.		–	–

References

[1]	"Characterization of a novel coronavirus associated with severe acute respiratory syndrome." Rota P.A., Oberste M.S., Monroe S.S., Nix W.A., Campagnoli R., Icenogle J.P., Penaranda S., Bankamp B., Maher K., Chen M.-H., Tong S., Tamin A., Lowe L., Frace M., DeRisi J.L., Chen Q., Wang D., Erdman D.D. , Peret T.C.T., Burns C., Ksiazek T.G., Rollin P.E., Sanchez A., Liffick S., Holloway B., Limor J., McCaustland K., Olsen-Rasmussen M., Fouchier R., Guenther S., Osterhaus A.D.M.E., Drosten C., Pallansch M.A., Anderson L.J., Bellini W.J. Science 300:1394-1399(2003) [PubMed] [Europe PMC] [Abstract] 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]	Erratum 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 361:1832-1832(2003)
[8]	"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.
[9]	Qin E., Zhu Q., Yu M., Fan B., Chang G., Si B., Yang B., Peng W., Jiang T., Liu B., Deng Y., Liu H., Zhang Y., Wang C., Li Y., Gan Y., Li X., Lu F. , Tan G., Yang R., Cao W.S., Wang J., Chen W., Cong L., Deng Y., Dong W., Han Y., Hu W., Lei M., Li C., Li G., Li G., Li H., Li S., Li S., Li W., Li W., Lin W., Liu J., Liu Z., Lu H., Ni P., Qi Q., Sun Y., Tang L., Tong Z., Wang J., Wang X., Wu Q., Xi Y., Xu Z., Yang L., Ye C., Ye J., Zhang B., Zhang F., Zhang J., Zhang X., Zhou J., Yang H. Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04 and Isolate GD01.
[10]	"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.
[11]	"Phylogeny of the SARS coronavirus." Eickmann M., Becker S., Klenk H.-D., Doerr H.W., Stadler K., Censini S., Guidotti S., Masignani V., Scarselli M., Mora M., Donati C., Han J.H., Song H.C., Abrignani S., Covacci A., Rappuoli R. Science 302:1504-1505(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate FRA.
[12]	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.
[13]	"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.
[14]	"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.
[15]	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.
[16]	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.
[17]	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.
[18]	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.
[19]	Wang Z., Cheng S., Zhang Y. Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate ZJ01.
[20]	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.
[21]	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.
[22]	"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.
[23]	"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.
[24]	"Mechanisms and enzymes involved in SARS coronavirus genome expression." Thiel V., Ivanov K.A., Putics A., Hertzig T., Schelle B., Bayer S., Weissbrich B., Snijder E.J., Rabenau H., Doerr H.W., Gorbalenya A.E., Ziebuhr J. J. Gen. Virol. 84:2305-2315(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"A second, non-canonical RNA-dependent RNA polymerase in SARS coronavirus." Imbert I., Guillemot J.-C., Bourhis J.-M., Bussetta C., Coutard B., Egloff M.-P., Ferron F., Gorbalenya A.E., Canard B. EMBO J. 25:4933-4942(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF NSP8.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"The nsp9 replicase protein of SARS-coronavirus, structure and functional insights." Sutton G., Fry E., Carter L., Sainsbury S., Walter T., Nettleship J., Berrow N., Owens R., Gilbert R., Davidson A., Siddell S., Poon L.L.M., Diprose J., Alderton D., Walsh M., Grimes J.M., Stuart D.I. Structure 12:341-353(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4107-4230.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	"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.
[42]	"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.
[43]	"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.
[44]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

RefSeq

NP_828849.2. NC_004718.3.

3D structure databases

PDBe
RCSB PDB
PDBj

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	4240-4378	[»]

ProteinModelPortal

P0C6X7.

SMR

P0C6X7. Positions 13-127, 819-930, 1002-1176, 1331-1469, 1541-1854, 3241-3546, 3837-3910, 3921-4111, 4118-4230, 4240-4362, 6430-6773.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1487760.

Proteomic databases

PRIDE

P0C6X7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR027351. (+)RNA_virus_helicase_core_dom.
IPR002589. A1pp.
IPR009461. Coronavirus_NSP13.
IPR027352. CV_MBD_dom.
IPR021590. NSP1.
IPR009466. NSP11.
IPR024375. Nsp3_coronavir.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
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.
IPR024358. SARS-CoV_Nsp3_N.
IPR022733. SARS_polyprot_cleavage.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view]

Pfam

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.
PF11633. Nsp3. 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.
PF01443. Viral_helicase1. 1 hit.
PF08715. Viral_protease. 1 hit.
[Graphical view]

SUPFAM

SSF101816. Nsp9. 1 hit.
SSF50494. Pept_Ser_Cys. 1 hit.
SSF144246. SSF144246. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

BindingDB

P0C6X7.

ChEMBL

CHEMBL5118.

EvolutionaryTrace

P0C6X7.

Entry information

Entry name

R1AB_CVHSA

Accession

Primary (citable) accession number: P0C6X7
Secondary accession number(s): P59641 , Q6WGN0, Q7T697, Q808C0, Q80BV7, Q80BV8, Q80E51

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	June 10, 2008
Last modified:	May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program