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P0C6V6

- R1A_PEDV7

UniProt

P0C6V6 - R1A_PEDV7

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Protein

Replicase polyprotein 1a

Gene

1a

Organism
Porcine epidemic diarrhea virus (strain CV777) (PEDV)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi

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).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-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function (By similarity).PROSITE-ProRule annotation
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-PROBy similarity
Sitei895 – 8962Cleavage; by PL1-PROBy similarity
Active sitei1091 – 10911For PL1-PRO activityPROSITE-ProRule annotation
Active sitei1239 – 12391For PL1-PRO activityPROSITE-ProRule annotation
Active sitei1729 – 17291For PL2-PRO activityPROSITE-ProRule annotation
Active sitei1888 – 18881For PL2-PRO activityPROSITE-ProRule annotation
Sitei2516 – 25172Cleavage; by PL2-PROBy similarity
Sitei2997 – 29982Cleavage; by 3CL-PROBy similarity
Active sitei3038 – 30381For 3CL-PRO activityPROSITE-ProRule annotation
Active sitei3141 – 31411For 3CL-PRO activityPROSITE-ProRule annotation
Sitei3299 – 33002Cleavage; by 3CL-PROBy similarity
Sitei3579 – 35802Cleavage; by 3CL-PROBy similarity
Sitei3662 – 36632Cleavage; by 3CL-PROBy similarity
Sitei3857 – 38582Cleavage; by 3CL-PROBy similarity
Sitei3965 – 39662Cleavage; by 3CL-PROBy similarity
Sitei4100 – 41012Cleavage; by 3CL-PROBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1162 – 119332C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4039 – 405517By similarityAdd
BLAST
Zinc fingeri4081 – 409414By 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 epidemic diarrhea virus (strain CV777) (PEDV)
Taxonomic identifieri229032 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
Virus hostiSus scrofa (Pig) [TaxID: 9823]
ProteomesiUP000008159: 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).By similarity
Chain Non-structural protein 8 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity
Chain Non-structural protein 9 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity
Chain Non-structural protein 10 : Host cytoplasmhost perinuclear region By similarity
Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes (By similarity).By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 41174117Replicase polyprotein 1aPRO_0000338347Add
BLAST
Chaini1 – 110110Non-structural protein 1By similarityPRO_0000338348Add
BLAST
Chaini111 – 895785Non-structural protein 2By similarityPRO_0000338349Add
BLAST
Chaini896 – 25161621Non-structural protein 3By similarityPRO_0000338350Add
BLAST
Chaini2517 – 2997481Non-structural protein 4By similarityPRO_0000338351Add
BLAST
Chaini2998 – 32993023C-like proteinaseBy similarityPRO_0000338352Add
BLAST
Chaini3300 – 3579280Non-structural protein 6By similarityPRO_0000338353Add
BLAST
Chaini3580 – 366283Non-structural protein 7By similarityPRO_0000338354Add
BLAST
Chaini3663 – 3857195Non-structural protein 8By similarityPRO_0000338355Add
BLAST
Chaini3858 – 3965108Non-structural protein 9By similarityPRO_0000338356Add
BLAST
Chaini3966 – 4100135Non-structural protein 10By similarityPRO_0000338357Add
BLAST
Chaini4111 – 41177Non-structural protein 11By similarityPRO_0000338358

Post-translational modificationi

Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed (By similarity).By similarity

