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P0C6V2

- R1A_CVPPU

UniProt

P0C6V2 - R1A_CVPPU

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Protein

Replicase polyprotein 1a

Gene
1a
Organism
Porcine transmissible gastroenteritis coronavirus (strain Purdue) (TGEV)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei110 – 1112Cleavage; by PL1-PRO By similarity
Sitei879 – 8802Cleavage; by PL1-PRO By similarity
Active sitei1093 – 10931For PL1-PRO activity By similarity
Active sitei1244 – 12441For PL1-PRO activity By similarity
Active sitei1588 – 15881For PL2-PRO activity By similarity
Active sitei1741 – 17411For PL2-PRO activity By similarity
Sitei2388 – 23892Cleavage; by PL2-PRO By similarity
Sitei2878 – 28792Cleavage; by 3CL-PRO By similarity
Active sitei2919 – 29191For 3CL-PRO activity By similarity
Active sitei3022 – 30221For 3CL-PRO activity By similarity
Sitei3180 – 31812Cleavage; by 3CL-PRO By similarity
Sitei3474 – 34752Cleavage; by 3CL-PRO By similarity
Sitei3557 – 35582Cleavage; by 3CL-PRO By similarity
Sitei3752 – 37532Cleavage; by 3CL-PRO By similarity
Sitei3863 – 38642Cleavage; by 3CL-PRO By similarity
Sitei3998 – 39992Cleavage; by 3CL-PRO By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1164 – 119532C4-typeAdd
BLAST
Zinc fingeri3937 – 395317 By similarityAdd
BLAST
Zinc fingeri3979 – 399214 By similarityAdd
BLAST

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: InterPro
  2. omega peptidase activity Source: InterPro
  3. RNA binding Source: UniProtKB-KW
  4. RNA-directed RNA polymerase activity Source: InterPro
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. induction by virus of host autophagy Source: UniProtKB-KW
  2. modulation by virus of host protein ubiquitination Source: UniProtKB-KW
  3. suppression by virus of host IRF3 activity Source: UniProtKB-KW
  4. viral genome replication Source: InterPro
  5. viral protein processing Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Activation of host autophagy by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host IRF3 by virus, Inhibition of host RLR pathway by virus, Modulation of host ubiquitin pathway by viral deubiquitinase, Modulation of host ubiquitin pathway by virus, Ubl conjugation pathway, Viral immunoevasion

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Replicase polyprotein 1a
Short name:
pp1a
Alternative name(s):
ORF1a polyprotein
Cleaved into the following 11 chains:
Non-structural protein 1
Short name:
nsp1
Alternative name(s):
p9
Non-structural protein 2
Short name:
nsp2
Alternative name(s):
p87
Alternative name(s):
PL1-PRO/PL2-PRO
PLP1/PLP2
Papain-like proteinases 1/2
p195
Non-structural protein 4
Short name:
nsp4
Alternative name(s):
Peptide HD2
3C-like proteinase (EC:3.4.22.-)
Short name:
3CL-PRO
Short name:
3CLp
Alternative name(s):
M-PRO
nsp5
p34
Non-structural protein 6
Short name:
nsp6
Non-structural protein 7
Short name:
nsp7
Alternative name(s):
p5
Non-structural protein 8
Short name:
nsp8
Alternative name(s):
p23
Non-structural protein 9
Short name:
nsp9
Alternative name(s):
p12
Non-structural protein 10
Short name:
nsp10
Alternative name(s):
Growth factor-like peptide
Short name:
GFL
p14
Non-structural protein 11
Short name:
nsp11
Gene namesi
ORF Names:1a
OrganismiPorcine transmissible gastroenteritis coronavirus (strain Purdue) (TGEV)
Taxonomic identifieri11151 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
Virus hostiSus scrofa (Pig) [TaxID: 9823]
ProteomesiUP000001440: Genome

