P0C6V2 (R1A_CVPPU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Replicase polyprotein 1a
Short name=pp1a

Alternative name(s):
ORF1a polyprotein

Cleaved into the following 11 chains:

1. Non-structural protein 1
   Short name=nsp1
   Alternative name(s):
   p9
2. Non-structural protein 2
   Short name=nsp2
   Alternative name(s):
   p87
3. Non-structural protein 3
   Short name=nsp3
   EC=3.4.19.12
   EC=3.4.22.-
   Alternative name(s):
   PL1-PRO/PL2-PRO
   PLP1/PLP2
   Papain-like proteinases 1/2
   p195
4. Non-structural protein 4
   Short name=nsp4
   Alternative name(s):
   Peptide HD2
5. 3C-like proteinase
   Short name=3CL-PRO
   Short name=3CLp
   EC=3.4.22.-
   Alternative name(s):
   M-PRO
   nsp5
   p34
6. Non-structural protein 6
   Short name=nsp6
7. Non-structural protein 7
   Short name=nsp7
   Alternative name(s):
   p5
8. Non-structural protein 8
   Short name=nsp8
   Alternative name(s):
   p23
9. Non-structural protein 9
   Short name=nsp9
   Alternative name(s):
   p12
10. Non-structural protein 10
    Short name=nsp10
    Alternative name(s):
    Growth factor-like peptide
    Short name=GFL
    p14
11. Non-structural protein 11
    Short name=nsp11

Gene names

ORF Names:

1a

Organism

Porcine transmissible gastroenteritis coronavirus (strain Purdue) (TGEV) [Complete proteome]

Taxonomic identifier

11151 [NCBI]

Taxonomic lineage

Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Nidovirales › Coronaviridae › Coronavirinae › Alphacoronavirus › Alphacoronavirus 1 › Transmissible gastroenteritis virus

Virus host

Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length	4017 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 papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 By similarity. 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-|-[SAGC]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter By similarity. Nsp9 is a ssRNA-binding protein By similarity.
Catalytic activity	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).
Subunit structure	3CL-PRO exists as monomer and homodimer. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer By similarity.
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.
Domain	The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane.
Post-translational modification	Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO is autocatalytically processed.
Sequence similarities	Belongs to the coronaviruses polyprotein 1ab family. Contains 1 Macro domain. Contains 2 peptidase C16 domains. Contains 1 peptidase C30 domain.

Ontologies

Keywords
Biological process	Activation of host autophagy by virus Host-virus interaction Inhibition of host IFN-mediated response initiation by virus Inhibition of host IRF3 by virus Inhibition of host innate immune response by virus Modulation of host ubiquitin pathway by viral deubiquitinase Modulation of host ubiquitin pathway by virus Ubl conjugation pathway Viral immunoevasion
Cellular component	Host cytoplasm Host membrane Membrane
Coding sequence diversity	Ribosomal frameshifting
Domain	Repeat Transmembrane Transmembrane helix Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
Molecular function	Hydrolase Protease Thiol protease
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	induction by virus of host autophagy Inferred from electronic annotation. Source: UniProtKB-KW modulation by virus of host protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host IRF3 activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon production Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro viral protein processing Inferred from electronic annotation. Source: InterPro
Cellular_component	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	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: InterPro cysteine-type endopeptidase 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 1a (identifier: P0C6V2-1)

Also known as: pp1a; ORF1a polyprotein;

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

Note: Produced by conventional translation.

Isoform Replicase polyprotein 1ab (identifier: P0C6Y5-1)

Also known as: pp1ab;

The sequence of this isoform can be found in the external entry P0C6Y5.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 4017