Interactioni

Subunit structurei

3CL-PRO exists as monomer and homodimer. The 3 peptides nsp2, nsp3 and nsp4 may form a complex. Nsp9 is a dimer. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp10 forms a dodecamer (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP0C6V6.
SMRiP0C6V6. Positions 2998-3297, 3860-3964, 3972-4096.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1959 – 197921HelicalSequence AnalysisAdd
BLAST
Transmembranei2022 – 204221HelicalSequence AnalysisAdd
BLAST
Transmembranei2105 – 212521HelicalSequence AnalysisAdd
BLAST
Transmembranei2127 – 214721HelicalSequence AnalysisAdd
BLAST
Transmembranei2150 – 217021HelicalSequence AnalysisAdd
BLAST
Transmembranei2528 – 254821HelicalSequence AnalysisAdd
BLAST
Transmembranei2619 – 263921HelicalSequence AnalysisAdd
BLAST
Transmembranei2654 – 267421HelicalSequence AnalysisAdd
BLAST
Transmembranei2754 – 277421HelicalSequence AnalysisAdd
BLAST
Transmembranei2787 – 280721HelicalSequence AnalysisAdd
BLAST
Transmembranei2814 – 283421HelicalSequence AnalysisAdd
BLAST
Transmembranei2863 – 288321HelicalSequence AnalysisAdd
BLAST
Transmembranei3336 – 335621HelicalSequence AnalysisAdd
BLAST
Transmembranei3361 – 338121HelicalSequence AnalysisAdd
BLAST
Transmembranei3399 – 341921HelicalSequence AnalysisAdd
BLAST
Transmembranei3431 – 345121HelicalSequence AnalysisAdd
BLAST
Transmembranei3454 – 347421HelicalSequence AnalysisAdd
BLAST
Transmembranei3476 – 349621HelicalSequence AnalysisAdd
BLAST
Transmembranei3500 – 352021HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1057 – 1296240Peptidase C16 1PROSITE-ProRule annotationAdd
BLAST
Domaini1297 – 1465169MacroPROSITE-ProRule annotationAdd
BLAST
Domaini1691 – 1951261Peptidase C16 2PROSITE-ProRule annotationAdd
BLAST
Domaini2998 – 3299302Peptidase C30PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1959 – 2170212HD1Add
BLAST
Regioni2528 – 2883356HD2Add
BLAST
Regioni3336 – 3520185HD3Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1816 – 1932117Val-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.PROSITE-ProRule annotation
Contains 2 peptidase C16 domains.PROSITE-ProRule annotation
Contains 1 peptidase C30 domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1162 – 119332C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4039 – 405517By similarityAdd
BLAST
Zinc fingeri4081 – 409414By similarityAdd
BLAST

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

InterProiIPR002589. Macro_dom.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR011050. Pectin_lyase_fold/virulence.
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. 1 hit.
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. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF51126. SSF51126. 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: P0C6V6-1) [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.