Subcellular locationi

Chain Non-structural protein 7 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.
Chain Non-structural protein 8 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.
Chain Non-structural protein 9 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.
Chain Non-structural protein 10 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1896 – 191621Helical; Reviewed predictionAdd
BLAST
Transmembranei1995 – 201521Helical; Reviewed predictionAdd
BLAST
Transmembranei2033 – 205321Helical; Reviewed predictionAdd
BLAST
Transmembranei2401 – 242121Helical; Reviewed predictionAdd
BLAST
Transmembranei2467 – 248721Helical; Reviewed predictionAdd
BLAST
Transmembranei2497 – 251721Helical; Reviewed predictionAdd
BLAST
Transmembranei2538 – 255821Helical; Reviewed predictionAdd
BLAST
Transmembranei2666 – 268621Helical; Reviewed predictionAdd
BLAST
Transmembranei2695 – 271521Helical; Reviewed predictionAdd
BLAST
Transmembranei2721 – 274121Helical; Reviewed predictionAdd
BLAST
Transmembranei2746 – 276621Helical; Reviewed predictionAdd
BLAST
Transmembranei3187 – 320721Helical; Reviewed predictionAdd
BLAST
Transmembranei3217 – 323721Helical; Reviewed predictionAdd
BLAST
Transmembranei3242 – 326221Helical; Reviewed predictionAdd
BLAST
Transmembranei3280 – 330021Helical; Reviewed predictionAdd
BLAST
Transmembranei3313 – 333321Helical; Reviewed predictionAdd
BLAST
Transmembranei3347 – 336721Helical; Reviewed predictionAdd
BLAST
Transmembranei3371 – 339121Helical; Reviewed predictionAdd
BLAST
Transmembranei3394 – 341421Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 40174017Replicase polyprotein 1aPRO_0000338302Add
BLAST
Chaini1 – 110110Non-structural protein 1 By similarityPRO_0000338303Add
BLAST
Chaini111 – 879769Non-structural protein 2 By similarityPRO_0000338304Add
BLAST
Chaini880 – 23881509Non-structural protein 3 By similarityPRO_0000338305Add
BLAST
Chaini2389 – 2878490Non-structural protein 4 By similarityPRO_0000338306Add
BLAST
Chaini2879 – 31803023C-like proteinasePRO_0000338307Add
BLAST
Chaini3181 – 3474294Non-structural protein 6 By similarityPRO_0000338308Add
BLAST
Chaini3475 – 355783Non-structural protein 7 By similarityPRO_0000338309Add
BLAST
Chaini3558 – 3752195Non-structural protein 8 By similarityPRO_0000338310Add
BLAST
Chaini3753 – 3863111Non-structural protein 9PRO_0000338311Add
BLAST
Chaini3864 – 3998135Non-structural protein 10 By similarityPRO_0000338312Add
BLAST
Chaini3999 – 401719Non-structural protein 11 Reviewed predictionPRO_0000338313Add
BLAST

Post-translational modificationi

Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO is autocatalytically processed.

Interactioni

Subunit structurei

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.

Structurei

Secondary structure

1
4017
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107
Helixi23 – 3614
Beta strandi41 – 455
Helixi46 – 516
Beta strandi59 – 7517
Beta strandi84 – 907
Beta strandi96 – 1049
Beta strandi1077 – 10804
Beta strandi1083 – 10864
Helixi1093 – 110210
Helixi1111 – 11166
Turni1117 – 11193
Helixi1122 – 113211
Helixi1142 – 11509
Beta strandi1156 – 11649
Beta strandi1167 – 118014
Beta strandi1183 – 11853
Beta strandi1187 – 11915
Turni1193 – 11953
Beta strandi1198 – 121720
Helixi1223 – 12253
Beta strandi1226 – 12283
Beta strandi1231 – 12388
Turni1240 – 12423
Beta strandi1244 – 12496
Turni1250 – 12534
Beta strandi1254 – 12574
Beta strandi1260 – 12623
Beta strandi1269 – 128012
Turni2889 – 28913
Helixi2892 – 28943
Beta strandi2895 – 29006
Beta strandi2903 – 29108
Beta strandi2913 – 29175
Helixi2918 – 29214
Helixi2931 – 29366
Helixi2940 – 29423
Beta strandi2943 – 29486
Beta strandi2950 – 29523
Beta strandi2954 – 29607
Beta strandi2963 – 29708
Beta strandi2988 – 29958
Beta strandi2998 – 30069
Beta strandi3025 – 30306
Beta strandi3033 – 304311
Beta strandi3049 – 30524
Helixi3059 – 30613
Helixi3078 – 309013
Helixi3104 – 31118
Turni3112 – 31154
Helixi3123 – 31253
Helixi3126 – 31327
Helixi3136 – 314611
Beta strandi3158 – 31603
Helixi3167 – 31759

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LVOX-ray1.96A/B/C/D/E/F2879-3180[»]
1P9UX-ray2.37A/B/C/D/E/F2879-3180[»]
2AMPX-ray2.70A/B2879-3180[»]
3MP2X-ray2.50A1071-1281[»]
3ZBDX-ray1.49A/B1-105[»]
4F49X-ray2.25A/B/C/D2879-3181[»]
ProteinModelPortaliP0C6V2.
SMRiP0C6V2. Positions 2879-3179, 3869-3994.