4017

Replicase polyprotein 1a

PRO_0000338302

Chain

1 – 110

110

Non-structural protein 1 By similarity

PRO_0000338303

Chain

111 – 879

769

Non-structural protein 2 By similarity

PRO_0000338304

Chain

880 – 2388

1509

Non-structural protein 3 By similarity

PRO_0000338305

Chain

2389 – 2878

490

Non-structural protein 4 By similarity

PRO_0000338306

Chain

2879 – 3180

302

3C-like proteinase

PRO_0000338307

Chain

3181 – 3474

294

Non-structural protein 6 By similarity

PRO_0000338308

Chain

3475 – 3557

83

Non-structural protein 7 By similarity

PRO_0000338309

Chain

3558 – 3752

195

Non-structural protein 8 By similarity

PRO_0000338310

Chain

3753 – 3863

111

Non-structural protein 9

PRO_0000338311

Chain

3864 – 3998

135

Non-structural protein 10 By similarity

PRO_0000338312

Chain

3999 – 4017

19

Non-structural protein 11 Potential

PRO_0000338313

Regions

Transmembrane

1896 – 1916

21

Helical; Potential

Transmembrane

1995 – 2015

21

Helical; Potential

Transmembrane

2033 – 2053

21

Helical; Potential

Transmembrane

2401 – 2421

21

Helical; Potential

Transmembrane

2467 – 2487

21

Helical; Potential

Transmembrane

2497 – 2517

21

Helical; Potential

Transmembrane

2538 – 2558

21

Helical; Potential

Transmembrane

2666 – 2686

21

Helical; Potential

Transmembrane

2695 – 2715

21

Helical; Potential

Transmembrane

2721 – 2741

21

Helical; Potential

Transmembrane

2746 – 2766

21

Helical; Potential

Transmembrane

3187 – 3207

21

Helical; Potential

Transmembrane

3217 – 3237

21

Helical; Potential

Transmembrane

3242 – 3262

21

Helical; Potential

Transmembrane

3280 – 3300

21

Helical; Potential

Transmembrane

3313 – 3333

21

Helical; Potential

Transmembrane

3347 – 3367

21

Helical; Potential

Transmembrane

3371 – 3391

21

Helical; Potential

Transmembrane

3394 – 3414

21

Helical; Potential

Domain

1055 – 1299

245

Peptidase C16 1

Domain

1318 – 1489

172

Macro

Domain

1550 – 1803

254

Peptidase C16 2

Domain

2879 – 3180

302

Peptidase C30

Zinc finger

1164 – 1195

32

C4-type

Zinc finger

3937 – 3953

17

By similarity

Zinc finger

3979 – 3992

14

By similarity

Region

1896 – 2053

158

HD1

Region

2401 – 2766

366

HD2

Region

3187 – 3414

228

HD3

Compositional bias

932 – 1042

111

Glu-rich

Sites

Active site

1093

1

For PL1-PRO activity By similarity

Active site

1244

1

For PL1-PRO activity By similarity

Active site

1588

1

For PL2-PRO activity By similarity

Active site

1741

1

For PL2-PRO activity By similarity

Active site

2919

1

For 3CL-PRO activity By similarity

Active site

3022

1

For 3CL-PRO activity By similarity

Site

110 – 111

2

Cleavage; by PL1-PRO By similarity

Site

879 – 880

2

Cleavage; by PL1-PRO By similarity

Site

2388 – 2389

2

Cleavage; by PL2-PRO By similarity

Site

2878 – 2879

2

Cleavage; by 3CL-PRO By similarity

Site

3180 – 3181

2

Cleavage; by 3CL-PRO By similarity

Site

3474 – 3475

2

Cleavage; by 3CL-PRO By similarity

Site

3557 – 3558

2

Cleavage; by 3CL-PRO By similarity

Site

3752 – 3753

2

Cleavage; by 3CL-PRO By similarity

Site

3863 – 3864

2

Cleavage; by 3CL-PRO By similarity

Site

3998 – 3999

2

Cleavage; by 3CL-PRO By similarity

Natural variations

Natural variant

572

1

F → S in strain: Isolate Purdue-115.

Natural variant

1041

1

E → D in strain: Isolate Purdue-115.

Natural variant

2375

1

P → T in strain: Isolate Purdue-115.

Natural variant

2381

1

E → Q in strain: Isolate Purdue-115.