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        10         20         30         40         50
MASNHVTLAF ANDAEISAFG FCTASEAVSY YSEAAASGFM QCRFVSLDLA
60 70 80 90 100
DTVEGLLPED YVMVVIGTTK LSAYVDTFGS RPRNICGWLL FSNCNYFLEE
110 120 130 140 150
LELTFGRRGG NIVPVDQYMC GADGKPVLQE SEWEYTDFFA DSEDGQLNIA
160 170 180 190 200
GITYVKAWIV ERSDVSYASQ NLTSIKSITY CSTYEHTFLD GTAMKVARTP
210 220 230 240 250
KIKKNVVLSE PLATIYREIG SPFVDNGSDA RSIIRRPVFL HAFVKCKCGS
260 270 280 290 300
YHWTVGDWTS YVSTCCGFKC KPVLVASCSA MPGSVVVTRA GAGTGVKYYN
310 320 330 340 350
NMFLRHVADI DGLAFWRILK VQSKDDLACS GKFLEHHEEG FTDPCYFLND
360 370 380 390 400
SSLATKLKFD ILSGKFSDEV KQAIIAGHVV VGSALVDIVD DALGQPWFIR
410 420 430 440 450
KLGDLASAPW EQLKAVVRGL GLLSDEVVLF GKRLSCATLS IVNGVFEFLA
460 470 480 490 500
DVPEKLAAAV TVFVNFLNEF FESACDCLKV GGKTFNKVGS YVLFDNALVK
510 520 530 540 550
LVKAKARGPR QAGICEVRYT SLVVGSTTKV VSKRVENANV NLVVVDEDVT
560 570 580 590 600
LNTTGRTVVV DGLAFFESDG FYRHLADADV VIEHPVYKSA CELKPVFECD
610 620 630 640 650
PIPDFPLPVA ASVAELCVQT DLLLKNYNTP YKTYSCVVRG DKCCITCTLQ
660 670 680 690 700
FKAPSYVEDA VNFVDLCTKN IGTAGFHEFY ITAHEQQDLQ GFLTTCCTMS
710 720 730 740 750
GFECFMPTIP QCPAVLEEID GGSIWRSFIT GLNTMWDFCK RLKVSFGLDG
760 770 780 790 800
IVVTVARKFK RLGALLAEMY NTYLSTVVEN LVLAGVSFKY YATSVPKIVL
810 820 830 840 850
GGCFHSVKSV FASVFQIPVQ AGIEKFKVFL NCVHPVVPRV IETSFVELEE
860 870 880 890 900
TTFKPPALNG GIAIVDGFAF YYDGTLYYPT DGNSVVPICF KKKGGGDVKF
910 920 930 940 950
SDEVSVKTID PVYKVSLEFE FESETIMAVL NKAVGNRIKV TGGWDDVVEY
960 970 980 990 1000
INVAIEVLKD HVEVPKYYIY DEEGGTDPNL PVMVSQWPLN DDTISQDLLD
1010 1020 1030 1040 1050
VEVVTDAPID SEGDEVDSSA PEKVADVANS EPGDDGLPVA PETNVESEVE
1060 1070 1080 1090 1100
EVAATLSFIK DTPSTVTKDP FAFDFVSYGG LKVLRQSHNN CWVTSTLVQL
1110 1120 1130 1140 1150
QLLGIVDDPA MELFSAGRVG PMVRKCYESQ KAILGSLGDV SACLESLTKD
1160 1170 1180 1190 1200
LHTLKITCSV VCGCGTGERI YEGCAFRMTP TLEPFPYGAC AQCAQVLMHT
1210 1220 1230 1240 1250
FKSIVGTGIF CRDTTALSLD SLVVKPLCAA AFIGKDSGHY VTNFYDAAMA
1260 1270 1280 1290 1300
IDGYGRHQIK YDTLNTICVK DVNWTAPLVP AVDSVVEPVV KPFYSYKNVD
1310 1320 1330 1340 1350
FYQGDFSDLV KLPCDFVVNA ANEKLSHGGG IAKAIDVYTK GMLQKCSNDY
1360 1370 1380 1390 1400
IKAHGPIKVG RGVMLEALGL KVFNVVGPRK GKHAPELLVK AYKSVFANSG
1410 1420 1430 1440 1450
VALTPLISVG IFSVPLEESL SAFLACVGDR HCKCFCYGDK EREAIIKYMD
1460 1470 1480 1490 1500
GLVDAIFKEA LVDTTPVQED VQQVSQKPVL PNFEPFRIEG AHAFYECNPE
1510 1520 1530 1540 1550
GLMSLGADKL VLFTNSNLDF CSVGKCLNDV TSGALLEAIN VFKKSNKTVP
1560 1570 1580 1590 1600
AGNCVTLDCA NMISITMVVL PFDGDANYDK NYARAVVKVS KLKGKLVLAV
1610 1620 1630 1640 1650
DDATLYSKLS HLSVLGFVST PDDVERFYAN KSVVIKVTED TRSVKAVKVE
1660 1670 1680 1690 1700
STATYGQQIG PCLVNDTVVT DNKPVVADVV AKVVPNANWD SHYGFDKAGE
1710 1720 1730 1740 1750
FHMLDHTGFT FPSEVVNGRR VIKTTDNNCW VNVTCLQLQF ARFRFKSAGL
1760 1770 1780 1790 1800
QAMWESYCTG DVAMFVHWLY WLTGVDKGQP SDSENALNML SKYIVPAGSV
1810 1820 1830 1840 1850
TIERVTHDGC CCSKRVVTAP VVNASVLKLG VEDGLCPHGL NYIGKVVVVK
1860 1870 1880 1890 1900
GTTIVVNVGK PVVAPSHLFL KGVSYTTFLD NGNGVVGHYT VFDHGTGMVH
1910 1920 1930 1940 1950
DGDAFVPGDL NVSPVTNVVV SEQTAVVIKD PVKKAELDAT KLLDTMNYAS
1960 1970 1980 1990 2000
ERFFSFGDFM SRNLITVFLY ILSILGLCFR AFRKRDVKVL AGVPQRTGII
2010 2020 2030 2040 2050
LRKSMRYNAK ALGVFFKLKL YWFKVLGKFS LGIYALYALL FMTIRFTPIG
2060 2070 2080 2090 2100