Miscellaneous databases

EvolutionaryTraceiP0C6V2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1055 – 1299245Peptidase C16 1Add
BLAST
Domaini1318 – 1489172MacroAdd
BLAST
Domaini1550 – 1803254Peptidase C16 2Add
BLAST
Domaini2879 – 3180302Peptidase C30Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1896 – 2053158HD1Add
BLAST
Regioni2401 – 2766366HD2Add
BLAST
Regioni3187 – 3414228HD3Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi932 – 1042111Glu-richAdd
BLAST

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.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1164 – 119532C4-typeAdd
BLAST
Zinc fingeri3937 – 395317 By similarityAdd
BLAST
Zinc fingeri3979 – 399214 By similarityAdd
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

InterProiIPR002589. Macro_dom.
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]
PfamiPF01661. 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]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
SUPFAMiSSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 2 hits.
SSF50494. SSF50494. 1 hit.
PROSITEiPS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

Isoform Replicase polyprotein 1a (identifier: P0C6V2-1) [UniParc]FASTAAdd to Basket

Also known as: pp1a, ORF1a polyprotein

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

« Hide

MSSKQFKILV NEDYQVNVPS LPIRDVLQEI KYCYRNGFEG YVFVPEYCRD     50
LVDCDRKDHY VIGVLGNGVS DLKPVLLTEP SVMLQGFIVR ANCNGVLEDF 100
DLKIARTGRG AIYVDQYMCG ADGKPVIEGD FKDYFGDEDI IEFEGEEYHC 150
AWTTVRDEKP LNQQTLFTIQ EIQYNLDIPH KLPNCATRHV APPVKKNSKI 200
VLSEDYKKLY DIFGSPFMGN GDCLSKCFDT LHFIAATLRC PCGSESSGVG 250
DWTGFKTACC GLSGKVKGVT LGDIKPGDAV VTSMSAGKGV KFFANCVLQY 300
AGDVEGVSIW KVIKTFTVDE TVCTPGFEGE LNDFIKPESK SLVACSVKRA 350
FITGDIDDAV HDCIITGKLD LSTNLFGNVG LLFKKTPWFV QKCGALFVDA 400
WKVVEELCGS LTLTYKQIYE VVASLCTSAF TIVNYKPTFV VPDNRVKDLV 450
DKCVKVLVKA FDVFTQIITI AGIEAKCFVL GAKYLLFNNA LVKLVSVKIL 500
GKKQKGLECA FFATSLVGAT VNVTPKRTET ATISLNKVDD VVAPGEGYIV 550
IVGDMAFYKS GEYYFMMSSP NFVLTNNVFK AVKVPSYDIV YDVDNDTKSK 600
MIAKLGSSFE YDGDIDAAIV KVNELLIEFR QQSLCFRAFK DDKSIFVEAY 650
FKKYKMPACL AKHIGLWNII KKDSCKRGFL NLFNHLNELE DIKETNIQAI 700
KNILCPDPLL DLDYGAIWYN CMPGCSDPSV LGSVQLLIGN GVKVVCDGCK 750
GFANQLSKGY NKLCNAARND IEIGGIPFST FKTPTNTFIE MTDAIYSVIE 800
QGKALSFRDA DVPVVDNGTI STADWSEPIL LEPAEYVKPK NNGNVIVIAG 850
YTFYKDEDEH FYPYGFGKIV QRMYNKMGGG DKTVSFSEEV DVQEIAPVTR 900
VKLEFEFDNE IVTGVLERAI GTRYKFTGTT WEEFEESISE ELDAIFDTLA 950
NQGVELEGYF IYDTCGGFDI KNPDGIMISQ YDINITADEK SEVSASSEEE 1000
EVESVEEDPE NEIVEASEGA EGTSSQEEVE TVEVADITST EEDVDIVEVS 1050
AKDDPWAAAV DVQEAEQFNP SLPPFKTTNL NGKIILKQGD NNCWINACCY 1100
QLQAFDFFNN EAWEKFKKGD VMDFVNLCYA ATTLARGHSG DAEYLLELML 1150
NDYSTAKIVL AAKCGCGEKE IVLERAVFKL TPLKESFNYG VCGDCMQVNT 1200
CRFLSVEGSG VFVHDILSKQ TPEAMFVVKP VMHAVYTGTT QNGHYMVDDI 1250
EHGYCVDGMG IKPLKKRCYT STLFINANVM TRAEKPKQEF KVEKVEQQPI 1300
VEENKSSIEK EEIQSPKNDD LILPFYKAGK LSFYQGALDV LINFLEPDVI 1350
VNAANGDLKH MGGVARAIDV FTGGKLTERS KDYLKKNKSI APGNAVFFEN 1400
VIEHLSVLNA VGPRNGDSRV EAKLCNVYKA IAKCEGKILT PLISVGIFNV 1450