Secondary structure

1

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4017

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Helix

23 – 36

14

Beta strand

41 – 45

5

Helix

46 – 51

6

Beta strand

59 – 75

17

Beta strand

84 – 90

7

Beta strand

96 – 104

9

Beta strand

1077 – 1080

4

Beta strand

1083 – 1086

4

Helix

1093 – 1102

10

Helix

1111 – 1116

6

Turn

1117 – 1119

3

Helix

1122 – 1132

11

Helix

1142 – 1150

9

Beta strand

1156 – 1164

9

Beta strand

1167 – 1180

14

Beta strand

1183 – 1185

3

Beta strand

1187 – 1191

5

Turn

1193 – 1195

3

Beta strand

1198 – 1217

20

Helix

1223 – 1225

3

Beta strand

1226 – 1228

3

Beta strand

1231 – 1238

8

Turn

1240 – 1242

3

Beta strand

1244 – 1249

6

Turn

1250 – 1253

4

Beta strand

1254 – 1257

4

Beta strand

1260 – 1262

3

Beta strand

1269 – 1280

12

Turn

2889 – 2891

3

Helix

2892 – 2894

3

Beta strand

2895 – 2900

6

Beta strand

2903 – 2910

8

Beta strand

2913 – 2917

5

Helix

2918 – 2921

4

Helix

2931 – 2936

6

Helix

2940 – 2942

3

Beta strand

2943 – 2948

6

Beta strand

2950 – 2952

3

Beta strand

2954 – 2960

7

Beta strand

2963 – 2970

8

Beta strand

2978 – 2980

3

Beta strand

2988 – 2995

8

Beta strand

2998 – 3006

9

Beta strand

3025 – 3030

6

Beta strand

3033 – 3043

11

Beta strand

3049 – 3052

4

Helix

3059 – 3061

3

Beta strand

3064 – 3067

4

Helix

3078 – 3090

13

Helix

3104 – 3111

8

Turn

3112 – 3115

4

Helix

3123 – 3125

3

Helix

3126 – 3132

7

Helix

3136 – 3146

11

Beta strand

3158 – 3160

3

Helix

3167 – 3175

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [UniParc]. Last modified June 10, 2008. Version 1. Checksum: 97ED2B170C4FD248	FASTA	4,017	447,352
	10 20 30 40 50 60 MSSKQFKILV NEDYQVNVPS LPIRDVLQEI KYCYRNGFEG YVFVPEYCRD LVDCDRKDHY 70 80 90 100 110 120 VIGVLGNGVS DLKPVLLTEP SVMLQGFIVR ANCNGVLEDF DLKIARTGRG AIYVDQYMCG 130 140 150 160 170 180 ADGKPVIEGD FKDYFGDEDI IEFEGEEYHC AWTTVRDEKP LNQQTLFTIQ EIQYNLDIPH 190 200 210 220 230 240 KLPNCATRHV APPVKKNSKI VLSEDYKKLY DIFGSPFMGN GDCLSKCFDT LHFIAATLRC 250 260 270 280 290 300 PCGSESSGVG DWTGFKTACC GLSGKVKGVT LGDIKPGDAV VTSMSAGKGV KFFANCVLQY 310 320 330 340 350 360 AGDVEGVSIW KVIKTFTVDE TVCTPGFEGE LNDFIKPESK SLVACSVKRA FITGDIDDAV 370 380 390 400 410 420 HDCIITGKLD LSTNLFGNVG LLFKKTPWFV QKCGALFVDA WKVVEELCGS LTLTYKQIYE 430 440 450 460 470 480 VVASLCTSAF TIVNYKPTFV VPDNRVKDLV DKCVKVLVKA FDVFTQIITI AGIEAKCFVL 490 500 510 520 530 540 GAKYLLFNNA LVKLVSVKIL GKKQKGLECA FFATSLVGAT VNVTPKRTET ATISLNKVDD 550 560 570 580 590 600 VVAPGEGYIV IVGDMAFYKS GEYYFMMSSP NFVLTNNVFK AVKVPSYDIV YDVDNDTKSK 610 620 630 640 650 660 MIAKLGSSFE YDGDIDAAIV KVNELLIEFR QQSLCFRAFK DDKSIFVEAY