SPVCDDVVAG YANSSFDKNE YCNSVICKVC LYGYQELSDF SHTQVVWQHL
2110 2120 2130 2140 2150
RDPLIGNVMP FFYLAFLAIF GGVYVKAITL YFIFQYLNSL GVFLGLQQSI
2160 2170 2180 2190 2200
WFLQLVPFDV FGDEIVVFFI VTRVLMFIKH VCLGCDKASC VACSKSARLK
2210 2220 2230 2240 2250
RVPVQTIFQG TSKSFYVHAN GGSKFCKKHN FFCLNCDSYG PGCTFINDVI
2260 2270 2280 2290 2300
ATEVGNVVKL NVQPTGPATI LIDKVEFSNG FYYLYSGDTF WKYNFDITDS
2310 2320 2330 2340 2350
KYTCKEALKN CSIITDFIVF NNNGSNVNQV KNACVYFSQM LCKPVKLVDS
2360 2370 2380 2390 2400
ALLASLSVDF GASLHSAFVS VLSNSFGKDL SSCNDMQDCK STLGFDDVPL
2410 2420 2430 2440 2450
DTFNAAVAEA HRYDVLLTDM SFNNFTTSYA KPEEKFPVHD IATCMRVGAK
2460 2470 2480 2490 2500
IVNHNVLVKD SIPVVWLVRD FIALSEETRK YIIRTTKVKG ITFMLTFNDC
2510 2520 2530 2540 2550
RMHTTIPTVC IANKKGAGLP SFSKVKKFFW FLCLFIVAAF FALSFLDFST
2560 2570 2580 2590 2600
QVSSDSDYDF KYIESGQLKT FDNPLSCVHN VFINFDQWHD AKFGFTPVNN
2610 2620 2630 2640 2650
PSCPIVVGVS DEARTVPGIP AGVYLAGKTL VFAINTIFGT SGLCFDASGV
2660 2670 2680 2690 2700
ADKGACIFNS ACTTLSGLGG TAVYCYKNGL VEGAKLYSEL APHSYYKMVD
2710 2720 2730 2740 2750
GNAVSLPEII SRGFGIRTIR TKAMTYCRVG QCVQSAEGVC FGADRFFVYN
2760 2770 2780 2790 2800
AESGSDFVCG TGLFTLLMNV ISVFSKTVPV TVLSGQILFN CIIAFVAVAV
2810 2820 2830 2840 2850
CFLFTKFKRM FGDMSVGVFT VGACTLLNNV SYIVTQNTLG MLGYATLYFL
2860 2870 2880 2890 2900
CTKGVRYMWI WHLGFLISYI LIAPWWVLMV YAFSAIFEFM PNLFKLKVST
2910 2920 2930 2940 2950
QLFEGDKFVG SFENAAAGTF VLDMHAYERL ANSISTEKLR QYASTYNKYK
2960 2970 2980 2990 3000
YYSGSASEAD YRLACFAHLA KAMMDYASNH NDTLYTPPTV SYNSTLQAGL
3010 3020 3030 3040 3050
RKMAQPSGVV EKCIVRVCYG NMALNGLWLG DIVMCPRHVI ASSTTSTIDY
3060 3070 3080 3090 3100
DYALSVLRLH NFSISSGNVF LGVVSATMRG ALLQIKVNQN NVHTPKYTYR
3110 3120 3130 3140 3150
TVRPGESFNI LACYDGAAAG VYGVNMRSNY TIRGSFINGA CGSPGYNINN
3160 3170 3180 3190 3200
GTVEFCYLHQ LELGSGCHVG SDLDGVMYGG YEDQPTLQVE GASSLFTENV
3210 3220 3230 3240 3250
LAFLYAALIN GSTWWLSSSR IAVDRFNEWA VHNGMTTVGN TDCFSILAAK
3260 3270 3280 3290 3300
TGVDVQRLLA SIQSLHKNFG GKQILGHTSL TDEFTTGEVV RQMYGVNLQG
3310 3320 3330 3340 3350
GYVSRACRNV LLVGSFLTFF WSELVSYTKF FWVNPGYVTP MFACLSLLSS
3360 3370 3380 3390 3400
LLMFTLKHKT LFFQVFLIPA LIVTSCINLA FDVEVYNYLA EHFDYHVSLM
3410 3420 3430 3440 3450
GFNAQGLVNI FVCFVVTILH GTYTWRFFNT PASSVTYVVA LLTAAYNYFY
3460 3470 3480 3490 3500
ASDILSCAMT LFASVTGNWF VGAVCYKVAV YMALRFPTFV AIFGDIKSVM
3510 3520 3530 3540 3550
FCYLVLGYFT CCFYGILYWF NRFFKVSVGV YDYTVSAAEF KYMVANGLRA
3560 3570 3580 3590 3600
PTGTLDSLLL SAKLIGIGGE RNIKISSVQS KLTDIKCSNV VLLGCLSSMN
3610 3620 3630 3640 3650
VSANSTEWAY CVDLHNKINL CNDPEKAQEM LLALLAFFLS KNSAFGLDDL
3660 3670 3680 3690 3700
LESYFNDNSM LQSVASTYVG LPSYVIYENA RQQYEDAVNN GSPPQLVKQL
3710 3720 3730 3740 3750
RHAMNVAKSE FDREASTQRK LDRMAEQAAA QMYKEARAVN RKSKVVSAMH
3760 3770 3780 3790 3800
SLLFGMLRRL DMSSVDTILN LAKDGVVPLS VIPAVSATKL NIVTSDIDSY
3810 3820 3830 3840 3850
NRIQREGCVH YAGTIWNIID IKDNDGKVVH VKEVTAQNAE SLSWPLVLGC
3860 3870 3880 3890 3900
ERIVKLQNNE IIPGKLKQRS IKAEGDGIVG EGKALYNNEG GRTFMYAFIS
3910 3920 3930 3940 3950
DKPDLRVVKW EFDGGCNTIE LEPPRKFLVD SPNGAQIKYL YFVRNLNTLR
3960 3970 3980 3990 4000
RGAVLGYIGA TVRLQAGKQT EQAINSSLLT LCAFAVDPAK TYIDAVKSGH
4010 4020 4030 4040 4050
KPVGNCVKML ANGSGNGQAV TNGVEASTNQ DSYGGASVCL YCRAHVEHPS
4060 4070 4080 4090 4100
MDGFCRLKGK YVQVPLGTVD PIRFVLENDV CKVCGCWLSN GCTCDRSIMQ
4110
STDMAYLNEY GALVQLD