RLETSLQCLL KTVNDRGLNV FVYTDQERQT IENFFSCSIP VNVTEDNVNH 1500
ERVSVSFDKT YGEQLKGTVV IKDKDVTNQL PSAFDVGQKV IKAIDIDWQA 1550
HYGFRDAAAF SASSHDAYKF EVVTHSNFIV HKQTDNNCWI NAICLALQRL 1600
KPQWKFPGVR GLWNEFLERK TQGFVHMLYH ISGVKKGEPG DAELMLHKLG 1650
DLMDNDCEII VTHTTACDKC AKVEKFVGPV VAAPLAIHGT DETCVHGVSV 1700
NVKVTQIKGT VAITSLIGPI IGEVLEATGY ICYSGSNRNG HYTYYDNRNG 1750
LVVDAEKAYH FNRDLLQVTT AIASNFVVKK PQAEERPKNC AFNKVAASPK 1800
IVQEQKLLAI ESGANYALTE FGRYADMFFM AGDKILRLLL EVFKYLLVLF 1850
MCLRSTKMPK VKVKPPLAFK DFGAKVRTLN YMRQLNKPSV WRYAKLVLLL 1900
IAIYNFFYLF VSIPVVHKLT CNGAVQAYKN SSFIKSAVCG NSILCKACLA 1950
SYDELADFQH LQVTWDFKSD PLWNRLVQLS YFAFLAVFGN NYVRCFLMYF 2000
VSQYLNLWLS YFGYVEYSWF LHVVNFESIS AEFVIVVIVV KAVLALKHIV 2050
FACSNPSCKT CSRTARQTRI PIQVVVNGSM KTVYVHANGT GKFCKKHNFY 2100
CKNCDSYGFE NTFICDEIVR DLSNSVKQTV YATDRSHQEV TKVECSDGFY 2150
RFYVGDEFTS YDYDVKHKKY SSQEVLKSML LLDDFIVYSP SGSALANVRN 2200
ACVYFSQLIG KPIKIVNSDL LEDLSVDFKG ALFNAKKNVI KNSFNVDVSE 2250
CKNLDECYRA CNLNVSFSTF EMAVNNAHRF GILITDRSFN NFWPSKVKPG 2300
SSGVSAMDIG KCMTSDAKIV NAKVLTQRGK SVVWLSQDFA ALSSTAQKVL 2350
VKTFVEEGVN FSLTFNAVGS DDDLPYERFT ESVSPKSGSG FFDVITQLKQ 2400
IVILVFVFIF ICGLCSVYSV ATQSYIESAE GYDYMVIKNG IVQPFDDTIS 2450
CVHNTYKGFG DWFKAKYGFI PTFGKSCPIV VGTVFDLENM RPIPDVPAYV 2500
SIVGRSLVFA INAAFGVTNM CYDHTGNAVS KDSYFDTCVF NTACTTLTGL 2550
GGTIVYCAKQ GLVEGAKLYS DLMPDYYYEH ASGNMVKLPA IIRGLGLRFV 2600
KTQATTYCRV GECIDSKAGF CFGGDNWFVY DNEFGNGYIC GNSVLGFFKN 2650
VFKLFNSNMS VVATSGAMLV NIIIACLAIA MCYGVLKFKK IFGDCTFLIV 2700
MIIVTLVVNN VSYFVTQNTF FMIIYAIVYY FITRKLAYPG ILDAGFIIAY 2750
INMAPWYVIT AYILVFLYDS LPSLFKLKVS TNLFEGDKFV GNFESAAMGT 2800
FVIDMRSYET IVNSTSIARI KSYANSFNKY KYYTGSMGEA DYRMACYAHL 2850
GKALMDYSVN RTDMLYTPPT VSVNSTLQSG LRKMAQPSGL VEPCIVRVSY 2900
GNNVLNGLWL GDEVICPRHV IASDTTRVIN YENEMSSVRL HNFSVSKNNV 2950
FLGVVSARYK GVNLVLKVNQ VNPNTPEHKF KSIKAGESFN ILACYEGCPG 3000
SVYGVNMRSQ GTIKGSFIAG TCGSVGYVLE NGILYFVYMH HLELGNGSHV 3050
GSNFEGEMYG GYEDQPSMQL EGTNVMSSDN VVAFLYAALI NGERWFVTNT 3100
SMSLESYNTW AKTNSFTELS STDAFSMLAA KTGQSVEKLL DSIVRLNKGF 3150
GGRTILSYGS LCDEFTPTEV IRQMYGVNLQ AGKVKSFFYP IMTAMTILFA 3200
FWLEFFMYTP FTWINPTFVS IVLAVTTLIS TVFVSGIKHK MLFFMSFVLP 3250
SVILVTAHNL FWDFSYYESL QSIVENTNTM FLPVDMQGVM LTVFCFIVFV 3300
TYSVRFFTCK QSWFSLAVTT ILVIFNMVKI FGTSDEPWTE NQIAFCFVNM 3350
LTMIVSLTTK DWMVVIASYR IAYYIVVCVM PSAFVSDFGF MKCISIVYMA 3400
CGYLFCCYYG ILYWVNRFTC MTCGVYQFTV SAAELKYMTA NNLSAPKNAY 3450
DAMILSAKLI GVGGKRNIKI STVQSKLTEM KCTNVVLLGL LSKMHVESNS 3500
KEWNYCVGLH NEINLCDDPE IVLEKLLALI AFFLSKHNTC DLSELIESYF 3550
ENTTILQSVA SAYAALPSWI ALEKARADLE EAKKNDVSPQ ILKQLTKAFN 3600
IAKSDFEREA SVQKKLDKMA EQAAASMYKE ARAVDRKSKI VSAMHSLLFG 3650
MLKKLDMSSV NTIIDQARNG VLPLSIIPAA SATRLVVITP SLEVFSKIRQ 3700
ENNVHYAGAI WTIVEVKDAN GSHVHLKEVT AANELNLTWP LSITCERTTK 3750
LQNNEIMPGK LKERAVRASA TLDGEAFGSG KALMASESGK SFMYAFIASD 3800
NNLKYVKWES NNDIIPIELE APLRFYVDGA NGPEVKYLYF VKNLNTLRRG 3850
AVLGYIGATV RLQAGKPTEH PSNSSLLTLC AFSPDPAKAY VDAVKRGMQP 3900
VNNCVKMLSN GAGNGMAVTN GVEANTQQDS YGGASVCIYC RCHVEHPAID 3950
GLCRYKGKFV QIPTGTQDPI RFCIENEVCV VCGCWLNNGC MCDRTSMQSF 4000
TVDQSYLNEC GVLVQLD 4017