FKKYKMPACL 670 680 690 700 710 720 AKHIGLWNII KKDSCKRGFL NLFNHLNELE DIKETNIQAI KNILCPDPLL DLDYGAIWYN 730 740 750 760 770 780 CMPGCSDPSV LGSVQLLIGN GVKVVCDGCK GFANQLSKGY NKLCNAARND IEIGGIPFST 790 800 810 820 830 840 FKTPTNTFIE MTDAIYSVIE QGKALSFRDA DVPVVDNGTI STADWSEPIL LEPAEYVKPK 850 860 870 880 890 900 NNGNVIVIAG YTFYKDEDEH FYPYGFGKIV QRMYNKMGGG DKTVSFSEEV DVQEIAPVTR 910 920 930 940 950 960 VKLEFEFDNE IVTGVLERAI GTRYKFTGTT WEEFEESISE ELDAIFDTLA NQGVELEGYF 970 980 990 1000 1010 1020 IYDTCGGFDI KNPDGIMISQ YDINITADEK SEVSASSEEE EVESVEEDPE NEIVEASEGA 1030 1040 1050 1060 1070 1080 EGTSSQEEVE TVEVADITST EEDVDIVEVS AKDDPWAAAV DVQEAEQFNP SLPPFKTTNL 1090 1100 1110 1120 1130 1140 NGKIILKQGD NNCWINACCY QLQAFDFFNN EAWEKFKKGD VMDFVNLCYA ATTLARGHSG 1150 1160 1170 1180 1190 1200 DAEYLLELML NDYSTAKIVL AAKCGCGEKE IVLERAVFKL TPLKESFNYG VCGDCMQVNT 1210 1220 1230 1240 1250 1260 CRFLSVEGSG VFVHDILSKQ TPEAMFVVKP VMHAVYTGTT QNGHYMVDDI EHGYCVDGMG 1270 1280 1290 1300 1310 1320 IKPLKKRCYT STLFINANVM TRAEKPKQEF KVEKVEQQPI VEENKSSIEK EEIQSPKNDD 1330 1340 1350 1360 1370 1380 LILPFYKAGK LSFYQGALDV LINFLEPDVI VNAANGDLKH MGGVARAIDV FTGGKLTERS 1390 1400 1410 1420 1430 1440 KDYLKKNKSI APGNAVFFEN VIEHLSVLNA VGPRNGDSRV EAKLCNVYKA IAKCEGKILT 1450 1460 1470 1480 1490 1500 PLISVGIFNV RLETSLQCLL KTVNDRGLNV FVYTDQERQT IENFFSCSIP VNVTEDNVNH 1510 1520 1530 1540 1550 1560 ERVSVSFDKT YGEQLKGTVV IKDKDVTNQL PSAFDVGQKV IKAIDIDWQA HYGFRDAAAF 1570 1580 1590 1600 1610 1620 SASSHDAYKF EVVTHSNFIV HKQTDNNCWI NAICLALQRL KPQWKFPGVR GLWNEFLERK 1630 1640 1650 1660 1670 1680 TQGFVHMLYH ISGVKKGEPG DAELMLHKLG DLMDNDCEII VTHTTACDKC AKVEKFVGPV 1690 1700 1710 1720 1730 1740 VAAPLAIHGT DETCVHGVSV NVKVTQIKGT VAITSLIGPI IGEVLEATGY ICYSGSNRNG 1750 1760 1770 1780 1790 1800 HYTYYDNRNG LVVDAEKAYH FNRDLLQVTT AIASNFVVKK PQAEERPKNC AFNKVAASPK 1810 1820 1830 1840 1850 1860 IVQEQKLLAI ESGANYALTE FGRYADMFFM AGDKILRLLL EVFKYLLVLF MCLRSTKMPK 1870 1880 1890 1900 1910 1920 VKVKPPLAFK DFGAKVRTLN YMRQLNKPSV WRYAKLVLLL IAIYNFFYLF VSIPVVHKLT 1930 1940 1950 1960 1970 1980 CNGAVQAYKN SSFIKSAVCG NSILCKACLA SYDELADFQH LQVTWDFKSD PLWNRLVQLS 1990 2000 2010 2020 2030 2040 YFAFLAVFGN NYVRCFLMYF VSQYLNLWLS YFGYVEYSWF LHVVNFESIS AEFVIVVIVV 2050 2060 2070 2080 2090 2100 KAVLALKHIV FACSNPSCKT CSRTARQTRI PIQVVVNGSM KTVYVHANGT GKFCKKHNFY 2110 2120 2130 2140 2150 2160 CKNCDSYGFE NTFICDEIVR DLSNSVKQTV YATDRSHQEV TKVECSDGFY RFYVGDEFTS 2170 2180 2190 2200 2210 2220 YDYDVKHKKY SSQEVLKSML LLDDFIVYSP SGSALANVRN ACVYFSQLIG KPIKIVNSDL 2230 2240 2250 2260 2270 2280 LEDLSVDFKG ALFNAKKNVI KNSFNVDVSE CKNLDECYRA CNLNVSFSTF EMAVNNAHRF 2290 2300 2310 2320 2330 2340 GILITDRSFN NFWPSKVKPG SSGVSAMDIG KCMTSDAKIV NAKVLTQRGK SVVWLSQDFA 2350 2360 2370 2380 2390 2400 ALSSTAQKVL