Note: Produced by conventional translation.

Length:4,117
Mass (Da):452,818
Last modified:June 10, 2008 - v1
Checksum:i4409589DAF0AA869
GO
Isoform Replicase polyprotein 1ab (identifier: P0C6Y4-1) [UniParc]FASTAAdd to Basket

Also known as: pp1ab

The sequence of this isoform can be found in the external entry P0C6Y4.
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:6,781
Mass (Da):753,158
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF353511 Genomic RNA. No translation available.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF353511 Genomic RNA. No translation available.

3D structure databases

ProteinModelPortali P0C6V6.
SMRi P0C6V6. Positions 2998-3297, 3860-3964, 3972-4096.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR002589. Macro_dom.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR011050. Pectin_lyase_fold/virulence.
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. 1 hit.
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. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF51126. SSF51126. 1 hit.
PROSITEi PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 2 hits.
[Graphical view ]
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Publicationsi

  1. "Further analysis of the genome of porcine epidemic diarrhea virus."
    Bridgen A., Kocherhans R., Tobler K., Carvajal A., Ackermann M.
    Adv. Exp. Med. Biol. 440:781-786(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Completion of the porcine epidemic diarrhoea coronavirus (PEDV) genome sequence."
    Kocherhans R., Bridgen A., Ackermann M., Tobler K.
    Virus Genes 23:137-144(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiR1A_PEDV7
AccessioniPrimary (citable) accession number: P0C6V6
Secondary accession number(s): Q91AV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: October 29, 2014
This is version 43 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

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

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