Note: Produced by conventional translation.

Length:4,017
Mass (Da):447,352
Last modified:June 10, 2008 - v1
Checksum:i97ED2B170C4FD248
GO
Isoform Replicase polyprotein 1ab (identifier: P0C6Y5-1) [UniParc]FASTAAdd to Basket

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.

Length:6,684
Mass (Da):748,912
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti572 – 5721F → S in strain: Isolate Purdue-115.
Natural varianti1041 – 10411E → D in strain: Isolate Purdue-115.
Natural varianti2375 – 23751P → T in strain: Isolate Purdue-115.
Natural varianti2381 – 23811E → Q in strain: Isolate Purdue-115.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z34093 mRNA. Translation: CAA83979.1.
AJ271965 Genomic RNA. Translation: CAB91144.1.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z34093 mRNA. Translation: CAA83979.1 .
AJ271965 Genomic RNA. Translation: CAB91144.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P0C6V2.
SMRi P0C6V2. Positions 2879-3179, 3869-3994.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P0C6V2.

Family and domain databases

InterProi IPR002589. Macro_dom.
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 ]
Pfami 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 ]
SMARTi SM00506. A1pp. 1 hit.
[Graphical view ]
SUPFAMi SSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 2 hits.
SSF50494. SSF50494. 1 hit.
PROSITEi PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiR1A_CVPPU
AccessioniPrimary (citable) accession number: P0C6V2
Secondary accession number(s): Q9IW06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 48 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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