VKTFVEEGVN FSLTFNAVGS DDDLPYERFT ESVSPKSGSG FFDVITQLKQ 2410 2420 2430 2440 2450 2460 IVILVFVFIF ICGLCSVYSV ATQSYIESAE GYDYMVIKNG IVQPFDDTIS CVHNTYKGFG 2470 2480 2490 2500 2510 2520 DWFKAKYGFI PTFGKSCPIV VGTVFDLENM RPIPDVPAYV SIVGRSLVFA INAAFGVTNM 2530 2540 2550 2560 2570 2580 CYDHTGNAVS KDSYFDTCVF NTACTTLTGL GGTIVYCAKQ GLVEGAKLYS DLMPDYYYEH 2590 2600 2610 2620 2630 2640 ASGNMVKLPA IIRGLGLRFV KTQATTYCRV GECIDSKAGF CFGGDNWFVY DNEFGNGYIC 2650 2660 2670 2680 2690 2700 GNSVLGFFKN VFKLFNSNMS VVATSGAMLV NIIIACLAIA MCYGVLKFKK IFGDCTFLIV 2710 2720 2730 2740 2750 2760 MIIVTLVVNN VSYFVTQNTF FMIIYAIVYY FITRKLAYPG ILDAGFIIAY INMAPWYVIT 2770 2780 2790 2800 2810 2820 AYILVFLYDS LPSLFKLKVS TNLFEGDKFV GNFESAAMGT FVIDMRSYET IVNSTSIARI 2830 2840 2850 2860 2870 2880 KSYANSFNKY KYYTGSMGEA DYRMACYAHL GKALMDYSVN RTDMLYTPPT VSVNSTLQSG 2890 2900 2910 2920 2930 2940 LRKMAQPSGL VEPCIVRVSY GNNVLNGLWL GDEVICPRHV IASDTTRVIN YENEMSSVRL 2950 2960 2970 2980 2990 3000 HNFSVSKNNV FLGVVSARYK GVNLVLKVNQ VNPNTPEHKF KSIKAGESFN ILACYEGCPG 3010 3020 3030 3040 3050 3060 SVYGVNMRSQ GTIKGSFIAG TCGSVGYVLE NGILYFVYMH HLELGNGSHV GSNFEGEMYG 3070 3080 3090 3100 3110 3120 GYEDQPSMQL EGTNVMSSDN VVAFLYAALI NGERWFVTNT SMSLESYNTW AKTNSFTELS 3130 3140 3150 3160 3170 3180 STDAFSMLAA KTGQSVEKLL DSIVRLNKGF GGRTILSYGS LCDEFTPTEV IRQMYGVNLQ 3190 3200 3210 3220 3230 3240 AGKVKSFFYP IMTAMTILFA FWLEFFMYTP FTWINPTFVS IVLAVTTLIS TVFVSGIKHK 3250 3260 3270 3280 3290 3300 MLFFMSFVLP SVILVTAHNL FWDFSYYESL QSIVENTNTM FLPVDMQGVM LTVFCFIVFV 3310 3320 3330 3340 3350 3360 TYSVRFFTCK QSWFSLAVTT ILVIFNMVKI FGTSDEPWTE NQIAFCFVNM LTMIVSLTTK 3370 3380 3390 3400 3410 3420 DWMVVIASYR IAYYIVVCVM PSAFVSDFGF MKCISIVYMA CGYLFCCYYG ILYWVNRFTC 3430 3440 3450 3460 3470 3480 MTCGVYQFTV SAAELKYMTA NNLSAPKNAY DAMILSAKLI GVGGKRNIKI STVQSKLTEM 3490 3500 3510 3520 3530 3540 KCTNVVLLGL LSKMHVESNS KEWNYCVGLH NEINLCDDPE IVLEKLLALI AFFLSKHNTC 3550 3560 3570 3580 3590 3600 DLSELIESYF ENTTILQSVA SAYAALPSWI ALEKARADLE EAKKNDVSPQ ILKQLTKAFN 3610 3620 3630 3640 3650 3660 IAKSDFEREA SVQKKLDKMA EQAAASMYKE ARAVDRKSKI VSAMHSLLFG MLKKLDMSSV 3670 3680 3690 3700 3710 3720 NTIIDQARNG VLPLSIIPAA SATRLVVITP SLEVFSKIRQ ENNVHYAGAI WTIVEVKDAN 3730 3740 3750 3760 3770 3780 GSHVHLKEVT AANELNLTWP LSITCERTTK LQNNEIMPGK LKERAVRASA TLDGEAFGSG 3790 3800 3810 3820 3830 3840 KALMASESGK SFMYAFIASD NNLKYVKWES NNDIIPIELE APLRFYVDGA NGPEVKYLYF 3850 3860 3870 3880 3890 3900 VKNLNTLRRG AVLGYIGATV RLQAGKPTEH PSNSSLLTLC AFSPDPAKAY VDAVKRGMQP 3910 3920 3930 3940 3950 3960 VNNCVKMLSN GAGNGMAVTN GVEANTQQDS YGGASVCIYC RCHVEHPAID GLCRYKGKFV 3970 3980 3990 4000 4010 QIPTGTQDPI RFCIENEVCV VCGCWLNNGC MCDRTSMQSF TVDQSYLNEC GVLVQLD
	Isoform Replicase polyprotein 1ab (pp1ab) [UniParc]. See P0C6Y5.		–	–

References

[1]	"Complete sequence (20 kilobases) of the polyprotein-encoding gene 1 of transmissible gastroenteritis virus." Eleouet J., Rasschaert D., Lambert P., Levy L., Vende P., Laude H. Virology 206:817-822(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Isolate Purdue-115.
[2]	"Engineering the largest RNA virus genome as an infectious bacterial artificial chromosome." Almazan F., Gonzalez J.M., Penzes Z., Izeta A., Calvo E., Plana-Duran J., Enjuanes L. Proc. Natl. Acad. Sci. U.S.A. 97:5516-5521(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate PUR46-MAD.
[3]	"Conservation of substrate specificities among coronavirus main proteases." Hegyi A., Ziebuhr J. J. Gen. Virol. 83:595-599(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN. Strain: Isolate Purdue-115.
[4]	"Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain." Anand K., Palm G.J., Mesters J.R., Siddell S.G., Ziebuhr J., Hilgenfeld R. EMBO J. 21:3213-3224(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 2879-3180.
[5]	"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: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 2879-3180 COMPLEXED WITH THE SUBSTRATE-ANALOG HEXAPEPTIDYL CMK.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z34093 mRNA. Translation: CAA83979.1.
AJ271965 Genomic RNA. Translation: CAB91144.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LVO	X-ray	1.96	A/B/C/D/E/F	2879-3180	[»]
1P9U	X-ray	2.37	A/B/C/D/E/F	2879-3180	[»]
2AMP	X-ray	2.70	A/B	2879-3180	[»]
3MP2	X-ray	2.50	A	1071-1281	[»]
3ZBD	X-ray	1.49	A/B	1-105	[»]
4F49	X-ray	2.25	A/B/C/D	2879-3181	[»]

ProteinModelPortal

P0C6V2.

SMR

P0C6V2. Positions 2879-3179, 3869-3994.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR002589. A1pp.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view]

Pfam

PF01661. Macro. 1 hit.
PF09401. NSP10. 2 hits.
PF08716. nsp7. 1 hit.
PF08717. nsp8. 1 hit.
PF08710. nsp9. 1 hit.
PF05409. Peptidase_C30. 1 hit.
PF08715. Viral_protease. 2 hits.
[Graphical view]

SMART

SM00506. A1pp. 1 hit.
[Graphical view]

SUPFAM

SSF101816. Nsp9. 1 hit.
SSF50494. Pept_Ser_Cys. 1 hit.
SSF144246. SSF144246. 2 hits.

PROSITE

PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0C6V2.

Entry information

Entry name

R1A_CVPPU

Accession

Primary (citable) accession number: P0C6V2
Secondary accession number(s): Q9IW06

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	June 10, 2008
Last modified:	April 3, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program